Mannose-Binding Lectin
Collectins
Complement Pathway, Mannose-Binding Lectin
Mannose
Mannose-Binding Lectins
Lectins
Genotype
Polymorphism, Genetic
Galectins
Genetic Predisposition to Disease
Plant Lectins
Mannose-Binding Protein-Associated Serine Proteases
Carrier Proteins
Galectin 3
Complement C1q
Molecular Sequence Data
Genetic characterization of a new type IV-A pilus gene cluster found in both classical and El Tor biotypes of Vibrio cholerae. (1/496)
The Vibrio cholerae genome contains a 5.4-kb pil gene cluster that resembles the Aeromonas hydrophila tap gene cluster and other type IV-A pilus assembly operons. The region consists of five complete open reading frames designated pilABCD and yacE, based on the nomenclature of related genes from Pseudomonas aeruginosa and Escherichia coli K-12. This cluster is present in both classical and El Tor biotypes, and the pilA and pilD genes are 100% conserved. The pilA gene encodes a putative type IV pilus subunit. However, deletion of pilA had no effect on either colonization of infant mice or adherence to HEp-2 cells, demonstrating that pilA does not encode the primary subunit of a pilus essential for these processes. The pilD gene product is similar to other type IV prepilin peptidases, proteins that process type IV signal sequences. Mutational analysis of the pilD gene showed that pilD is essential for secretion of cholera toxin and hemagglutinin-protease, mannose-sensitive hemagglutination (MSHA), production of toxin-coregulated pili, and colonization of infant mice. Defects in these functions are likely due to the lack of processing of N termini of four Eps secretion proteins, four proteins of the MSHA cluster, and TcpB, all of which contain type IV-A leader sequences. Some pilD mutants also showed reduced adherence to HEp-2 cells, but this defect could not be complemented in trans, indicating that the defect may not be directly due to a loss of pilD. Taken together, these data demonstrate the effectiveness of the V. cholerae genome project for rapid identification and characterization of potential virulence factors. (+info)A role for the mannose-sensitive hemagglutinin in biofilm formation by Vibrio cholerae El Tor. (2/496)
While much has been learned regarding the genetic basis of host-pathogen interactions, less is known about the molecular basis of a pathogen's survival in the environment. Biofilm formation on abiotic surfaces represents a survival strategy utilized by many microbes. Here it is shown that Vibrio cholerae El Tor does not use the virulence-associated toxin-coregulated pilus to form biofilms on borosilicate but rather uses the mannose-sensitive hemagglutinin (MSHA) pilus, which plays no role in pathogenicity. In contrast, attachment of V. cholerae to chitin is shown to be independent of the MSHA pilus, suggesting divergent pathways for biofilm formation on nutritive and nonnutritive abiotic surfaces. (+info)Steps in the development of a Vibrio cholerae El Tor biofilm. (3/496)
We report that, in a simple, static culture system, wild-type Vibrio cholerae El Tor forms a three-dimensional biofilm with characteristic water channels and pillars of bacteria. Furthermore, we have isolated and characterized transposon insertion mutants of V. cholerae that are defective in biofilm development. The transposons were localized to genes involved in (i) the biosynthesis and secretion of the mannose-sensitive haemagglutinin type IV pilus (MSHA); (ii) the synthesis of exopolysaccharide; and (iii) flagellar motility. The phenotypes of these three groups suggest that the type IV pilus and flagellum accelerate attachment to the abiotic surface, the flagellum mediates spread along the abiotic surface, and exopolysaccharide is involved in the formation of three-dimensional biofilm architecture. (+info)Lectin-carbohydrate interactions: fine specificity difference between two mannose-binding proteins. (4/496)
Two types of rat mannose-binding proteins (MBPs), MBP-A (serum type) and MBP-C (liver type), have similar binding specificity for monosaccharide and similar binding site construct according to the X-ray structure, but exhibit different affinity toward natural oligosaccharides and glycoproteins. To understand the basis for this phenomenon, we used cloned fragment of MBP-A and -C (entire carbohydrate-recognition domain and a short connecting piece) that exists as stable trimers in various binding studies. Binding of a number of mannose-containing di- and tri-saccharides and high-mannose type oligosaccharides indicated that MBP-C has an extended binding area of weak interaction with the second and the third mannose residues, whereas MBP-A recognizes just a single mannose residue. In addition, MBP-C has a weak secondary binding site some 25 A away from the primary site. These findings explain the higher affinity of MBP-C for natural high-mannose type oligosaccharides as compared to MBP-A. A huge affinity differential manifested by natural glycoproteins (e.g., inhibitory potency of thyroglobulin is approximately 200 fold higher for MBP-C than for MBP-A in a solid-phase assay) may be due to steric hindrance experienced by MBP-A in the competition assay, and suggests different arrangement of subunit in the MBP trimers. (+info)Localization and topology of ratp28, a member of a novel family of putative steroid-binding proteins. (5/496)
