Proteins that bind to particles and cells to increase susceptibility to PHAGOCYTOSIS, especially ANTIBODIES bound to EPITOPES that attach to FC RECEPTORS. COMPLEMENT C3B may also participate.
The engulfing and degradation of microorganisms; other cells that are dead, dying, or pathogenic; and foreign particles by phagocytic cells (PHAGOCYTES).
Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes.
A birth defect in which the URINARY BLADDER is malformed and exposed, inside out, and protruded through the ABDOMINAL WALL. It is caused by closure defects involving the top front surface of the bladder, as well as the lower abdominal wall; SKIN; MUSCLES; and the pubic bone.
Serum glycoproteins participating in the host defense mechanism of COMPLEMENT ACTIVATION that creates the COMPLEMENT MEMBRANE ATTACK COMPLEX. Included are glycoproteins in the various pathways of complement activation (CLASSICAL COMPLEMENT PATHWAY; ALTERNATIVE COMPLEMENT PATHWAY; and LECTIN COMPLEMENT PATHWAY).
The natural bactericidal property of BLOOD due to normally occurring antibacterial substances such as beta lysin, leukin, etc. This activity needs to be distinguished from the bactericidal activity contained in a patient's serum as a result of antimicrobial therapy, which is measured by a SERUM BACTERICIDAL TEST.
Any blood or formed element especially in invertebrates.
A mitosporic Tremellales fungal genus whose species usually have a capsule and do not form pseudomycellium. Teleomorphs include Filobasidiella and Fidobasidium.
Techniques used for determining the values of photometric parameters of light resulting from LUMINESCENCE.
A class of C-type lectins that target the carbohydrate structures found on invading pathogens. Binding of collectins to microorganisms results in their agglutination and enhanced clearance. Collectins form trimers that may assemble into larger oligomers. Each collectin polypeptide chain consists of four regions: a relatively short N-terminal region, a collagen-like region, an alpha-helical coiled-coil region, and carbohydrate-binding region.
ENDOCARDIUM infection that is usually caused by STREPTOCOCCUS. Subacute infective endocarditis evolves over weeks and months with modest toxicity and rare metastatic infection.
The larger fragment generated from the cleavage of COMPLEMENT C3 by C3 CONVERTASE. It is a constituent of the ALTERNATIVE PATHWAY C3 CONVERTASE (C3bBb), and COMPLEMENT C5 CONVERTASES in both the classical (C4b2a3b) and the alternative (C3bBb3b) pathway. C3b participates in IMMUNE ADHERENCE REACTION and enhances PHAGOCYTOSIS. It can be inactivated (iC3b) or cleaved by various proteases to yield fragments such as COMPLEMENT C3C; COMPLEMENT C3D; C3e; C3f; and C3g.
Complement activation initiated by the interaction of microbial ANTIGENS with COMPLEMENT C3B. When COMPLEMENT FACTOR B binds to the membrane-bound C3b, COMPLEMENT FACTOR D cleaves it to form alternative C3 CONVERTASE (C3BBB) which, stabilized by COMPLEMENT FACTOR P, is able to cleave multiple COMPLEMENT C3 to form alternative C5 CONVERTASE (C3BBB3B) leading to cleavage of COMPLEMENT C5 and the assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.
A family of blood flukes of the class Trematoda which is found in animals and man. It Includes the genera Heterobilharzia, Schistosomatium, Schistosoma, Ornithobilharzia, Bilharziella, Trichobilharzia, Pseudobilharzia, and Austrobilharzia.
The sequential activation of serum COMPLEMENT PROTEINS to create the COMPLEMENT MEMBRANE ATTACK COMPLEX. Factors initiating complement activation include ANTIGEN-ANTIBODY COMPLEXES, microbial ANTIGENS, or cell surface POLYSACCHARIDES.
Zymosan is a polysaccharide derived from the cell walls of Saccharomyces cerevisiae, commonly used in research as an immunostimulant to induce inflammation and study phagocytosis, complement activation, and oxidative burst in neutrophils and macrophages.
A large increase in oxygen uptake by neutrophils and most types of tissue macrophages through activation of an NADPH-cytochrome b-dependent oxidase that reduces oxygen to a superoxide. Individuals with an inherited defect in which the oxidase that reduces oxygen to superoxide is decreased or absent (GRANULOMATOUS DISEASE, CHRONIC) often die as a result of recurrent bacterial infections.
Cells that can carry out the process of PHAGOCYTOSIS.
A specific mannose-binding member of the collectin family of lectins. It binds to carbohydrate groups on invading pathogens and plays a key role in the MANNOSE-BINDING LECTIN COMPLEMENT PATHWAY.
The relatively long-lived phagocytic cell of mammalian tissues that are derived from blood MONOCYTES. Main types are PERITONEAL MACROPHAGES; ALVEOLAR MACROPHAGES; HISTIOCYTES; KUPFFER CELLS of the liver; and OSTEOCLASTS. They may further differentiate within chronic inflammatory lesions to EPITHELIOID CELLS or may fuse to form FOREIGN BODY GIANT CELLS or LANGHANS GIANT CELLS. (from The Dictionary of Cell Biology, Lackie and Dow, 3rd ed.)
Complement activation initiated by the binding of COMPLEMENT C1 to ANTIGEN-ANTIBODY COMPLEXES at the COMPLEMENT C1Q subunit. This leads to the sequential activation of COMPLEMENT C1R and COMPLEMENT C1S subunits. Activated C1s cleaves COMPLEMENT C4 and COMPLEMENT C2 forming the membrane-bound classical C3 CONVERTASE (C4B2A) and the subsequent C5 CONVERTASE (C4B2A3B) leading to cleavage of COMPLEMENT C5 and the assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.
A species of the fungus CRYPTOCOCCUS. Its teleomorph is Filobasidiella neoformans.
Immunoglobulins produced in a response to BACTERIAL ANTIGENS.
A subcomponent of complement C1, composed of six copies of three polypeptide chains (A, B, and C), each encoded by a separate gene (C1QA; C1QB; C1QC). This complex is arranged in nine subunits (six disulfide-linked dimers of A and B, and three disulfide-linked homodimers of C). C1q has binding sites for antibodies (the heavy chain of IMMUNOGLOBULIN G or IMMUNOGLOBULIN M). The interaction of C1q and immunoglobulin activates the two proenzymes COMPLEMENT C1R and COMPLEMENT C1S, thus initiating the cascade of COMPLEMENT ACTIVATION via the CLASSICAL COMPLEMENT PATHWAY.
The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B.
White blood cells. These include granular leukocytes (BASOPHILS; EOSINOPHILS; and NEUTROPHILS) as well as non-granular leukocytes (LYMPHOCYTES and MONOCYTES).
Molecules on the surface of some B-lymphocytes and macrophages, that recognize and combine with the C3b, C3d, C1q, and C4b components of complement.
A glycoprotein that is important in the activation of CLASSICAL COMPLEMENT PATHWAY. C4 is cleaved by the activated COMPLEMENT C1S into COMPLEMENT C4A and COMPLEMENT C4B.
A species of gram-negative, aerobic BACTERIA. It is a commensal and pathogen only of humans, and can be carried asymptomatically in the NASOPHARYNX. When found in cerebrospinal fluid it is the causative agent of cerebrospinal meningitis (MENINGITIS, MENINGOCOCCAL). It is also found in venereal discharges and blood. There are at least 13 serogroups based on antigenic differences in the capsular polysaccharides; the ones causing most meningitis infections being A, B, C, Y, and W-135. Each serogroup can be further classified by serotype, serosubtype, and immunotype.
Polysaccharides found in bacteria and in capsules thereof.
Infections with bacteria of the species NEISSERIA MENINGITIDIS.
Polysaccharides consisting of mannose units.
Potentially pathogenic bacteria found in nasal membranes, skin, hair follicles, and perineum of warm-blooded animals. They may cause a wide range of infections and intoxications.
Serum that contains antibodies. It is obtained from an animal that has been immunized either by ANTIGEN injection or infection with microorganisms containing the antigen.
An adhesion-promoting leukocyte surface membrane heterodimer. The alpha subunit consists of the CD11b ANTIGEN and the beta subunit the CD18 ANTIGEN. The antigen, which is an integrin, functions both as a receptor for complement 3 and in cell-cell and cell-substrate adhesive interactions.
Amyloid P component is a small, non-fibrillar glycoprotein found in normal serum and in all amyloid deposits. It has a pentagonal (pentaxin) structure. It is an acute phase protein, modulates immunologic responses, inhibits ELASTASE, and has been suggested as an indicator of LIVER DISEASE.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
A species of gram-negative bacteria that grows preferentially in the vacuoles of the host cell. It is the etiological agent of Q FEVER.
Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.
Molecular sites on or in some B-lymphocytes and macrophages that recognize and combine with COMPLEMENT C3B. The primary structure of these receptors reveal that they contain transmembrane and cytoplasmic domains, with their extracellular portion composed entirely of thirty short consensus repeats each having 60 to 70 amino acids.
Immunoglobulins produced in a response to FUNGAL ANTIGENS.
A gram-positive organism found in the upper respiratory tract, inflammatory exudates, and various body fluids of normal and/or diseased humans and, rarely, domestic animals.
A bacterium which causes mastitis in cattle and occasionally in man.
The body fluid that circulates in the vascular system (BLOOD VESSELS). Whole blood includes PLASMA and BLOOD CELLS.
An acute infectious disease caused by COXIELLA BURNETII. It is characterized by a sudden onset of FEVER; HEADACHE; malaise; and weakness. In humans, it is commonly contracted by inhalation of infected dusts derived from infected domestic animals (ANIMALS, DOMESTIC).
Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins.
A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection.
A genus of gram-positive, facultatively anaerobic, coccoid bacteria. Its organisms occur singly, in pairs, and in tetrads and characteristically divide in more than one plane to form irregular clusters. Natural populations of Staphylococcus are found on the skin and mucous membranes of warm-blooded animals. Some species are opportunistic pathogens of humans and animals.
Specific molecular sites on the surface of various cells, including B-lymphocytes and macrophages, that combine with IMMUNOGLOBULIN Gs. Three subclasses exist: Fc gamma RI (the CD64 antigen, a low affinity receptor), Fc gamma RII (the CD32 antigen, a high affinity receptor), and Fc gamma RIII (the CD16 antigen, a low affinity receptor).
Molecules found on the surface of some, but not all, B-lymphocytes, T-lymphocytes, and macrophages, which recognize and combine with the Fc (crystallizable) portion of immunoglobulin molecules.
Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
The complex formed by the binding of antigen and antibody molecules. The deposition of large antigen-antibody complexes leading to tissue damage causes IMMUNE COMPLEX DISEASES.
Cell surface molecules on cells of the immune system that specifically bind surface molecules or messenger molecules and trigger changes in the behavior of cells. Although these receptors were first identified in the immune system, many have important functions elsewhere.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Physicochemical property of fimbriated (FIMBRIAE, BACTERIAL) and non-fimbriated bacteria of attaching to cells, tissue, and nonbiological surfaces. It is a factor in bacterial colonization and pathogenicity.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
A class of immunoglobulin bearing mu chains (IMMUNOGLOBULIN MU-CHAINS). IgM can fix COMPLEMENT. The name comes from its high molecular weight and originally being called a macroglobulin.
Transport proteins that carry specific substances in the blood or across cell membranes.
Large, phagocytic mononuclear leukocytes produced in the vertebrate BONE MARROW and released into the BLOOD; contain a large, oval or somewhat indented nucleus surrounded by voluminous cytoplasm and numerous organelles.
Substances elaborated by bacteria that have antigenic activity.
The capacity of a normal organism to remain unaffected by microorganisms and their toxins. It results from the presence of naturally occurring ANTI-INFECTIVE AGENTS, constitutional factors such as BODY TEMPERATURE and immediate acting immune cells such as NATURAL KILLER CELLS.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.