We have cloned ratp28, a membrane protein from rat liver homologous to the previously described hpr6.6, a putative steroid-binding protein in humans. Ratp28 has a type II topology as determined by protease digestion experiments on intact and detergent-solubilized membranes. Subcellular fractionation by sucrose density centrifugation revealed a distribution for ratp28 identical to Bip as a marker for membranes of the endoplasmic reticulum. In these experiments no association was found with markers for Golgi or plasma membranes, indicating that ratp28 is localized to the endoplasmic reticulum. (+info)Rat mannose-binding protein a binds CD14. (6/496)
Lipopolysaccharide (LPS) has been known to induce inflammation by interacting with CD14, which serves as a receptor for LPS. Mannose-binding protein (MBP) belongs to the collectin subgroup of the C-type lectin superfamily, along with surfactant proteins SP-A and SP-D. We have recently demonstrated that SP-A modulates LPS-induced cellular responses by interaction with CD14 (H. Sano, H. Sohma, T. Muta, S. Nomura, D. R. Voelker, and Y. Kuroki, J. Immunol. 163:387-395, 2000) and that SP-D also interacts with CD14 (H. Sano, H. Chiba, D. Iwaki, H. Sohma, D. R. Voelker, and Y. Kuroki, J. Biol. Chem. 275:22442-22451, 2000). In this study, we examined whether MBP, a collectin highly homologous to SP-A and SP-D, could bind CD14. Recombinant rat MBP-A bound recombinant human soluble CD14 in a concentration-dependent manner. Its binding was not inhibited in the presence of excess mannose or EDTA. MBP-A bound deglycosylated CD14 treated with N-glycosidase F, neuraminidase, and O-glycosidase, indicating that MBP-A interacts with the peptide portion of CD14. Since LPS was also a ligand for the collectins, we compared the characteristics of binding of MBP-A to LPS with those of binding to CD14. MBP-A bound to lipid A from Salmonella enterica serovar Minnesota and rough LPS (S. enterica serovar Minnesota Re595 and Escherichia coli J5, Rc), but not to smooth LPS (E. coli O26:B6 and O111:B4). Unlike CD14 binding, EDTA and excess mannose attenuated the binding of MBP-A to rough LPS. From these results, we conclude that CD14 is a novel ligand for MBP-A and that MBP-A utilizes a different mechanism for CD14 recognition from that for LPS. (+info)Polymorphisms in the MBL2 promoter correlated with risk of HIV-1 vertical transmission and AIDS progression. (7/496)
We investigated the polymorphisms of the promoter region of the MBL2 gene, which codifies for the Mannose-binding protein (MBP). The study population included 90 children with vertically acquired HIV-infection, further divided on the basis of the disease rate, 27 HIV exposed-uninfected children, and 74 healthy control subjects matched for ethnic origin to evaluate the MBP involvement in the risk of HIV-1 infection and to assess the role of the MBP promoter in AIDS progression. A region of 380 bp in the promoter of the MBL2 gene was analysed by PCR and direct sequencing of both DNA strands. We found that the polymorphism at position -550 influences the risk of HIV-infection and AIDS progression. Also a 6 bp deletion at position -328 was correlated with HIV-1 infection. This study indicates that the promoter of the MBL2 gene influences vertical transmission of HIV and the course of perinatal infection. (+info)Conformational disorder of proteins assessed by real-space molecular dynamics refinement. (8/496)
Motion is critical to the function of many proteins, but much more difficult to study than structure. Due to lack of easy alternatives, although there are inherent limitations, there have been several prior attempts to extract some information from the Bragg scattering in conventional diffraction patterns. Bragg diffraction reflects only a small proportion of a protein's motion and disorder, so fitted values likely underestimate reality. However, this work shows that the fitted estimates should be even smaller, because current methods of refinement over-fit the Bragg diffraction, leading to a component of the disorder that is not based on any experimental data, and could be characterized as a guess. Real-space refinement is less susceptible than other methods, but its application depends on the availability of very accurate experimental phases. A future challenge will be the collection of such data without resort to cryo-techniques, so that a physiologically relevant understanding can be achieved. (+info)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.
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.
The Mannose-Binding Lectin (MBL) pathway is a part of the complement system, which is a group of proteins that play a crucial role in the body's immune defense against infectious agents. The MBL pathway is an alternative activation pathway of the complement system, which can be initiated without the need for antibodies.
MBL is a protein found in blood plasma and other bodily fluids. It recognizes and binds to specific sugars (mannose and fucose) found on the surface of many microorganisms, including bacteria, viruses, fungi, and parasites. When MBL binds to these sugars, it triggers a series of proteolytic cleavage events that activate the complement components C4 and C2, forming the C3 convertase (C4b2a).
The C3 convertase then cleaves the complement component C3 into C3a and C3b. C3b can bind to the surface of microorganisms, leading to their opsonization (coating) and subsequent phagocytosis by immune cells. Additionally, C3b can also trigger the formation of the membrane attack complex (MAC), which creates a pore in the membrane of microorganisms, leading to their lysis and death.
Overall, the MBL pathway plays an essential role in innate immunity, providing a rapid and effective defense against invading microorganisms.
Mannose is a simple sugar (monosaccharide) that is similar in structure to glucose. It is a hexose, meaning it contains six carbon atoms. Mannose is a stereoisomer of glucose, meaning it has the same chemical formula but a different structural arrangement of its atoms.
Mannose is not as commonly found in foods as other simple sugars, but it can be found in some fruits, such as cranberries, blueberries, and peaches, as well as in certain vegetables, like sweet potatoes and turnips. It is also found in some dietary fibers, such as those found in beans and whole grains.
In the body, mannose can be metabolized and used for energy, but it is also an important component of various glycoproteins and glycolipids, which are molecules that play critical roles in many biological processes, including cell recognition, signaling, and adhesion.
Mannose has been studied as a potential therapeutic agent for various medical conditions, including urinary tract infections (UTIs), because it can inhibit the attachment of certain bacteria to the cells lining the urinary tract. Additionally, mannose-binding lectins have been investigated for their potential role in the immune response to viral and bacterial infections.
Mannose-binding lectins (MBLs) are a group of proteins that belong to the collectin family and play a crucial role in the innate immune system. They are primarily produced by the liver and secreted into the bloodstream. MBLs have a specific affinity for mannose sugar residues found on the surface of various microorganisms, including bacteria, viruses, fungi, and parasites.
The primary function of MBLs is to recognize and bind to these mannose-rich structures, which triggers the complement system's activation through the lectin pathway. This process leads to the destruction of the microorganism by opsonization (coating the microbe to enhance phagocytosis) or direct lysis. MBLs also have the ability to neutralize certain viruses and inhibit the replication of others, further contributing to their antimicrobial activity.
Deficiencies in MBL levels or function have been associated with an increased susceptibility to infections, particularly in children and older adults. However, the clinical significance of MBL deficiency remains a subject of ongoing research.
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.
Genotype, in genetics, refers to the complete heritable genetic makeup of an individual organism, including all of its genes. It is the set of instructions contained in an organism's DNA for the development and function of that organism. The genotype is the basis for an individual's inherited traits, and it can be contrasted with an individual's phenotype, which refers to the observable physical or biochemical characteristics of an organism that result from the expression of its genes in combination with environmental influences.