2-Deoxyglucose selectively inhibits Fc and complement receptor-mediated phagocytosis in mouse peritoneal macrophages II. Dissociation of the inhibitory effects of 2-deoxyglucose on phagocytosis and ATP generation. (1/1165)

Macrophages incubated in 2-deoxy-D-glucose (2-dG)-containing medium showed a marked decrease in cellular ATP content, and were unable to ingest IgG- and complement-coated erythrocytes via the corresponding membrane receptors for these ligands. However, the inhibitory effects of 2-dG on Fc- and C3 receptor-mediated phagocytosis were not a consequence of lowered macrophage ATP levels since addition of glucose or mannose to the culture medium restored the capacity of the macrophages to ingest IgG- and C3-coated particles without increasing ATP levels. These results indicate that Fc- and C3 receptor-mediated phagocytosis (opsonin dependent) differs qualitatively from the ingestion of latex and zymosan particles (opsonin independent); they suggest that the same regulatory molecules govern the responses of phagocytic cells to signals initiated by both the Fc and C3 receptors. The possibility that these molecules are regulated by glycosylation is discussed.  (+info)

Influenza A virus accelerates neutrophil apoptosis and markedly potentiates apoptotic effects of bacteria. (2/1165)

Neutrophils are recruited into the airway in the early phase of uncomplicated influenza A virus (IAV) infection and during the bacterial superinfections that are a significant cause of morbidity and mortality in IAV-infected subjects. In this report, we show that IAV accelerates neutrophil apoptosis. Unopsonized Escherichia coli had similar effects, although apoptotic effects of opsonized E coli were greater. When neutrophils were treated with both IAV and unopsonized E coli, a marked enhancement of the rate and extent of neutrophil apoptosis occurred as compared with that caused by either pathogen alone. Treatment of neutrophils with IAV markedly increased phagocytosis of E coli. Simultaneous treatment of neutrophils with IAV and E coli also elicited greater hydrogen peroxide production than did either pathogen alone. IAV increased neutrophil expression of Fas antigen and Fas ligand, and it also increased release of Fas ligand into the cell supernatant. These findings may have relevance to the understanding of inflammatory responses to IAV in vivo and of bacterial superinfection of IAV-infected subjects.  (+info)

Role of antibody and complement in opsonization of group B streptococci. (3/1165)

A requirement for the classic complement pathway in opsonization of group B streptococci was observed by using both a chemiluminescence and a radiolabeled bacterial uptake technique. The classic pathway increased levels of opsonization for types Ia and II stock and wild strains and for some type III wild strains. In contrast, other type III wild strains and the type III stock strain had accelerated kinetics of uptake in the presence of an intact classic pathway, but the level of opsonization was unchanged from that with antibody alone. We could not demonstrate a significant role for the alternative pathway in opsonizing stock or wild strains of group B streptococci. Futhermore, electrophoretic and complement consumption analysis by hemolytic titration failed to reveal alternative pathway activation by the majority of strains of this group. Therapy aimed at supplying opsonins for these organisms will require the presence of type-specific antibody.  (+info)

Type-specific opsonophagocytosis of group A Streptococcus by use of a rapid chemiluminescence assay. (4/1165)

A whole-blood chemiluminescence (CL) assay was developed to determine the presence of type-specific opsonic antibodies against group A streptococcus (GAS). Convalescent sera with high bactericidal activities against an M-1 serotype were used to opsonize different M-types of GAS. CL responses were monitored for 20 min, and results were expressed as integral counts/minute per phagocyte. CL responses of phagocytes incubated with M-1 GAS opsonized with homologous (M-1) serum were significantly higher than responses of phagocytes incubated with heterologous (M-3) GAS. Adsorption of convalescent serum against the homologous, but not the heterologous, strain markedly reduced the CL response, demonstrating type specificity. The CL assay showed a high correlation with the indirect bactericidal test (r=0.90). In conclusion, this CL assay is a rapid, highly sensitive, specific, and reproducible method for quantifying type-specific opsonic antibodies against GAS and will be a useful tool for future clinical, basic science, and epidemiological studies.  (+info)

Pseudomonas aeruginosa outer-membrane protein F epitopes are highly immunogenic in mice when expressed on a plant virus. (5/1165)

A synthetic peptide (peptide 10) representing a surface-exposed, linear B cell epitope from outer-membrane (OM) protein F of Pseudomonas aeruginosa was shown previously to afford protection in mice from P. aeruginosa infection. This peptide was expressed in tandem with the protein F peptide 18 on each of the two coat proteins of cowpea mosaic virus (CPMV). The chimaeric virus particles (CVPs) expressing the peptides on the S (small) coat protein (CPMV-PAE4) and L (large) coat protein (CPMV-PAE5) were used to immunize mice. Following subcutaneous immunization in Freund's and QuilA adjuvants, CPMV-PAE4 induced antibodies predominantly against peptide 18, whereas CPMV-PAE5 produced antibodies exclusively against peptide 10, indicating that the site of peptide expression on CPMV influences its immune recognition. The anti-peptide antibodies elicited by CPMV-PAE5 were predominantly of the IgG2a isotype, indicating a highly polarized TH1-type response. The peptide-specific IgG2a strongly recognized the whole F protein, but more importantly, recognized protein F in all seven Fisher-Devlin immunotypes of P. aeruginosa. Furthermore, the peptide-specific IgG2a in CVP/QS-21 adjuvant-immunized mice was shown to bind complement and to augment phagocytosis of P. aeruginosa by human neutrophils in vitro. The ability of CPMV-PAE5 to induce P. aeruginosa-specific opsonic IgG2a gives it potential for further development as a protective vaccine against P. aeruginosa.  (+info)

Participation of cofilin in opsonized zymosan-triggered activation of neutrophil-like HL-60 cells through rapid dephosphorylation and translocation to plasma membranes. (6/1165)

We studied the roles of cofilin, an actin-binding phosphoprotein, in superoxide production of neutrophil-like HL-60 cells triggered by opsonized zymosan (OZ). OZ caused dephosphorylation of cofilin as well as a transient increase of F-actin. Both reactions were complete within 30 s. Okadaic acid (OA) magnified the OZ-triggered O2--production 3.3-fold at 1 microM, but inhibited it completely at 5 microM. We used these critical concentrations to study the effects of OA on changes in phosphorylation and intracellular localization of cofilin. The OZ-induced dephosphorylation of cofilin was inhibited by 5 microM OA but not by 1 microM OA. Subcellular fractionation and immunoblotting revealed that 1 microM OA increased cofilin on the phagosomal membranous fraction but 5 microM OA decreased it. At 1 microM, OA increased translocation of p47phox to membranes, which may explain in part the enhancing effect of 1 microM OA. Confocal laser scanning microscopy showed that: (i) Cofilin diffused throughout the cytosol of resting cells, but accumulated at the plasma membranes forming phagocytic vesicles in activated cells. (ii) At 1 microM, OA had little effect on the OZ-evoked translocation of cofilin, whereas 5 microM OA suppressed it completely. (iii) OA alone, which could not trigger the phagocytic respiratory burst, did not cause any change in the distribution of cofilin at such concentrations. Furthermore, in a superoxide-producing cell-free system employing membranous and cytosolic fractions, affinity-purified anti-cofilin antibody showed an enhancing effect. These results suggest that cofilin participates in the superoxide production of the OZ-activated phagocytes through dephosphorylation and translocation. The roles of cofilin in the activated leukocytes will be discussed.  (+info)

Relationship between cell surface carbohydrates and intrastrain variation on opsonophagocytosis of Streptococcus pneumoniae. (7/1165)

Streptococcus pneumoniae undergoes spontaneous phase variation between a transparent and an opaque colony phenotype, the latter being more virulent in a murine model of sepsis. Opaque pneumococci have previously been shown to express lower amounts of C polysaccharide (cell wall teichoic acid) and in this study were shown to have a higher content of capsular polysaccharide by immunoelectron microscopy. This report then examined the relationship between expression of these two cell surface carbohydrate structures and their relative contribution to the increased virulence of opaque variants. Comparison of genetically related strains showed that the differential content of capsular polysaccharide did not affect the amount of teichoic acid as measured by a capture enzyme-linked immunosorbent assay (ELISA). In contrast, when the teichoic acid structure was altered by replacing choline in the growth medium with structural analogs, the quantity of capsular polysaccharide as measured by a capture ELISA was decreased, demonstrating a linkage in the expression of the two surface carbohydrate structures. A standardized assay was used to assess the relative contribution of cell surface carbohydrates to opsonophagocytosis. The opaque variants required 1.2- to 30-fold more immune human serum to achieve 50% opsonophagocytic killing than did related transparent variants (types 6B and 9V). The opsonophagocytic titer was proportional to the quantity of capsular polysaccharide rather than teichoic acid. The major factor in binding of the opsonin, C-reactive protein (CRP), was also the amount of capsular polysaccharide rather than the teichoic acid ligand. Only for the transparent variant (type 6B), which bound more CRP, was there enhanced opsonophagocytic killing in the presence of this serum protein. Increased expression of capsular polysaccharide, therefore, appeared to be the major factor in the decreased opsonophagocytic killing of opaque pneumococci.  (+info)

Avidity as a determinant of the protective efficacy of human antibodies to pneumococcal capsular polysaccharides. (8/1165)

Antibodies reactive with capsular polysaccharides are considered the principal mediators of immunity against invasive diseases caused by Streptococcus pneumoniae. In this study, we tested the hypothesis that anti-pneumococcal capsular polysaccharide (PPS) antibody avidity can influence protective efficacy. We measured the avidities of individual adult postvaccination immunoglobulin G2 (IgG2) antibodies to PPS serotypes 6B and 23F and examined the relationship between avidity and opsonophagocytic and mouse-protective activities. The avidities of PPS 6B- and PPS 23F-specific IgG2 antibodies ranged from 6 to 31 nM-1 and from 3 to 20 nM-1, respectively. We observed an inverse correlation between the magnitude of avidity and the amount of antibody required to protect mice against lethal bacteremia caused by serotype 6B pneumococci. Similarly, higher-avidity antibodies were more effective than lower-avidity antibodies in vitro in mediating complement-dependent opsonophagocytosis of both 6B and 23F pneumococci. These data suggest that in adults, PPS antibodies are sufficiently polymorphic to possess biologically significant variations in avidity. We conclude that avidity functions as an important determinant of anticapsular antibody protective efficacy against pneumococci.  (+info)

Opsonins are proteins found in the blood that help enhance the immune system's response to foreign substances, such as bacteria and viruses. They do this by coating the surface of these pathogens, making them more recognizable to immune cells like neutrophils and macrophages. This process, known as opsonization, facilitates the phagocytosis (engulfing and destroying) of the pathogen by these immune cells.

There are two main types of opsonins:

1. IgG antibodies: These are a type of antibody produced by the immune system in response to an infection. They bind to specific antigens on the surface of the pathogen, marking them for destruction by phagocytic cells.
2. Complement proteins: The complement system is a group of proteins that work together to help eliminate pathogens. When activated, the complement system can produce various proteins that act as opsonins, including C3b and C4b. These proteins bind to the surface of the pathogen, making it easier for phagocytic cells to recognize and destroy them.

In summary, opsonin proteins are crucial components of the immune system's response to infections, helping to mark foreign substances for destruction by immune cells like neutrophils and macrophages.

Phagocytosis is the process by which certain cells in the body, known as phagocytes, engulf and destroy foreign particles, bacteria, or dead cells. This mechanism plays a crucial role in the immune system's response to infection and inflammation. Phagocytes, such as neutrophils, monocytes, and macrophages, have receptors on their surface that recognize and bind to specific molecules (known as antigens) on the target particles or microorganisms.

Once attached, the phagocyte extends pseudopodia (cell extensions) around the particle, forming a vesicle called a phagosome that completely encloses it. The phagosome then fuses with a lysosome, an intracellular organelle containing digestive enzymes and other chemicals. This fusion results in the formation of a phagolysosome, where the engulfed particle is broken down by the action of these enzymes, neutralizing its harmful effects and allowing for the removal of cellular debris or pathogens.

Phagocytosis not only serves as a crucial defense mechanism against infections but also contributes to tissue homeostasis by removing dead cells and debris.

Neutrophils are a type of white blood cell that are part of the immune system's response to infection. They are produced in the bone marrow and released into the bloodstream where they circulate and are able to move quickly to sites of infection or inflammation in the body. Neutrophils are capable of engulfing and destroying bacteria, viruses, and other foreign substances through a process called phagocytosis. They are also involved in the release of inflammatory mediators, which can contribute to tissue damage in some cases. Neutrophils are characterized by the presence of granules in their cytoplasm, which contain enzymes and other proteins that help them carry out their immune functions.