It is important to note that an individual's genotype is not necessarily identical to their genetic sequence. Some genes have multiple forms called alleles, and an individual may inherit different alleles for a given gene from each parent. The combination of alleles that an individual inherits for a particular gene is known as their genotype for that gene.
Understanding an individual's genotype can provide important information about their susceptibility to certain diseases, their response to drugs and other treatments, and their risk of passing on inherited genetic disorders to their offspring.
Genetic polymorphism refers to the occurrence of multiple forms (called alleles) of a particular gene within a population. These variations in the DNA sequence do not generally affect the function or survival of the organism, but they can contribute to differences in traits among individuals. Genetic polymorphisms can be caused by single nucleotide changes (SNPs), insertions or deletions of DNA segments, or other types of genetic rearrangements. They are important for understanding genetic diversity and evolution, as well as for identifying genetic factors that may contribute to disease susceptibility in humans.
Galectins are a family of animal lectins (carbohydrate-binding proteins) that bind specifically to beta-galactosides. They play important roles in various biological processes, including inflammation, immune response, cancer progression, and development. Galectins are widely distributed in various tissues and organ systems, and they can be found both intracellularly and extracellularly.
There are 15 known mammalian galectins, which are classified into three groups based on their structure: prototype (Gal-1, -2, -5, -7, -10, -13, -14, and -16), chimera-type (Gal-3), and tandem-repeat type (Gal-4, -6, -8, -9, and -12). Each galectin has a unique set of functions, but they often work together to regulate cellular processes.
Abnormal expression or function of galectins has been implicated in various diseases, including cancer, fibrosis, and autoimmune disorders. Therefore, galectins are considered potential targets for the development of new therapeutic strategies.
Genetic predisposition to disease refers to an increased susceptibility or vulnerability to develop a particular illness or condition due to inheriting specific genetic variations or mutations from one's parents. These genetic factors can make it more likely for an individual to develop a certain disease, but it does not guarantee that the person will definitely get the disease. Environmental factors, lifestyle choices, and interactions between genes also play crucial roles in determining if a genetically predisposed person will actually develop the disease. It is essential to understand that having a genetic predisposition only implies a higher risk, not an inevitable outcome.
Plant lectins are proteins or glycoproteins that are abundantly found in various plant parts such as seeds, leaves, stems, and roots. They have the ability to bind specifically to carbohydrate structures present on cell membranes, known as glycoconjugates. This binding property of lectins is reversible and non-catalytic, meaning it does not involve any enzymatic activity.
Lectins play several roles in plants, including defense against predators, pathogens, and herbivores. They can agglutinate red blood cells, stimulate the immune system, and have been implicated in various biological processes such as cell growth, differentiation, and apoptosis (programmed cell death). Some lectins also exhibit mitogenic activity, which means they can stimulate the proliferation of certain types of cells.
In the medical field, plant lectins have gained attention due to their potential therapeutic applications. For instance, some lectins have been shown to possess anti-cancer properties and are being investigated as potential cancer treatments. However, it is important to note that some lectins can be toxic or allergenic to humans and animals, so they must be used with caution.
Mannose-binding protein-associated serine proteases (MASPs) are a group of enzymes that are associated with mannose-binding lectin (MBL), a protein involved in the innate immune system's response to pathogens. MASPs are responsible for activating the complement system, which is a part of the immune system that helps to eliminate pathogens and damaged cells from the body.
MASPs are proteases, meaning they cleave other proteins at specific sites. There are two main types of MASPs, MASP-1 and MASP-2, which are activated by the binding of MBL to carbohydrate structures on the surface of pathogens. Once activated, MASP-1 and MASP-2 cleave complement components C4 and C2, leading to the formation of the C3 convertase enzyme complex, which ultimately results in the activation of the complement system.
MASPs have also been shown to play a role in other physiological processes, such as tissue remodeling and inflammation. Mutations in MASP genes have been associated with various immune disorders, including recurrent infections, autoimmune diseases, and inflammatory conditions.
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.