Bladder exstrophy is a congenital birth defect that affects the urinary and reproductive systems, as well as the abdominal wall. In this condition, the bladder is not fully formed and is turned inside out and exposed on the outside of the body at birth. This results in the inability to control urination and can also lead to other complications such as infection and kidney damage if left untreated.

Bladder exstrophy occurs due to a problem with the development of the fetus during pregnancy, specifically during the formation of the lower abdominal wall. It is more common in boys than girls, and can occur on its own or as part of a spectrum of defects known as the exstrophy-epispadias complex.

Treatment for bladder exstrophy typically involves surgical reconstruction to repair the bladder and lower abdominal wall. This may be done in stages, starting with the closure of the abdominal wall and then followed by bladder reconstruction at a later time. In some cases, additional surgeries may be necessary to address other associated defects or complications. With proper treatment, most children with bladder exstrophy can lead normal lives, although they may require ongoing medical management and monitoring throughout their lives.

The complement system is a group of proteins found in the blood and on the surface of cells that when activated, work together to help eliminate pathogens such as bacteria, viruses, and fungi from the body. The proteins are normally inactive in the bloodstream. When they encounter an invading microorganism or foreign substance, a series of reactions take place leading to the activation of the complement system. Activation results in the production of effector molecules that can punch holes in the cell membranes of pathogens, recruit and activate immune cells, and help remove debris and dead cells from the body.

There are three main pathways that can lead to complement activation: the classical pathway, the lectin pathway, and the alternative pathway. Each pathway involves a series of proteins that work together in a cascade-like manner to amplify the response and generate effector molecules. The three main effector molecules produced by the complement system are C3b, C4b, and C5b. These molecules can bind to the surface of pathogens, marking them for destruction by other immune cells.

Complement proteins also play a role in the regulation of the immune response. They help to prevent excessive activation of the complement system, which could damage host tissues. Dysregulation of the complement system has been implicated in a number of diseases, including autoimmune disorders and inflammatory conditions.

In summary, Complement System Proteins are a group of proteins that play a crucial role in the immune response by helping to eliminate pathogens and regulate the immune response. They can be activated through three different pathways, leading to the production of effector molecules that mark pathogens for destruction. Dysregulation of the complement system has been linked to various diseases.

Blood bactericidal activity refers to the ability of an individual's blood to kill or inhibit the growth of bacteria. This is an important aspect of the body's immune system, as it helps to prevent infection and maintain overall health. The bactericidal activity of blood can be influenced by various factors, including the presence of antibodies, white blood cells (such as neutrophils), and complement proteins.

In medical terms, the term "bactericidal" specifically refers to an agent or substance that is capable of killing bacteria. Therefore, when we talk about blood bactericidal activity, we are referring to the collective ability of various components in the blood to kill or inhibit the growth of bacteria. This is often measured in laboratory tests as a way to assess a person's immune function and their susceptibility to infection.

It's worth noting that not all substances in the blood are bactericidal; some may simply inhibit the growth of bacteria without killing them. These substances are referred to as bacteriostatic. Both bactericidal and bacteriostatic agents play important roles in maintaining the body's defense against infection.

Hemocytes are specialized cells found in the open circulatory system of invertebrates, including insects, crustaceans, and mollusks. They play crucial roles in the immune response and defense mechanisms of these organisms. Hemocytes can be categorized into several types based on their functions and morphologies, such as phagocytic cells, encapsulating cells, and clotting cells. These cells are responsible for various immunological activities, including recognition and removal of foreign particles, pathogens, and debris; production of immune effector molecules; and contribution to the formation of blood clots to prevent excessive bleeding. In some invertebrates, hemocytes also participate in wound healing, tissue repair, and other physiological processes.

'Cryptococcus' is a genus of encapsulated, budding yeast that are found in the environment, particularly in soil and bird droppings. The most common species that causes infection in humans is Cryptococcus neoformans, followed by Cryptococcus gattii.

Infection with Cryptococcus can occur when a person inhales the microscopic yeast cells, which can then lead to lung infections (pneumonia) or disseminated disease, particularly in people with weakened immune systems. The most common form of disseminated cryptococcal infection is meningitis, an inflammation of the membranes surrounding the brain and spinal cord.

Cryptococcal infections can be serious and even life-threatening, especially in individuals with HIV/AIDS or other conditions that weaken the immune system. Treatment typically involves antifungal medications, such as amphotericin B and fluconazole.

Luminescent measurements refer to the quantitative assessment of the emission of light from a substance that has been excited, typically through some form of energy input such as electrical energy or radiation. In the context of medical diagnostics and research, luminescent measurements can be used in various applications, including bioluminescence imaging, which is used to study biological processes at the cellular and molecular level.

Bioluminescence occurs when a chemical reaction produces light within a living organism, often through the action of enzymes such as luciferase. By introducing a luciferase gene into cells or organisms, researchers can use bioluminescent measurements to track cellular processes and monitor gene expression in real time.

Luminescent measurements may also be used in medical research to study the properties of materials used in medical devices, such as LEDs or optical fibers, or to develop new diagnostic tools based on light-emitting nanoparticles or other luminescent materials.

In summary, luminescent measurements are a valuable tool in medical research and diagnostics, providing a non-invasive way to study biological processes and develop new technologies for disease detection and treatment.

Collectins are a group of proteins that belong to the collectin family, which are involved in the innate immune system. They are composed of a collagen-like region and a carbohydrate recognition domain (CRD), which allows them to bind to specific sugars on the surface of microorganisms, cells, and particles. Collectins play a crucial role in the defense against pathogens by promoting the clearance of microbes, modulating inflammation, and regulating immune responses.

Some examples of collectins include:

* Surfactant protein A (SP-A) and surfactant protein D (SP-D), which are found in the lungs and help to maintain the stability of the lung lining and protect against respiratory infections.
* Mannose-binding lectin (MBL), which is a serum protein that binds to mannose sugars on the surface of microorganisms, activating the complement system and promoting phagocytosis.
* Collectin liver 1 (CL-L1) and collectin kidney 1 (CL-K1), which are found in the liver and kidneys, respectively, and play a role in the clearance of apoptotic cells and immune complexes.

Deficiencies or mutations in collectins can lead to increased susceptibility to infections, autoimmune diseases, and other disorders.

Subacute bacterial endocarditis (SBE) is a type of infective endocarditis that typically has a more indolent course compared to acute bacterial endocarditis. It is caused by organisms that are less virulent and have a higher affinity for damaged heart valves or endocardium.

The most common causative organisms of SBE include Streptococcus viridans, Streptococcus bovis, and enterococci. The infection often develops over a period of weeks to months, with nonspecific symptoms such as fatigue, weakness, fever, weight loss, and night sweats.

SBE can lead to serious complications, including heart failure, valvular damage, embolic events, and even death if left untreated. Treatment typically involves prolonged courses of intravenous antibiotics, with surgical intervention reserved for cases with severe valvular damage or uncontrolled infection.

Preventive measures include appropriate management of underlying heart conditions, prophylactic antibiotic therapy in high-risk individuals undergoing dental or invasive procedures, and good oral hygiene.

Complement C3b is a protein fragment that plays a crucial role in the complement system, which is a part of the immune system that helps to clear pathogens and damaged cells from the body. C3b is generated during the activation of the complement system, particularly via the classical, lectin, and alternative pathways.

Once formed, C3b can bind covalently to the surface of microbes or other target particles, marking them for destruction by other components of the immune system. Additionally, C3b can interact with other proteins in the complement system to generate the membrane attack complex (MAC), which forms pores in the membranes of targeted cells, leading to their lysis and removal.

In summary, Complement C3b is a vital protein fragment involved in the recognition, tagging, and elimination of pathogens and damaged cells during the immune response.

The alternative complement pathway is one of the three initiating pathways of the complement system, which is a part of the innate immune system that helps to clear pathogens and damaged cells from the body. The other two pathways are the classical and lectin pathways.

The alternative pathway is continuously activated at a low level, even in the absence of infection or injury, through the spontaneous cleavage of complement component C3 into C3a and C3b by the protease factor D in the presence of magnesium ions. The generated C3b can then bind covalently to nearby surfaces, including pathogens and host cells.

On self-surfaces, regulatory proteins like decay-accelerating factor (DAF) or complement receptor 1 (CR1) help to prevent the formation of the alternative pathway convertase and thus further activation of the complement system. However, on foreign surfaces, the C3b can recruit more complement components, forming a complex called the alternative pathway convertase (C3bBb), which cleaves additional C3 molecules into C3a and C3b.

The generated C3b can then bind to the surface and participate in the formation of the membrane attack complex (MAC), leading to the lysis of the target cell. The alternative pathway plays a crucial role in the defense against gram-negative bacteria, fungi, and parasites, as well as in the clearance of immune complexes and apoptotic cells. Dysregulation of the alternative complement pathway has been implicated in several diseases, including autoimmune disorders and atypical hemolytic uremic syndrome (aHUS).

Schistosomatidae is a family of trematode flatworms, more commonly known as blood flukes. These parasitic worms are responsible for causing schistosomiasis (also known as bilharzia or snail fever), a significant public health problem in tropical and subtropical regions.

The life cycle of Schistosoma species involves two intermediate hosts: freshwater snails and humans. The adult worms live in the blood vessels of the human host, where they lay eggs that are excreted through urine or feces. These eggs hatch in fresh water, releasing miracidia, which infect specific snail species. After several developmental stages within the snail, cercariae are released into the water and penetrate the skin of humans coming into contact with infested water, thus completing the life cycle.

Schistosomatidae includes several genera, among which Schistosoma mansoni, S. haematobium, and S. japonicum are the most prevalent and clinically significant species causing schistosomiasis in humans.

Complement activation is the process by which the complement system, a part of the immune system, is activated to help eliminate pathogens and damaged cells from the body. The complement system consists of a group of proteins that work together to recognize and destroy foreign substances.

Activation of the complement system can occur through three different pathways: the classical pathway, the lectin pathway, and the alternative pathway. Each pathway involves a series of proteolytic reactions that ultimately result in the formation of the membrane attack complex (MAC), which creates a pore in the membrane of the target cell, leading to its lysis and removal.

The classical pathway is typically activated by the binding of antibodies to antigens on the surface of a pathogen or damaged cell. The lectin pathway is activated by the recognition of specific carbohydrate structures on the surface of microorganisms. The alternative pathway can be spontaneously activated and serves as an amplification loop for both the classical and lectin pathways.

Complement activation plays a crucial role in the immune response, but uncontrolled or excessive activation can also lead to tissue damage and inflammation. Dysregulation of complement activation has been implicated in various diseases, including autoimmune disorders, inflammatory conditions, and neurodegenerative diseases.

Zymosan is a type of substance that is derived from the cell walls of yeast and some types of fungi. It's often used in laboratory research as an agent to stimulate inflammation, because it can activate certain immune cells (such as neutrophils) and cause them to release pro-inflammatory chemicals.

In medical terms, Zymosan is sometimes used as a tool for studying the immune system and inflammation in experimental settings. It's important to note that Zymosan itself is not a medical condition or disease, but rather a research reagent with potential applications in understanding human health and disease.

Respiratory burst is a term used in the field of biology, particularly in the context of immunology and cellular processes. It does not have a direct application to clinical medicine, but it is important for understanding certain physiological and pathophysiological mechanisms. Here's a definition of respiratory burst:

Respiratory burst is a rapid increase in oxygen consumption by phagocytic cells (like neutrophils, monocytes, and macrophages) following their activation in response to various stimuli, such as pathogens or inflammatory molecules. This process is part of the innate immune response and serves to eliminate invading microorganisms.

The respiratory burst involves the activation of NADPH oxidase, an enzyme complex present in the membrane of phagosomes (the compartment where pathogens are engulfed). Upon activation, NADPH oxidase catalyzes the reduction of oxygen to superoxide radicals, which then dismutate to form hydrogen peroxide. These reactive oxygen species (ROS) can directly kill or damage microorganisms and also serve as signaling molecules for other immune cells.

While respiratory burst is a crucial part of the immune response, excessive or dysregulated ROS production can contribute to tissue damage and chronic inflammation, which have implications in various pathological conditions, such as atherosclerosis, neurodegenerative diseases, and cancer.