Galectin-3 is a type of protein belonging to the galectin family, which binds to carbohydrates (sugars) and plays a role in various biological processes such as inflammation, immune response, and cancer. It is also known as Mac-2 binding protein or LGALS3.
Galectin-3 is unique among galectins because it can form oligomers (complexes of multiple subunits) and has a wide range of functions in the body. It is involved in cell adhesion, proliferation, differentiation, apoptosis (programmed cell death), and angiogenesis (formation of new blood vessels).
In the context of disease, Galectin-3 has been implicated in several pathological conditions such as fibrosis, heart failure, and cancer. High levels of Galectin-3 have been associated with poor prognosis in patients with heart failure, and it is considered a potential biomarker for this condition. In addition, Galectin-3 has been shown to promote tumor growth, angiogenesis, and metastasis, making it a target for cancer therapy.
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.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
I'm sorry for any confusion, but "Mannosephosphates" is not a widely recognized or established term in medicine or biochemistry. It seems that this term may be a combination of "mannose," which is a type of sugar (monosaccharide), and "phosphates," which are compounds containing phosphorus. However, without more context, it's difficult to provide an accurate medical definition for this term.
In biochemistry, mannose can be linked to phosphate groups in various ways, such as in the context of mannose-1-phosphate or mannose-6-phosphate, which are involved in different metabolic pathways. If you could provide more information about where you encountered this term, I might be able to give a more precise definition or explanation.
IGF-2 (Insulin-like Growth Factor 2) receptor is a type of transmembrane protein that plays a role in cell growth, differentiation, and survival. Unlike other receptors in the insulin and IGF family, IGF-2 receptor does not mediate the activation of intracellular signaling pathways upon binding to its ligand (IGF-2). Instead, it acts as a clearance receptor that facilitates the removal of IGF-2 from circulation by transporting it to lysosomes for degradation.
The IGF-2 receptor is also known as cation-independent mannose-6-phosphate receptor (CI-M6PR) because it can also bind and transport mannose-6-phosphate-containing enzymes to lysosomes for degradation.
Mutations in the IGF-2 receptor gene have been associated with certain types of cancer, as well as developmental disorders such as Beckwith-Wiedemann syndrome.
MBL deficiency
Mannan-binding lectin
Malpuech facial clefting syndrome
LMAN2
LMAN1
LMAN2L
Leguminous lectin family
Pattern recognition receptor
Jacalin-like lectin domain
Complement component 1s
MASP1 (protein)
Rheumatic fever
Lectin pathway
MASP2 (protein)
TATA box
Alphatorquevirus
BanLec
Biomphalaria glabrata
GBA3
Giardiasis
Î’-Mannosidase
Acute-phase protein
MANEA
MAN1A2
GBA2
Oxyrrhis
Sialic acid
Map44
Mannose-binding protein-associated serine protease
Sialidase-3
A combination of the HLA-DRB1*03 phenotype and low plasma mannose-binding lectin predisposes to autoantibody formation in women...
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Evaluation of Mannose Binding Lectin Gene Variants in Pediatric Influenza Virus-Related Critical Illness.
Fact file for Mannose-binding lectin deficiency
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Mannose-binding lectin deficiency (Concept Id: C3280586) - MedGen - NCBI
Emerging evidence of a COVID-19 thrombotic syndrome has treatment implications | Nature Reviews Rheumatology
MBL deficiency - Wikipedia
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Mannose-binding lectin gene polymorphisms in a cohort study of ANCA-associated small vessel vasculitis. - Radcliffe Department...
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Mannose-binding lectin deficiency and disease severity in non-cystic fibrosis bronchiectasis: a prospective study<...
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Establishment of a recombined mannose-binding lectin protein-magnetic beads-enriched binding recombinant enzyme-assisted...