Phagocytes are a type of white blood cell in the immune system that engulf and destroy foreign particles, microbes, and cellular debris. They play a crucial role in the body's defense against infection and tissue damage. There are several types of phagocytes, including neutrophils, monocytes, macrophages, and dendritic cells. These cells have receptors that recognize and bind to specific molecules on the surface of foreign particles or microbes, allowing them to engulf and digest the invaders. Phagocytosis is an important mechanism for maintaining tissue homeostasis and preventing the spread of infection.

Mannose-Binding Lectin (MBL) is a protein that belongs to the collectin family and plays a crucial role in the innate immune system. It's primarily produced by the liver and secreted into the bloodstream. MBL binds to carbohydrate structures, such as mannose, found on the surface of various microorganisms, including bacteria, viruses, fungi, and parasites.

Once MBL binds to these microorganisms, it activates the complement system through the lectin pathway, which leads to the destruction of the pathogens by opsonization (marking for phagocytosis) or direct lysis. Additionally, MBL can also initiate other immune responses, such as inflammation and immune cell activation, helping to protect the host from infections.

Deficiencies in MBL have been associated with increased susceptibility to certain infectious diseases, autoimmune disorders, and allergies. However, more research is needed to fully understand the complex role of MBL in human health and disease.

Macrophages are a type of white blood cell that are an essential part of the immune system. They are large, specialized cells that engulf and destroy foreign substances, such as bacteria, viruses, parasites, and fungi, as well as damaged or dead cells. Macrophages are found throughout the body, including in the bloodstream, lymph nodes, spleen, liver, lungs, and connective tissues. They play a critical role in inflammation, immune response, and tissue repair and remodeling.

Macrophages originate from monocytes, which are a type of white blood cell produced in the bone marrow. When monocytes enter the tissues, they differentiate into macrophages, which have a larger size and more specialized functions than monocytes. Macrophages can change their shape and move through tissues to reach sites of infection or injury. They also produce cytokines, chemokines, and other signaling molecules that help coordinate the immune response and recruit other immune cells to the site of infection or injury.

Macrophages have a variety of surface receptors that allow them to recognize and respond to different types of foreign substances and signals from other cells. They can engulf and digest foreign particles, bacteria, and viruses through a process called phagocytosis. Macrophages also play a role in presenting antigens to T cells, which are another type of immune cell that helps coordinate the immune response.

Overall, macrophages are crucial for maintaining tissue homeostasis, defending against infection, and promoting wound healing and tissue repair. Dysregulation of macrophage function has been implicated in a variety of diseases, including cancer, autoimmune disorders, and chronic inflammatory conditions.

The "Classical Complement Pathway" is one of the three pathways that make up the complement system, which is a part of the immune system in humans and other animals. The complement system helps to enhance the ability of antibodies and phagocytic cells to clear pathogens from the body.

The Classical Complement Pathway is initiated by the binding of the first component of the complement system, C1, to an activator surface, such as an antigen-antibody complex. Activation of C1 results in the sequential activation of other components of the complement system, including C4 and C2, which form the C3 convertase (C4b2a). The C3 convertase cleaves the third component of the complement system, C3, into C3a and C3b. C3b then binds to the activator surface and forms a complex with other components of the complement system, leading to the formation of the membrane attack complex (MAC), which creates a pore in the membrane of the target cell, causing its lysis.

The Classical Complement Pathway plays an important role in the immune response to pathogens and can also contribute to inflammation and tissue damage in certain diseases, such as autoimmune disorders and allergies.

'Cryptococcus neoformans' is a species of encapsulated, budding yeast that is an important cause of fungal infections in humans and animals. The capsule surrounding the cell wall is composed of polysaccharides and is a key virulence factor, allowing the organism to evade host immune responses. C. neoformans is found worldwide in soil, particularly in association with bird droppings, and can be inhaled, leading to pulmonary infection. In people with weakened immune systems, such as those with HIV/AIDS, hematological malignancies, or organ transplants, C. neoformans can disseminate from the lungs to other sites, most commonly the central nervous system (CNS), causing meningitis. The infection can also affect other organs, including the skin, bones, and eyes.

The diagnosis of cryptococcosis typically involves microscopic examination and culture of clinical specimens, such as sputum, blood, or cerebrospinal fluid (CSF), followed by biochemical and molecular identification of the organism. Treatment usually consists of a combination of antifungal medications, such as amphotericin B and fluconazole, along with management of any underlying immunodeficiency. The prognosis of cryptococcosis depends on various factors, including the patient's immune status, the extent and severity of infection, and the timeliness and adequacy of treatment.

Bacterial antibodies are a type of antibodies produced by the immune system in response to an infection caused by bacteria. These antibodies are proteins that recognize and bind to specific antigens on the surface of the bacterial cells, marking them for destruction by other immune cells. Bacterial antibodies can be classified into several types based on their structure and function, including IgG, IgM, IgA, and IgE. They play a crucial role in the body's defense against bacterial infections and provide immunity to future infections with the same bacteria.

Complement C1q is a protein that is part of the complement system, which is a group of proteins in the blood that help to eliminate pathogens and damaged cells from the body. C1q is the first component of the classical complement pathway, which is activated by the binding of C1q to antibodies that are attached to the surface of a pathogen or damaged cell.

C1q is composed of six identical polypeptide chains, each containing a collagen-like region and a globular head region. The globular heads can bind to various structures, including the Fc regions of certain antibodies, immune complexes, and some types of cells. When C1q binds to an activating surface, it triggers a series of proteolytic reactions that lead to the activation of other complement components and the formation of the membrane attack complex (MAC), which can punch holes in the membranes of pathogens or damaged cells, leading to their destruction.

In addition to its role in the immune system, C1q has also been found to have roles in various physiological processes, including tissue remodeling, angiogenesis, and the clearance of apoptotic cells. Dysregulation of the complement system, including abnormalities in C1q function, has been implicated in a variety of diseases, including autoimmune disorders, inflammatory diseases, and neurodegenerative conditions.

Immunoglobulin G (IgG) is a type of antibody, which is a protective protein produced by the immune system in response to foreign substances like bacteria or viruses. IgG is the most abundant type of antibody in human blood, making up about 75-80% of all antibodies. It is found in all body fluids and plays a crucial role in fighting infections caused by bacteria, viruses, and toxins.

IgG has several important functions:

1. Neutralization: IgG can bind to the surface of bacteria or viruses, preventing them from attaching to and infecting human cells.
2. Opsonization: IgG coats the surface of pathogens, making them more recognizable and easier for immune cells like neutrophils and macrophages to phagocytose (engulf and destroy) them.
3. Complement activation: IgG can activate the complement system, a group of proteins that work together to help eliminate pathogens from the body. Activation of the complement system leads to the formation of the membrane attack complex, which creates holes in the cell membranes of bacteria, leading to their lysis (destruction).
4. Antibody-dependent cellular cytotoxicity (ADCC): IgG can bind to immune cells like natural killer (NK) cells and trigger them to release substances that cause target cells (such as virus-infected or cancerous cells) to undergo apoptosis (programmed cell death).
5. Immune complex formation: IgG can form immune complexes with antigens, which can then be removed from the body through various mechanisms, such as phagocytosis by immune cells or excretion in urine.

IgG is a critical component of adaptive immunity and provides long-lasting protection against reinfection with many pathogens. It has four subclasses (IgG1, IgG2, IgG3, and IgG4) that differ in their structure, function, and distribution in the body.

Leukocytes, also known as white blood cells (WBCs), are a crucial component of the human immune system. They are responsible for protecting the body against infections and foreign substances. Leukocytes are produced in the bone marrow and circulate throughout the body in the bloodstream and lymphatic system.

There are several types of leukocytes, including:

1. Neutrophils - These are the most abundant type of leukocyte and are primarily responsible for fighting bacterial infections. They contain enzymes that can destroy bacteria.
2. Lymphocytes - These are responsible for producing antibodies and destroying virus-infected cells, as well as cancer cells. There are two main types of lymphocytes: B-lymphocytes and T-lymphocytes.
3. Monocytes - These are the largest type of leukocyte and help to break down and remove dead or damaged tissues, as well as microorganisms.
4. Eosinophils - These play a role in fighting parasitic infections and are also involved in allergic reactions and inflammation.
5. Basophils - These release histamine and other chemicals that cause inflammation in response to allergens or irritants.

An abnormal increase or decrease in the number of leukocytes can indicate an underlying medical condition, such as an infection, inflammation, or a blood disorder.

Complement receptors are proteins found on the surface of various cells in the human body, including immune cells and some non-immune cells. They play a crucial role in the complement system, which is a part of the innate immune response that helps to eliminate pathogens and damaged cells from the body. Complement receptors bind to complement proteins or fragments that are generated during the activation of the complement system. This binding triggers various intracellular signaling events that can lead to diverse cellular responses, such as phagocytosis, inflammation, and immune regulation.

There are several types of complement receptors, including:

1. CR1 (CD35): A receptor found on erythrocytes, B cells, neutrophils, monocytes, macrophages, and glomerular podocytes. It functions in the clearance of immune complexes and regulates complement activation.
2. CR2 (CD21): Expressed mainly on B cells and follicular dendritic cells. It facilitates antigen presentation, B-cell activation, and immune regulation.
3. CR3 (CD11b/CD18, Mac-1): Present on neutrophils, monocytes, macrophages, and some T cells. It mediates cell adhesion, phagocytosis, and intracellular signaling.
4. CR4 (CD11c/CD18, p150,95): Expressed on neutrophils, monocytes, macrophages, and dendritic cells. It is involved in cell adhesion, phagocytosis, and intracellular signaling.
5. C5aR (CD88): Found on various immune cells, including neutrophils, monocytes, macrophages, mast cells, eosinophils, and dendritic cells. It binds to the complement protein C5a and mediates chemotaxis, degranulation, and inflammation.
6. C5L2 (GPR77): Present on various cell types, including immune cells. Its function is not well understood but may involve regulating C5a-mediated responses or acting as a receptor for other ligands.

These receptors play crucial roles in the immune response and inflammation by mediating various functions such as chemotaxis, phagocytosis, cell adhesion, and intracellular signaling. Dysregulation of these receptors has been implicated in several diseases, including autoimmune disorders, infections, and cancer.

Complement C4 is a protein that plays a crucial role in the complement system, which is a part of the immune system that helps to clear pathogens and damaged cells from the body. Complement C4 is involved in the early stages of the complement activation cascade, where it helps to identify and tag foreign or abnormal cells for destruction by other components of the immune system.

Specifically, Complement C4 can be cleaved into two smaller proteins, C4a and C4b, during the complement activation process. C4b then binds to the surface of the target cell and helps to initiate the formation of the membrane attack complex (MAC), which creates a pore in the cell membrane and leads to lysis or destruction of the target cell.

Deficiencies or mutations in the Complement C4 gene can lead to various immune disorders, including certain forms of autoimmune diseases and susceptibility to certain infections.

Neisseria meningitidis is a Gram-negative, aerobic, bean-shaped diplococcus bacterium. It is one of the leading causes of bacterial meningitis and sepsis (known as meningococcal disease) worldwide. The bacteria can be found in the back of the nose and throat of approximately 10-25% of the general population, particularly in children, teenagers, and young adults, without causing any symptoms or illness. However, when the bacterium invades the bloodstream and spreads to the brain or spinal cord, it can lead to life-threatening infections such as meningitis (inflammation of the membranes surrounding the brain and spinal cord) and septicemia (blood poisoning).

Neisseria meningitidis is classified into 12 serogroups based on the chemical structure of their capsular polysaccharides. The six major serogroups that cause most meningococcal disease worldwide are A, B, C, W, X, and Y. Vaccines are available to protect against some or all of these serogroups.

Meningococcal disease can progress rapidly, leading to severe symptoms such as high fever, headache, stiff neck, confusion, nausea, vomiting, and a rash consisting of purple or red spots. Immediate medical attention is required if someone experiences these symptoms, as meningococcal disease can cause permanent disabilities or death within hours if left untreated.

Bacterial polysaccharides are complex carbohydrates that consist of long chains of sugar molecules (monosaccharides) linked together by glycosidic bonds. They are produced and used by bacteria for various purposes such as:

1. Structural components: Bacterial polysaccharides, such as peptidoglycan and lipopolysaccharide (LPS), play a crucial role in maintaining the structural integrity of bacterial cells. Peptidoglycan is a major component of the bacterial cell wall, while LPS forms the outer layer of the outer membrane in gram-negative bacteria.
2. Nutrient storage: Some bacteria synthesize and store polysaccharides as an energy reserve, similar to how plants store starch. These polysaccharides can be broken down and utilized by the bacterium when needed.
3. Virulence factors: Bacterial polysaccharides can also function as virulence factors, contributing to the pathogenesis of bacterial infections. For example, certain bacteria produce capsular polysaccharides (CPS) that surround and protect the bacterial cells from host immune defenses, allowing them to evade phagocytosis and persist within the host.
4. Adhesins: Some polysaccharides act as adhesins, facilitating the attachment of bacteria to surfaces or host cells. This is important for biofilm formation, which helps bacteria resist environmental stresses and antibiotic treatments.
5. Antigenic properties: Bacterial polysaccharides can be highly antigenic, eliciting an immune response in the host. The antigenicity of these molecules can vary between different bacterial species or even strains within a species, making them useful as targets for vaccines and diagnostic tests.

In summary, bacterial polysaccharides are complex carbohydrates that serve various functions in bacteria, including structural support, nutrient storage, virulence factor production, adhesion, and antigenicity.

Meningococcal infections are caused by the bacterium Neisseria meningitidis, also known as meningococcus. These infections can take several forms, but the most common are meningitis (inflammation of the membranes surrounding the brain and spinal cord) and septicemia (bloodstream infection). Meningococcal infections are contagious and can spread through respiratory droplets or close contact with an infected person. They can be serious and potentially life-threatening, requiring prompt medical attention and treatment with antibiotics. Symptoms of meningococcal meningitis may include fever, headache, stiff neck, and sensitivity to light, while symptoms of septicemia may include fever, chills, rash, and severe muscle pain. Vaccination is available to prevent certain strains of meningococcal disease.

Mannans are a type of complex carbohydrate, specifically a heteropolysaccharide, that are found in the cell walls of certain plants, algae, and fungi. They consist of chains of mannose sugars linked together, often with other sugar molecules such as glucose or galactose.

Mannans have various biological functions, including serving as a source of energy for microorganisms that can break them down. In some cases, mannans can also play a role in the immune response and are used as a component of vaccines to stimulate an immune response.

In the context of medicine, mannans may be relevant in certain conditions such as gut dysbiosis or allergic reactions to foods containing mannans. Additionally, some research has explored the potential use of mannans as a delivery vehicle for drugs or other therapeutic agents.

Staphylococcus aureus is a type of gram-positive, round (coccal) bacterium that is commonly found on the skin and mucous membranes of warm-blooded animals and humans. It is a facultative anaerobe, which means it can grow in the presence or absence of oxygen.

Staphylococcus aureus is known to cause a wide range of infections, from mild skin infections such as pimples, impetigo, and furuncles (boils) to more severe and potentially life-threatening infections such as pneumonia, endocarditis, osteomyelitis, and sepsis. It can also cause food poisoning and toxic shock syndrome.

The bacterium is often resistant to multiple antibiotics, including methicillin, which has led to the emergence of methicillin-resistant Staphylococcus aureus (MRSA) strains that are difficult to treat. Proper hand hygiene and infection control practices are critical in preventing the spread of Staphylococcus aureus and MRSA.

'Immune sera' refers to the serum fraction of blood that contains antibodies produced in response to an antigenic stimulus, such as a vaccine or an infection. These antibodies are proteins known as immunoglobulins, which are secreted by B cells (a type of white blood cell) and can recognize and bind to specific antigens. Immune sera can be collected from an immunized individual and used as a source of passive immunity to protect against infection or disease. It is often used in research and diagnostic settings to identify or measure the presence of specific antigens or antibodies.

The Macrophage-1 Antigen (also known as Macrophage Antigen-1 or CD14) is a glycoprotein found on the surface of various cells, including monocytes, macrophages, and some dendritic cells. It functions as a receptor for complexes formed by lipopolysaccharides (LPS) and LPS-binding protein (LBP), which are involved in the immune response to gram-negative bacteria. CD14 plays a crucial role in activating immune cells and initiating the release of proinflammatory cytokines upon recognizing bacterial components.

In summary, Macrophage-1 Antigen is a cell surface receptor that contributes to the recognition and response against gram-negative bacteria by interacting with LPS-LBP complexes.

Serum Amyloid P-component (SAP) is a protein that is normally present in the blood and other bodily fluids. It is a part of the larger family of pentraxin proteins, which are involved in the innate immune response, meaning they provide immediate defense against foreign invaders without needing to adapt over time. SAP plays a role in inflammation, immune complex clearance, and complement activation.

In the context of amyloidosis, SAP binds to misfolded proteins called amyloid fibrils, which can deposit in various tissues and organs, leading to their dysfunction and failure. The accumulation of these amyloid fibrils with SAP is a hallmark of systemic amyloidosis.

It's important to note that while SAP plays a role in the pathogenesis of amyloidosis, it is not directly responsible for causing the disease. Instead, its presence can serve as a useful marker for diagnosing and monitoring the progression of amyloidosis.

In a medical context, "hot temperature" is not a standard medical term with a specific definition. However, it is often used in relation to fever, which is a common symptom of illness. A fever is typically defined as a body temperature that is higher than normal, usually above 38°C (100.4°F) for adults and above 37.5-38°C (99.5-101.3°F) for children, depending on the source.

Therefore, when a medical professional talks about "hot temperature," they may be referring to a body temperature that is higher than normal due to fever or other causes. It's important to note that a high environmental temperature can also contribute to an elevated body temperature, so it's essential to consider both the body temperature and the environmental temperature when assessing a patient's condition.

Coxiella burnetii is a gram-negative, intracellular bacterium that causes Q fever, a zoonotic disease with various clinical manifestations ranging from asymptomatic seroconversion to acute and chronic forms. The bacterium is highly infectious and can be transmitted to humans through inhalation of contaminated aerosols or direct contact with infected animals or their products. C. burnetii has a unique ability to survive and replicate within host cells, particularly within phagocytic vacuoles, by inhibiting phagosome-lysosome fusion and altering the intracellular environment to promote its survival.

The bacterium exhibits a biphasic developmental cycle, consisting of small cell variants (SCVs) and large cell variants (LCVs). SCVs are metabolically inactive and highly resistant to environmental stressors, including heat, desiccation, and disinfectants. LCVs, on the other hand, are metabolically active and undergo replication within host cells. C. burnetii can form persistent infections, which may contribute to chronic Q fever and its associated complications, such as endocarditis and vascular infection.

Q fever is a worldwide distributed disease, with a higher incidence in rural areas where livestock farming is prevalent. The primary reservoirs for C. burnetii are domestic animals, including cattle, sheep, and goats, although wild animals and arthropods can also serve as potential hosts. Effective antibiotic treatment options for Q fever include doxycycline and fluoroquinolones, while vaccination with the phase I whole-cell vaccine is available in some countries to prevent infection in high-risk populations.

Lectins are a type of proteins that bind specifically to carbohydrates and have been found in various plant and animal sources. They play important roles in biological recognition events, such as cell-cell adhesion, and can also be involved in the immune response. Some lectins can agglutinate certain types of cells or precipitate glycoproteins, while others may have a more direct effect on cellular processes. In some cases, lectins from plants can cause adverse effects in humans if ingested, such as digestive discomfort or allergic reactions.

Complement receptor 3b (CR3b or CD11b/CD18) is not a medical definition itself, but I can provide you with the relevant information regarding this term.

Complement receptor 3 (CR3) is a heterodimeric receptor consisting of two subunits, CD11b (also known as Mac-1 or CR3 alpha) and CD18 (also known as beta2 integrin). There are two forms of the CD11b/CD18 heterodimer: CR3a (CD11b/CD18) and CR3b (CD11b/CD18'). The difference between these two forms lies in the conformation of the CD11b subunit.

Complement receptor 3b (CR3b or CD11b/CD18') is a less common form of the CR3 receptor, which is primarily expressed on myeloid cells such as monocytes, macrophages, and neutrophils. CR3b has a higher affinity for complement component C3b and its fragments iC3b and C3dg compared to CR3a.

CR3b plays a role in various immune functions, including:

1. Phagocytosis: Binding of C3b or its fragments to CR3b facilitates the recognition and uptake of opsonized pathogens by phagocytes.
2. Adhesion: The integrin component of CR3b mediates cell-cell and cell-matrix interactions, contributing to leukocyte migration and recruitment to sites of inflammation or infection.
3. Intracellular signaling: Activation of CR3b can lead to intracellular signaling events that modulate immune responses, such as the release of pro-inflammatory cytokines and reactive oxygen species.

In summary, Complement receptor 3b (CR3b or CD11b/CD18') is a less common form of CR3 primarily expressed on myeloid cells that binds complement component C3b and its fragments with high affinity, mediating phagocytosis, adhesion, and intracellular signaling.

Fungal antibodies are a type of protein called immunoglobulins that are produced by the immune system in response to the presence of fungi in the body. These antibodies are specifically designed to recognize and bind to antigens on the surface of fungal cells, marking them for destruction by other immune cells.

There are several types of fungal antibodies, including IgA, IgG, IgM, and IgE, each with a specific role in the immune response. For example, IgG antibodies are the most common type of antibody found in the blood and provide long-term immunity to fungi, while IgE antibodies are associated with allergic reactions to fungi.

Fungal antibodies can be measured in the blood or other bodily fluids to help diagnose fungal infections, monitor the effectiveness of treatment, or assess immune function in individuals who are at risk for fungal infections, such as those with weakened immune systems due to HIV/AIDS, cancer, or organ transplantation.

Streptococcus pneumoniae, also known as the pneumococcus, is a gram-positive, alpha-hemolytic bacterium frequently found in the upper respiratory tract of healthy individuals. It is a leading cause of community-acquired pneumonia and can also cause other infectious diseases such as otitis media (ear infection), sinusitis, meningitis, and bacteremia (bloodstream infection). The bacteria are encapsulated, and there are over 90 serotypes based on variations in the capsular polysaccharide. Some serotypes are more virulent or invasive than others, and the polysaccharide composition is crucial for vaccine development. S. pneumoniae infection can be treated with antibiotics, but the emergence of drug-resistant strains has become a significant global health concern.

Streptococcus agalactiae, also known as Group B Streptococcus (GBS), is a type of bacteria that commonly colonizes the gastrointestinal and genitourinary tracts of humans. It is Gram-positive, facultatively anaerobic, and forms chains when viewed under the microscope.

While S. agalactiae can be carried asymptomatically by many adults, it can cause serious infections in newborns, pregnant women, elderly individuals, and people with weakened immune systems. In newborns, GBS can lead to sepsis, pneumonia, and meningitis, which can result in long-term health complications or even be fatal if left untreated.

Pregnant women are often screened for GBS colonization during the third trimester of pregnancy, and those who test positive may receive intrapartum antibiotics to reduce the risk of transmission to their newborns during delivery.

Blood is the fluid that circulates in the body of living organisms, carrying oxygen and nutrients to the cells and removing carbon dioxide and other waste products. It is composed of red and white blood cells suspended in a liquid called plasma. The main function of blood is to transport oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs. It also transports nutrients, hormones, and other substances to the cells and removes waste products from them. Additionally, blood plays a crucial role in the body's immune system by helping to fight infection and disease.

Q fever is a zoonotic disease caused by the bacterium Coxiella burnetii. It is characterized by acute or chronic flu-like symptoms, pneumonia, and hepatitis. The bacteria are primarily transmitted to humans through inhalation of contaminated dust or aerosols from infected animals such as cattle, sheep, and goats. Q fever can also be transmitted through consumption of unpasteurized milk or direct contact with infected animals. It is often asymptomatic or mildly symptomatic in animals but can cause severe disease in humans.

The acute form of Q fever typically presents with sudden onset of high fever, severe headache, fatigue, muscle pain, and cough. Some patients may also develop pneumonia or hepatitis. The chronic form of the disease is less common but more serious, often affecting people with compromised immune systems. Chronic Q fever can lead to endocarditis, an infection of the inner lining of the heart, which can be life-threatening if left untreated.