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Dr Melinda Dean | UniSC | University of the Sunshine Coast, Queensland, Australia
Complement activation in progressive renal disease
Pediatric Common Variable Immunodeficiency Workup: Laboratory Studies, Imaging Studies, Other Tests
Pediatric Common Variable Immunodeficiency Clinical Presentation: History, Physical, Causes
Teste specializate de alergologie si imunologie - Page 23 of 33 - Synevo
autoimmune disease of cardiovascular system - Ontology Report - Rat Genome Database
MMRRC:039824-MU
miR-128-3p inhibits apoptosis and inflammation in LPS-induced sepsis by targeting TGFBR2
Pattern recognition molecule mannose-bindin1
- Melinda also has a particular interest in innate immune protein and pattern recognition molecule mannose binding lectin. (edu.au)
Deficiency8
- Deficiency of the mannose-binding lectin (MBL) protein, an antigen-recognition molecule involved in systemic and mucosal innate immunity, is determined by variant alleles in MBL2 gene promoter and exon-1 regions. (elsevierpure.com)
- Mannose-binding lectin (MBL) deficiency, defined as MBL protein level of less than 100 ng/ml, is present in about 5% of people of European descent and in about 10% of sub-Saharan Africans. (nih.gov)
- Mannose-binding lectin deficiency is a condition that affects the immune system. (nih.gov)
- People with this condition have low levels (deficiency) of an immune system protein called mannose-binding lectin in their blood. (nih.gov)
- People with mannose-binding lectin deficiency can develop infections of the upper respiratory tract and other body systems. (nih.gov)
- Infants and young children with mannose-binding lectin deficiency seem to be more susceptible to infections than affected adults, but adults can also develop recurrent infections. (nih.gov)
- MBL deficiency is a pathology of the innate immune system involving Mannan-binding lectin pathway components such as MBL2. (wikipedia.org)
- Mannose Binding Lectin, IgG Subclass and Antibody Deficiency: Efficacy of Intravenous Immunoglobulins. (yumaregional.org)
Fucose4
- A number of C-type lectins recognise oligosaccharides rich in mannose and fucose - sugars with similar structures to glucose. (nih.gov)
- Cell detachment from pyrite results in microbial "footprints" which, based on lectin binding assays, consist of mannose, glucose and fucose containing compounds. (ufz.de)
- it occurs when mannose-binding lectin (MBL), a serum protein, binds to mannose, fucose, or N -acetylglucosamine groups on bacterial cell walls, yeast walls, or viruses. (msdmanuals.com)
- The biochemical activity of GDP-D-mannose-4,6 dehydratase (GMD) that converts mannose to fucose is decreased in patients with LAD type 2. (medscape.com)
Proteins4
- Mechanisms involve competitive inhibition of carbohydrate binding within sets of defined proteins, in contrast to broadly indiscriminate, irreversible glycation of proteins. (nih.gov)
- Glycans, either alone or complexed with glycan-binding proteins, can deliver intracellular signals or control extracellular processes that promote initiation, execution and resolution of cell death programs. (nature.com)
- Herein, we review the role of glycans and glycan-binding proteins as essential components of the cell death machinery during physiologic and pathologic settings. (nature.com)
- At that time, glycobiology, which is the study of carbohydrates and their recognition by motif-specific carbohydrate-binding proteins or lectins, lagged far behind the studies that defined the structural and cellular biology of cell death. (nature.com)
Polymorphism1
- Mannose-Binding Lectin 2 Gene Polymorphism in PANDAS Patients. (cdc.gov)
Receptors1
- ArtinM is a D-mannose carbohydrate-binding lectin that interacts with phagocytic cell receptors inducing the production of pro-inflammatory mediators related to the antitumor immune response. (usp.br)
Adaptive immunity1
- How do C-type lectins tailor adaptive immunity following phagocytosis of apoptotic cells? (nature.com)
Immunity3
- Mannose-binding lectin (MBL), a complement factor of innate immunity, has been hypothesized to play a role in the clearance of pathogenic autoantibodies from the circulation, in particular those autoantibodies that lack galactose sugar residues. (eur.nl)
- BACKGROUND: Mannose-binding lectin (MBL) is a key component of innate immunity. (ed.ac.uk)