Diagnosis of Q fever typically involves a combination of clinical evaluation, serological testing, and PCR (polymerase chain reaction) assays. Treatment usually involves antibiotics such as doxycycline or fluoroquinolones for several weeks to months, depending on the severity and duration of the illness. Prevention measures include avoiding contact with infected animals, wearing protective clothing and masks when handling animal products, and pasteurizing milk before consumption.

Fibronectin is a high molecular weight glycoprotein that is found in many tissues and body fluids, including plasma, connective tissue, and the extracellular matrix. It is composed of two similar subunits that are held together by disulfide bonds. Fibronectin plays an important role in cell adhesion, migration, and differentiation by binding to various cell surface receptors, such as integrins, and other extracellular matrix components, such as collagen and heparan sulfate proteoglycans.

Fibronectin has several isoforms that are produced by alternative splicing of a single gene transcript. These isoforms differ in their biological activities and can be found in different tissues and developmental stages. Fibronectin is involved in various physiological processes, such as wound healing, tissue repair, and embryonic development, and has been implicated in several pathological conditions, including fibrosis, tumor metastasis, and thrombosis.

"Pseudomonas aeruginosa" is a medically important, gram-negative, rod-shaped bacterium that is widely found in the environment, such as in soil, water, and on plants. It's an opportunistic pathogen, meaning it usually doesn't cause infection in healthy individuals but can cause severe and sometimes life-threatening infections in people with weakened immune systems, burns, or chronic lung diseases like cystic fibrosis.

P. aeruginosa is known for its remarkable ability to resist many antibiotics and disinfectants due to its intrinsic resistance mechanisms and the acquisition of additional resistance determinants. It can cause various types of infections, including respiratory tract infections, urinary tract infections, gastrointestinal infections, dermatitis, and severe bloodstream infections known as sepsis.

The bacterium produces a variety of virulence factors that contribute to its pathogenicity, such as exotoxins, proteases, and pigments like pyocyanin and pyoverdine, which aid in iron acquisition and help the organism evade host immune responses. Effective infection control measures, appropriate use of antibiotics, and close monitoring of high-risk patients are crucial for managing P. aeruginosa infections.

Staphylococcus is a genus of Gram-positive, facultatively anaerobic bacteria that are commonly found on the skin and mucous membranes of humans and other animals. Many species of Staphylococcus can cause infections in humans, but the most notable is Staphylococcus aureus, which is responsible for a wide range of illnesses, from minor skin infections to life-threatening conditions such as pneumonia, endocarditis, and sepsis.

Staphylococcus species are non-motile, non-spore forming, and typically occur in grape-like clusters when viewed under a microscope. They can be coagulase-positive or coagulase-negative, with S. aureus being the most well-known coagulase-positive species. Coagulase is an enzyme that causes the clotting of plasma, and its presence is often used to differentiate S. aureus from other Staphylococcus species.

These bacteria are resistant to many commonly used antibiotics, including penicillin, due to the production of beta-lactamases. Methicillin-resistant Staphylococcus aureus (MRSA) is a particularly problematic strain that has developed resistance to multiple antibiotics and can cause severe, difficult-to-treat infections.

Proper hand hygiene, use of personal protective equipment, and environmental cleaning are crucial measures for preventing the spread of Staphylococcus in healthcare settings and the community.

IgG receptors, also known as Fcγ receptors (Fc gamma receptors), are specialized protein molecules found on the surface of various immune cells, such as neutrophils, monocytes, macrophages, and some lymphocytes. These receptors recognize and bind to the Fc region of IgG antibodies, one of the five classes of immunoglobulins in the human body.

IgG receptors play a crucial role in immune responses by mediating different effector functions, including:

1. Antibody-dependent cellular cytotoxicity (ADCC): IgG receptors on natural killer (NK) cells and other immune cells bind to IgG antibodies coated on the surface of virus-infected or cancer cells, leading to their destruction.
2. Phagocytosis: When IgG antibodies tag pathogens or foreign particles, phagocytes like neutrophils and macrophages recognize and bind to these immune complexes via IgG receptors, facilitating the engulfment and removal of the targeted particles.
3. Antigen presentation: IgG receptors on antigen-presenting cells (APCs) can internalize immune complexes, process the antigens, and present them to T cells, thereby initiating adaptive immune responses.
4. Inflammatory response regulation: IgG receptors can modulate inflammation by activating or inhibiting downstream signaling pathways in immune cells, depending on the specific type of Fcγ receptor and its activation state.

There are several types of IgG receptors (FcγRI, FcγRII, FcγRIII, and FcγRIV) with varying affinities for different subclasses of IgG antibodies (IgG1, IgG2, IgG3, and IgG4). The distinct functions and expression patterns of these receptors contribute to the complexity and fine-tuning of immune responses in the human body.

Fc receptors (FcRs) are specialized proteins found on the surface of various immune cells, including neutrophils, monocytes, macrophages, eosinophils, basophils, mast cells, and B lymphocytes. They play a crucial role in the immune response by recognizing and binding to the Fc region of antibodies (IgG, IgA, and IgE) after they have interacted with their specific antigens.

FcRs can be classified into several types based on the class of antibody they bind:

1. FcγRs - bind to the Fc region of IgG antibodies
2. FcαRs - bind to the Fc region of IgA antibodies
3. FcεRs - bind to the Fc region of IgE antibodies

The binding of antibodies to Fc receptors triggers various cellular responses, such as phagocytosis, degranulation, and antibody-dependent cellular cytotoxicity (ADCC), which contribute to the elimination of pathogens, immune complexes, and other foreign substances. Dysregulation of Fc receptor function has been implicated in several diseases, including autoimmune disorders and allergies.

Antibodies are proteins produced by the immune system in response to the presence of a foreign substance, such as a bacterium or virus. They are capable of identifying and binding to specific antigens (foreign substances) on the surface of these invaders, marking them for destruction by other immune cells. Antibodies are also known as immunoglobulins and come in several different types, including IgA, IgD, IgE, IgG, and IgM, each with a unique function in the immune response. They are composed of four polypeptide chains, two heavy chains and two light chains, that are held together by disulfide bonds. The variable regions of the heavy and light chains form the antigen-binding site, which is specific to a particular antigen.

An antigen-antibody complex is a type of immune complex that forms when an antibody binds to a specific antigen. An antigen is any substance that triggers an immune response, while an antibody is a protein produced by the immune system to neutralize or destroy foreign substances like antigens.

When an antibody binds to an antigen, it forms a complex that can be either soluble or insoluble. Soluble complexes are formed when the antigen is small and can move freely through the bloodstream. Insoluble complexes, on the other hand, are formed when the antigen is too large to move freely, such as when it is part of a bacterium or virus.

The formation of antigen-antibody complexes plays an important role in the immune response. Once formed, these complexes can be recognized and cleared by other components of the immune system, such as phagocytes, which help to prevent further damage to the body. However, in some cases, the formation of large numbers of antigen-antibody complexes can lead to inflammation and tissue damage, contributing to the development of certain autoimmune diseases.

Immunologic receptors are specialized proteins found on the surface of immune cells that recognize and bind to specific molecules, known as antigens, on the surface of pathogens or infected cells. This binding triggers a series of intracellular signaling events that activate the immune cell and initiate an immune response.

There are several types of immunologic receptors, including:

1. T-cell receptors (TCRs): These receptors are found on the surface of T cells and recognize antigens presented in the context of major histocompatibility complex (MHC) molecules.
2. B-cell receptors (BCRs): These receptors are found on the surface of B cells and recognize free antigens in solution.
3. Pattern recognition receptors (PRRs): These receptors are found inside immune cells and recognize conserved molecular patterns associated with pathogens, such as lipopolysaccharides and flagellin.
4. Fc receptors: These receptors are found on the surface of various immune cells and bind to the constant region of antibodies, mediating effector functions such as phagocytosis and antibody-dependent cellular cytotoxicity (ADCC).

Immunologic receptors play a critical role in the recognition and elimination of pathogens and infected cells, and dysregulation of these receptors can lead to immune disorders and diseases.

I believe there may be some confusion in your question. "Rabbits" is a common name used to refer to the Lagomorpha species, particularly members of the family Leporidae. They are small mammals known for their long ears, strong legs, and quick reproduction.

However, if you're referring to "rabbits" in a medical context, there is a term called "rabbit syndrome," which is a rare movement disorder characterized by repetitive, involuntary movements of the fingers, resembling those of a rabbit chewing. It is also known as "finger-chewing chorea." This condition is usually associated with certain medications, particularly antipsychotics, and typically resolves when the medication is stopped or adjusted.

Bacterial adhesion is the initial and crucial step in the process of bacterial colonization, where bacteria attach themselves to a surface or tissue. This process involves specific interactions between bacterial adhesins (proteins, fimbriae, or pili) and host receptors (glycoproteins, glycolipids, or extracellular matrix components). The attachment can be either reversible or irreversible, depending on the strength of interaction. Bacterial adhesion is a significant factor in initiating biofilm formation, which can lead to various infectious diseases and medical device-associated infections.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Immunoglobulin M (IgM) is a type of antibody that is primarily found in the blood and lymph fluid. It is the first antibody to be produced in response to an initial exposure to an antigen, making it an important part of the body's primary immune response. IgM antibodies are large molecules that are composed of five basic units, giving them a pentameric structure. They are primarily found on the surface of B cells as membrane-bound immunoglobulins (mlgM), where they function as receptors for antigens. Once an mlgM receptor binds to an antigen, it triggers the activation and differentiation of the B cell into a plasma cell that produces and secretes large amounts of soluble IgM antibodies.

IgM antibodies are particularly effective at agglutination (clumping) and complement activation, which makes them important in the early stages of an immune response to help clear pathogens from the bloodstream. However, they are not as stable or long-lived as other types of antibodies, such as IgG, and their levels tend to decline after the initial immune response has occurred.

In summary, Immunoglobulin M (IgM) is a type of antibody that plays a crucial role in the primary immune response to antigens by agglutination and complement activation. It is primarily found in the blood and lymph fluid, and it is produced by B cells after they are activated by an antigen.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Monocytes are a type of white blood cell that are part of the immune system. They are large cells with a round or oval shape and a nucleus that is typically indented or horseshoe-shaped. Monocytes are produced in the bone marrow and then circulate in the bloodstream, where they can differentiate into other types of immune cells such as macrophages and dendritic cells.

Monocytes play an important role in the body's defense against infection and tissue damage. They are able to engulf and digest foreign particles, microorganisms, and dead or damaged cells, which helps to clear them from the body. Monocytes also produce cytokines, which are signaling molecules that help to coordinate the immune response.

Elevated levels of monocytes in the bloodstream can be a sign of an ongoing infection, inflammation, or other medical conditions such as cancer or autoimmune disorders.

Bacterial antigens are substances found on the surface or produced by bacteria that can stimulate an immune response in a host organism. These antigens can be proteins, polysaccharides, teichoic acids, lipopolysaccharides, or other molecules that are recognized as foreign by the host's immune system.

When a bacterial antigen is encountered by the host's immune system, it triggers a series of responses aimed at eliminating the bacteria and preventing infection. The host's immune system recognizes the antigen as foreign through the use of specialized receptors called pattern recognition receptors (PRRs), which are found on various immune cells such as macrophages, dendritic cells, and neutrophils.

Once a bacterial antigen is recognized by the host's immune system, it can stimulate both the innate and adaptive immune responses. The innate immune response involves the activation of inflammatory pathways, the recruitment of immune cells to the site of infection, and the production of antimicrobial peptides.

The adaptive immune response, on the other hand, involves the activation of T cells and B cells, which are specific to the bacterial antigen. These cells can recognize and remember the antigen, allowing for a more rapid and effective response upon subsequent exposures.

Bacterial antigens are important in the development of vaccines, as they can be used to stimulate an immune response without causing disease. By identifying specific bacterial antigens that are associated with virulence or pathogenicity, researchers can develop vaccines that target these antigens and provide protection against infection.

Innate immunity, also known as non-specific immunity or natural immunity, is the inherent defense mechanism that provides immediate protection against potentially harmful pathogens (like bacteria, viruses, fungi, and parasites) without the need for prior exposure. This type of immunity is present from birth and does not adapt to specific threats over time.

Innate immune responses involve various mechanisms such as:

1. Physical barriers: Skin and mucous membranes prevent pathogens from entering the body.
2. Chemical barriers: Enzymes, stomach acid, and lysozyme in tears, saliva, and sweat help to destroy or inhibit the growth of microorganisms.
3. Cellular responses: Phagocytic cells (neutrophils, monocytes, macrophages) recognize and engulf foreign particles and pathogens, while natural killer (NK) cells target and eliminate virus-infected or cancerous cells.
4. Inflammatory response: When an infection occurs, the innate immune system triggers inflammation to increase blood flow, recruit immune cells, and remove damaged tissue.
5. Complement system: A group of proteins that work together to recognize and destroy pathogens directly or enhance phagocytosis by coating them with complement components (opsonization).

Innate immunity plays a crucial role in initiating the adaptive immune response, which is specific to particular pathogens and provides long-term protection through memory cells. Both innate and adaptive immunity work together to maintain overall immune homeostasis and protect the body from infections and diseases.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Kuhlman, M; K Joiner; R A Ezekowitz (1989-05-01). "The human mannose-binding protein functions as an opsonin". The Journal of ... Wang, J Y; C C Shieh; P F You; H Y Lei; K B Reid (August 1998). "Inhibitory effect of pulmonary surfactant proteins A and D on ... Wang, J Y; U Kishore; B L Lim; P Strong; K B Reid (November 1996). "Interaction of human lung surfactant proteins A and D with ... O'Riordan, D M; J E Standing; K Y Kwon; D Chang; E C Crouch; A H Limper (June 1995). "Surfactant protein D interacts with ...
Some proteins hinder opsonin-related ingestion; Staphylococcus aureus produces Protein A to block antibody receptors, which ... and group A streptococci produce proteins such as M protein and fimbrial proteins to block engulfment. ... They include opsonin receptors, scavenger receptors, and Toll-like receptors. Opsonin receptors increase the phagocytosis of ... "Complement" is the name given to a complex series of protein molecules found in the blood that destroy cells or mark them for ...
... a putative opsonin receptor for lung surfactant protein D". Proc. Natl. Acad. Sci. U.S.A. 96 (19): 10794-9. Bibcode:1999PNAS... ... Deleted in malignant brain tumors 1 protein is a protein that in humans is encoded by the DMBT1 gene. Loss of sequences from ... "Human salivary agglutinin binds to lung surfactant protein-D and is identical with scavenger receptor protein gp-340". Biochem ... The DMBT1 protein is a glycoprotein containing multiple scavenger receptor cysteine-rich (SRCR) domains separated by SRCR- ...
Opsonins are normally soluble proteins, which when bound to the surface of a cell induce phagocytes to phagocytose that cell. ... Opsonins include Mfge8, Gas6, Protein S, antibodies and complement factors C1q and C3b. Phagoptosis has multiple functions ... binding of opsonins. It is clear that otherwise-viable cells can expose/bind such phagocytosis-promoting signals as a result of ... binding soluble proteins that tag the cell for phagocytosis. For example, phosphatidylserine is an "eat-me" signal that, when ...
However, there are now known to be at least 50 proteins that act as opsonins for pathogens or other targets. Opsonins induce ... Opsonins help clear pathogens, as well as dead, dying and diseased cells. Opsonins were discovered and named "opsonins" in 1904 ... Opsonins are extracellular proteins that, when bound to substances or cells, induce phagocytes to phagocytose the substances or ... Therefore, Some opsonins (including some complement proteins) have evolved to bind Pathogen-associated molecular patterns, ...
Similar to the complement protein C3 in function, TEP1 acts as an opsonin which facilitates extensive parasite killing. TEP1 ... TEP1 interacts with a heterodimeric protein complex made up of two leucine-rich repeat (LRR) domain containing proteins: ... The cleaved protein is known as TEP1-cut and represents the activated form. This mechanism is equivalent to the maturation of ... The TEP1 protein is glycosylated and secreted into the body cavity by mosquito immune cells as a 165 kDa zymogen - this ...
... opsonin proteins MeSH D12.776.377.715.548.114.820 - plantibodies MeSH D12.776.377.715.548.114.837 - precipitins MeSH D12.776. ... groel protein MeSH D12.776.602.500.500.100 - fusion proteins, bcr-abl MeSH D12.776.602.500.500.320 - fusion proteins, gag-onc ... oncogene protein v-maf MeSH D12.776.964.700.750.875 - oncogene proteins v-abl MeSH D12.776.964.700.750.882 - oncogene proteins ... fusion proteins, gag-pol MeSH D12.776.964.775.350.400 - hiv core protein p24 MeSH D12.776.964.775.375.325 - fusion proteins, ...
... opsonin proteins MeSH D12.776.124.486.485.114.820 - plantibodies MeSH D12.776.124.486.485.114.837 - precipitins MeSH D12.776. ... opsonin proteins MeSH D12.776.124.790.651.114.820 - plantibodies MeSH D12.776.124.790.651.114.837 - precipitins MeSH D12.776. ... complement c1 inactivator proteins MeSH D12.776.124.486.274.920.250.500 - complement c1 inhibitor protein MeSH D12.776.124.486. ... bence jones protein MeSH D12.776.124.486.485.900.225 - cryoglobulins MeSH D12.776.124.486.485.900.500 - myeloma proteins MeSH ...
... forming a blood clot that stops bleeding C-reactive protein, opsonin on microbes, acute phase protein Various other globulins ... The liver plays the major role in producing proteins that are secreted into the blood, including major plasma proteins, factors ... All plasma proteins except Gamma-globulins are synthesised in the liver. Human serum albumin, osmolyte and carrier protein α- ... Vitamin D-binding protein, carries vitamin D FGF21, a protein hormone that induces mitochondrial oxidation of fatty acids, ...
September 1999). "Cloning of gp-340, a putative opsonin receptor for lung surfactant protein D". Proceedings of the National ... Surfactant protein D, also known as SP-D, is a lung surfactant protein part of the collagenous family of proteins called ... "Microfibril-associated protein 4 is present in lung washings and binds to the collagen region of lung surfactant protein D". ... Surfactant+Protein+D at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles with short ...
"Complement proteins bind to nanoparticle protein corona and undergo dynamic exchange in vivo". Nature Nanotechnology. 12 (4): ... "Study: How to keep nanoparticle caterpillars safe from the crows of the immune system". EurekAlert!. "Opsonins and Dysopsonins ... Resulting from his PhD research, Moghimi introduced the opsonin-dysopsonin hypothesis, suggesting a regulatory role for certain ... a polymer that is used widely for prolonging the blood circulation time of proteins and particulate drug carriers. His lab was ...
In addition, merely around 50 amino acids (the fibronogen-like domain) align with any known protein, specifically the ficolin ... Tunicate intelectin is an opsonin for phagocytosis by hemocyte. Amphioxus intelectin has been shown to agglutinate bacteria. In ... Intelectins are lectins (carbohydrate-binding proteins) expressed in humans and other chordates. Humans express two types of ... Genes on human chromosome 1, Pages using gallery with unknown parameters, Lectins, Glycobiology, Immune system, Protein ...
Clustered Band 3 proteins with attached antibodies activate complement, and complement C3 fragments are opsonins recognized by ... The fusion proteins were a way to spread the infection to other cells by simply merging them with the infected one (HIV does ... Also, viral fusion proteins cause the formation of the placental syncytium to limit exchange of migratory cells between the ... One of the pathways is siRNA in which long double stranded RNA is cut into pieces that serve as templates for protein complex ...
It is thought to assist in complement binding to foreign and damaged cells and enhances phagocytosis by macrophages (opsonin- ... CAA39671". NCBI Entrez Protein. "Human C-reactive protein complexed with phosphocholine". Protein Data Bank in Europe. Enocsson ... C-reactive protein (CRP) is an annular (ring-shaped) pentameric protein found in blood plasma, whose circulating concentrations ... C-reactive protein C-reactive protein GRCh38: Ensembl release 89: ENSG00000132693 - Ensembl, May 2017 GRCm38: Ensembl release ...
... hence opsonins tend to enhance macrophages' phagocytic activity. Both complement proteins and antibodies can bind to antigens ... For example, IL-2 signaling in T cells upregulates the expression of anti-apoptotic protein Bcl-2, but T cell production of IL- ... They can be identified using flow cytometry or immunohistochemical staining by their specific expression of proteins such as ... Opsonins can cause a stronger adhesion between the macrophage and pathogen during phagocytosis, ...
It was found that when opsonins, like fibrinogen, are numerous in the protein corona, the proteins tend to induce macrophage ... In "soft" protein coronas, it is common to observe an exchange of proteins at the surface; larger proteins with lower ... pH can alter protein binding affinity in protein-nanoparticle interactions, thus modifying the adsorbed protein pattern at the ... This process is governed by the intermolecular protein-nanoparticle and protein-protein interactions that exist within a ...
... protein A renders them inaccessible to the opsonins, thus impairing phagocytosis of the bacteria via immune cell attack. ... In addition to protein A, other immunoglobulin-binding bacterial proteins such as Protein G, Protein A/G and Protein L are all ... Immunoprecipitation studies with protein A conjugated to beads are also commonly used to purify proteins or protein complexes ... Protein A is a 42 kDa surface protein originally found in the cell wall of the bacteria Staphylococcus aureus. It is encoded by ...
... and other proteins. They also express receptors to detect and adhere to endothelium and Fc receptors for opsonin. In leukocytes ... For targets to be recognized, they must be coated in opsonins - a process known as antibody opsonization. They can internalize ... Neutrophils also release an assortment of proteins in three types of granules by a process called degranulation. The contents ... October 2009). "Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense ...
... the MASP protein functions to cleave the blood protein C4 into C4a and C4b. The C4b fragments can then bind to the surface of ... is a lectin that is instrumental in innate immunity as an opsonin and via the lectin pathway. MBL has an oligomeric structure ( ... "Mannose-binding protein C precursor [Homo sapiens]". Retrieved 2012-01-03. Jensen PH, Laursen I, Matthiesen F, Højrup P (2007 ... It is produced in the liver as a response to infection, and is part of many other factors termed acute phase proteins. ...
The protein encoded by this gene is a thermolabile beta-2-macroglycoprotein found in all human serum and is a member of the ... ficolin/opsonin p35 lectin family. The protein, which was initially identified based on its reactivity with sera from patients ... The protein can activate the complement pathway in association with MASPs and sMAP, thereby aiding in host defense through the ... Ficolin-3 is a protein that in humans is encoded by the FCN3 gene. Ficolin-3 was initially identified as H-ficolin, in which H ...
Due to their positive charge, cationic liposomes bind to various plasma proteins, forming a protein corona on their surface and ... This new biological identity then causes opsonins to tag them as pathogens and encourages clearance through phagocytic ... This positive charge can also create some issues in vivo, such as binding to plasma proteins in the bloodstream, which leads to ... acting as a protective layer and reducing the formation of a protein corona. The presence of PEG on the surface of the liposome ...
... is a protein fragment that is part of the complement system, a component of the vertebrate immune system. iC3b is produced ... Complement receptors on white blood cells are able to bind iC3b, so iC3b functions as an opsonin. Unlike intact C3b, iC3b ... Complement factor I can further cleave iC3b into a protein fragment known as C3d. Robbins Basic Pathology 8th ed 2007. R Cotran ...
... creating a more hostile environment for pathogens and facilitating protein degradation. The bacterial proteins are denatured in ... Opsonins are molecular tags such as antibodies and complements that attach to pathogens and up-regulate phagocytosis. ... Other proteins such as Toll-like receptors are involved in pathogen pattern recognition and are often recruited to phagosomes ... The two proteins, along with Rho GTPases, are important components of the innate immune response, inducing cytokine production ...
These globular regions of C1q can also bind to bacterial and viral surface proteins, apoptotic cells, and acute phase proteins ... C3b can act as an opsonin . C3b is very similar to C4 in both structure and function also has a thioester bond that forces it ... C2a diffuses into the plasma as a protein inflammatory mediator while C2b remains attached with C4b forming C4bC2b what is ... The classical complement pathway can be initiated by the binding of antigen-antibody complexes to the C1q protein. The globular ...
Ficolin-2, which was initially identified as L-ficolin, is a protein that in humans is encoded by the FCN2 gene. The product of ... 1996). "A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin". J. Biol. Chem. 271 ... 1997). "Purification and binding properties of a human ficolin-like protein". J. Immunol. Methods. 204 (1): 43-9. doi:10.1016/ ... Edgar PF (1996). "Hucolin, a new corticosteroid-binding protein from human plasma with structural similarities to ficolins, ...
Ficolin-1, and also commonly termed M-ficolin is a protein that in humans is encoded by the FCN1 gene. Proteins of the ficolin ... 1996). "A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin". J. Biol. Chem. 271 ... The collagen-like and the fibrinogen-like domains are also found in other proteins such as tenascins, while the former is also ... 2004). "The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan- ...
... (SAA1) is a protein that in humans is encoded by the SAA1 gene. SAA1 is a major acute-phase protein mainly ... Shah C, Hari-Dass R, Raynes JG (Sep 2006). "Serum amyloid A is an innate immune opsonin for Gram-negative bacteria". Blood. 108 ... Hari-Dass R, Shah C, Meyer DJ, Raynes JG (May 2005). "Serum amyloid A protein binds to outer membrane protein A of gram- ... In addition to its association with HDL, SAA1 interacts with a number of mammalian proteins, mostly cell surface proteins such ...
Surfactant protein A (SP-A) Surfactant protein D (SP-D) CL-L1 CL-P1 CL-K1 Peptidoglycan recognition proteins (PGRPs) PGLYRP1 ... signal sequences Junctional diversity Immunoglobulin class switching Allelic exclusion Polyclonal response Phagocytosis Opsonin ... Royet J, Gupta D, Dziarski R (December 2011). "Peptidoglycan recognition proteins: modulators of the microbiome and ... proteins Amyloid SAP SAA Positive Alpha 1-antichymotrypsin Alpha 1-antitrypsin Alpha 2-macroglobulin C-reactive protein ...
The recognition and clearance of invading microorganisms occurs through both opsonin-dependent and opsonin-independent pathways ... protein kinase A (PKA) and the exchange proteins directly activated by cAMP (Epac-1 and -2). Epac-1 and PKA are both important ... The molecular mechanisms facilitating opsonin-dependent phagocytosis are different for specific opsonin/receptor pairs. For ... The latent complex is covalently linked to the extracellular matrix by binding to latent TGF-β-binding proteins. TGF-β is ...
Pentraxin-related protein PTX3 also known as TNF-inducible gene 14 protein (TSG-14) is a protein that in humans is encoded by ... "PTX3 function as an opsonin for the dectin-1-dependent internalization of zymosan by macrophages". Journal of Leukocyte Biology ... the amino-terminal domain and the pentraxin domain of the protein. The transcribed PTX3 protein is 381 amino acids long, has a ... "Relationship of TSG-14 protein to the pentraxin family of major acute phase proteins". Journal of Immunology. 153 (8): 3700-7. ...
Kuhlman, M; K Joiner; R A Ezekowitz (1989-05-01). "The human mannose-binding protein functions as an opsonin". The Journal of ... Wang, J Y; C C Shieh; P F You; H Y Lei; K B Reid (August 1998). "Inhibitory effect of pulmonary surfactant proteins A and D on ... Wang, J Y; U Kishore; B L Lim; P Strong; K B Reid (November 1996). "Interaction of human lung surfactant proteins A and D with ... ORiordan, D M; J E Standing; K Y Kwon; D Chang; E C Crouch; A H Limper (June 1995). "Surfactant protein D interacts with ...
In the case of many viruses, resistance is related to the presence on the cell surface of protein receptors that bind to the ... An opsonin generally is a protein substance, such as one of the circulating immunoglobulins or complement components. ... In the case of many viruses, resistance is related to the presence on the cell surface of protein receptors that bind to the ... Ingestion of bacteria may require the help of still other components of the blood, called opsonins, which act to coat the ...
The plasma proteins contribute proteases and opsonins to combat infection. The liver is an important innate immune organ that ... mannose binding protein, complement factors, ferritin, serum amyloid A and P, and surfactant proteins[11,12]. All acute ... CINC-1 is an acute-phase protein induced by focal brain injury causing leukocyte mobilization and liver injury. FASEB J. 2003; ... Relation of endotoxin, endotoxin binding proteins and macrophages to severe alcoholic liver injury and multiple organ failure. ...
NE inhibits innate immune function by digesting opsonins and opsonin receptors, degrading innate immune proteins such as ... Proteins are shown using a "sausage" cartoon representation where the thickness of the tube indicates the B-factor. The color ... Proteins are shown using a "sausage" cartoon representation where the thickness of the tube indicates the B-factor. The color ... The N-terminal domain of Bacillus subtilis RNase Y (Nter-BsRNaseY) is thought to interact with various protein partners within ...
... nonspecific antimicrobial proteins and opsonins, and normal relatively nonpathogenic airway flora. Anatomic structures of the ... as well as surfactant-associated proteins A (Sp-A) and D (Sp-D). Both of these latter proteins can modulate phagocytosis, ... The role of inter-alpha inhibitor proteins in the diagnosis of neonatal sepsis. J Pediatr. 2009 Apr. 154(4):620-622.e1. [QxMD ... The alveoli do not contain a significant exudate, but protein-rich hyaline membranes similar to those found in adult ...
One factor is the low content of protective proteins (opsonins) normally present in peritoneal fluid of a person with normal ... Most cases are also positive for cytotoxic proteins such as granzyme B, TIA-1, and perforin. T-cell receptor gene rearrangement ... Evaluation of the fluid requires gross examination, protein estimation, total cell count, differential cell count, Gram stain, ... S-100 protein, HMB45, and CD45 should be performed when suspicion for a non-epithelial malignant effusion exists.[17] Once a ...
Opsonin Proteins Medicine & Life Sciences 100% * Urochordata Medicine & Life Sciences 96% * Phagocytosis Medicine & Life ... N2 - Opsonins play a key role in invertebrate humoral immune systems. An opsonin for yeast was identified in the plasma of the ... AB - Opsonins play a key role in invertebrate humoral immune systems. An opsonin for yeast was identified in the plasma of the ... Opsonins play a key role in invertebrate humoral immune systems. An opsonin for yeast was identified in the plasma of the ...
... of Txnip degradation by pharmacologically inhibiting the HECT E3 ubiquitin ligase with heclin and AMP-dependent protein kinase ... Thioredoxin-interacting protein (Txnip) inhibits the activity of thioredoxin (Trx) to modulate inflammatory responses. The ... Thioredoxin-interacting protein (Txnip) inhibits the activity of thioredoxin (Trx) to modulate inflammatory responses. The ... of Txnip degradation by pharmacologically inhibiting the HECT E3 ubiquitin ligase with heclin and AMP-dependent protein kinase ...
... which is a major opsonin of the complement system. Deficiency in factor I activity is associated with an increased incidence of ... Complement factor I is a serine protease present in human plasma that is involved in the degradation of complement protein C3b ... Degradation of C3b by fI abrogates the action of this protein in the C3 pathway [27]. Complement C3b is the major opsonin of ... C4b-binding protein CR1 and membrane cofactor protein (MCP) [26]. Factor I-mediated cleavage of the α chain of C3b liberates 3 ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonins. Opsonin Proteins. Protein p16. Cyclin-Dependent Kinase Inhibitor p16. Protein p53. Tumor Suppressor Protein p53. ... Proto-Oncogene Protein c-met. Proto-Oncogene Proteins c-met. Proto-Oncogene Protein p21(ras). Proto-Oncogene Proteins p21(ras) ... Proto-Oncogene Protein pp60(c-src). Proto-Oncogene Proteins pp60(c-src). ... Proto-Oncogene Protein c-kit. Proto-Oncogene Proteins c-kit. ... Heat-Shock Proteins 90. HSP90 Heat-Shock Proteins. I-kappa B. I ...
Opsonin Proteins *Plantibodies *Precipitins *Reagins [71094] References:. Maloney DG. "Anti-CD20 antibody therapy for B-cell ... In our body, Interferon is a family of small intercellular signaling proteins, as cytokines, are released by cells in response ... to a wide variety of inducers including viral infections, that activate the synthesis and secretion of antiviral proteins. In ...
STTR Phase I: Designer peptide opsonins against COVID-19. Dodd-o, J., Heffernan, C., Acevedo-Jake, A. M., Dave, R. & Kumar, V. ...
Cloning of gp-340, a putative opsonin receptor for lung surfactant protein D Madsen, J, Poustka, A, Kliem, A, Reid, KB, ... Human salivary agglutinin binds to lung surfactant protein-D and is identical with scavenger receptor protein gp-340 Groenink, ... Deleted in malignant brain tumors 1 protein (DMBT1 aka Gp-340, Hensin, salivary agglutinin) is a binding protein that could ... Metabolism of proteins (Homo sapiens) * * Surfactant metabolism (Homo sapiens) * DMBT1 binds SFTPD 12mer, SFTPAs (Homo sapiens) ...
Recently it has been shown that [mannan-binding protein (MBP)]? is the main opsonin in the human blood serum. This was ... The proteins account for 5% of the serum globulin fraction. Most of these proteins circulate as zymogens, which are inactive ... It does not rely on a pathogen-binding protein like the other pathways. In the alternative pathway, C3 is split into C3a and ... The lectin pathway is homologous to the classical pathway, but with the opsonin, [mannan-binding lectin (MBL)]? and ficolins, ...
... and lower absorbed opsonin proteins compared with the conventional liposomes. Compared to TP-loaded traditional liposomes (TP/ ... in which FGel provided a protein scaffold to mimic snail mucus proteins, while GL mimicked the adhesion and bioactivity of ... In the biosynthesis of glycyrrhizin, both gene and protein levels of bAS and CYP88D6 have been found with upregulated ... Single-point mutation into cysteine enabled the thiol-maleimide reaction and site-specific protein assembly using a two-arm ...
Opsonins from the complement cascade include C1q, C3b, and C4b. Additional important opsonins include mannose-binding proteins ... Acute-Phase Proteins. The acute-phase proteins are another class of antimicrobial mediators. Acute-phase proteins are primarily ... Additional proteins found in blood plasma, such as acute-phase proteins, complement proteins, and cytokines, are involved in ... Plasma protein mediators. Acute-phase proteins (C-reactive protein, serum amyloid A, ferritin, fibrinogen, transferrin, and ...
"Our cloaking strategy prevents the binding of opsonins - signaling proteins that activate the immune system," Tasciotti said. " ... The proteins that give us the greatest advantages are already within the membrane and we can use it as-is." ... "We accomplished this with the lipids and proteins present on the membrane of the very same cells of the immune system. We ... "We compared the absorption of proteins onto the surface of uncoated and coated particles to see how the particles might evade ...
Herein, we review the role of glycans and glycan-binding proteins as essential components of the cell death machinery during ... Glycans, either alone or complexed with glycan-binding proteins, can deliver intracellular signals or control extracellular ... CRT acts as a coreceptor for opsonin C1q and as an endocytic pattern recognition receptor on macrophages.98 Similarly, soluble ... The cargo proteins, mannosidase-like protein (EDEM) in the ER and hydrolase α-mannosidase, as well as accumulation of N-glycans ...
... cellular processes may be triggered depending upon which proteins are adsorbed to the surface (e.g., as opsonins) and their ... Early-arriving proteins may be partially or wholly displaced by later-arriving proteins that have a greater affinity for the ... M. Sprintz notes that the binding of plasma proteins has relevance to the displacement of other highly protein-bound drugs, ... With many hundreds of plasma proteins (the predominant plasma protein is albumin) to choose from, unmodified implanted devices ...
Among the different complement proteins, the opsonins C3 and C4 have a protector thioester radical. This molecule allows the C4 ... Description and applications: Claudin proteins are a family of proteins associated with tight junctions. Tight junctions are ... Secreted Protein Acidic and Rich in Cysteine), osteonectin, or BM-40 (Basement Membrane Protein 40). It is a multifunctional ... BLR1, a G protein coupled receptor originally isolated from Burkitts lymphoma cells, has now been shown to be the specific ...

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