- Intracellular lectins and glycan-modifying enzymes mediate autophagy and control host immunity and inflammation. (nature.com)
Innate immune protein1
- Mannose-binding lectin (MBL) is an innate immune protein with strong biologic plausibility for protecting against influenza virus-related sepsis and bacterial co-infection. (escholarship.org)
Soluble1
- Mannose-binding lectin, soluble DC-SIGN and DC-SIGNR, and surfactant protein D, were tested for carbohydrate binding in the presence of glucose concentrations typical of diabetes, via surface plasmon resonance and affinity chromatography. (nih.gov)
Complement system1
- Activation of the complement system occurs through the classical (CP), lectin (LP), or alternative (AP) pathways. (jrheum.org)
Endogenous2
- Furthermore, differential binding was observed also to known endogenous ligands C1q, mannose-binding lectin, and secretory IgA. (researchgate.net)
- Endogenous lectins and glycans are critical signals in the resolution of cell death. (nature.com)
Subclass1
- A subclass of lectins that are specific for CARBOHYDRATES that contain MANNOSE. (bvsalud.org)
Serum1
- Crosstalk between innate and adaptive immune responses to infectious bronchitis virus after vaccination and challenge of chickens varying in serum mannose-binding lectin concentrations. (southernbiotech.com)
Serine1
- TGF-β signaling is initiated when the ligand binds to type II serine/threonine kinase receptor (TGFBR2), which then phosphorylates and activates type I serine/threonine kinase receptor (TGFBR1) [ 13 ]. (degruyter.com)
Pathway activation1
- E, Lectin complement pathway activation activity. (biomedcentral.com)
Susceptibility1
- We conclude that high glucose disrupts C-type lectin function, potentially illuminating new perspectives on susceptibility to infectious and inflammatory disease in diabetes. (nih.gov)
Heterogeneity1
- 2008). Genetic Heterogeneity of Lectin Complement Activation Pathway Defects See also LCAPD2 (613791), caused by variation in the MASP2 gene (605102) on chromosome 1p36, and LCAPD3 (613860), caused by variation in the FCN3 gene (604973) on chromosome 1p36. (nih.gov)
Vaccine1
- C-reactive protein, Immunoglobulins and mannose binding lectin (MBL) levels were measured and correlated to vaccine response. (manchester.ac.uk)
Ligand1
- High glucose inhibited C-type lectin binding to high-mannose glycoprotein and binding of DC-SIGN to fucosylated ligand (blood group B) was abrogated in high glucose. (nih.gov)
Glucose1
- Complement activation via the lectin pathway was inhibited in high glucose and also in high trehalose - a nonreducing sugar with glucoside stereochemistry. (nih.gov)
Pathways1
- The classical, lectin, and alternative pathways converge into a final common pathway when C3 convertase (C3 con) cleaves C3 into C3a and C3b. (msdmanuals.com)
Cohort1
- Mannose-binding lectin gene polymorphisms in a cohort study of ANCA-associated small vessel vasculitis. (ox.ac.uk)
Immune2
- Within the immune system, host-pathogen and regulatory host-host interactions operate through binding of oligosaccharides by C-type lectin. (nih.gov)
- 7 It is possible that these major histocompatibility complexes bind antigens in such a way that they increase the likelihood of T-cells mounting an immune response to self-antigens. (lww.com)
Enrichment2
- To establish a nested recombinant enzyme -assisted polymerase chain reaction (RAP) technique combined with recombined mannose-binding lectin protein (M1 protein )- magnetic beads enrichment for the detection of Candida albicans (C. albicans) and Candida tropicalis (C. tropicalis) in blood samples for the early diagnosis of candidemia albicans and candidiemia tropicalis. (bvsalud.org)
- A Bacterial Mannose Binding Lectin as a Tool for the Enrichment of C- and O-Mannosylated Peptides. (mpg.de)
Structures1
- Legume Lectins: Structures, Functions, and Carbohydrate-binding Specificities. (gr.jp)
Interactions2
- Two decades later, pioneering studies suggested that lectin-like molecules constitutively expressed on the surface of macrophages can selectively recognize changes on glycans decorating the surface of apoptotic thymocytes, 4 , 5 although these studies likewise did not provide substantial insight into the mechanisms by which lectin-glycan interactions regulate cell death. (nature.com)
- We discuss here the contribution of glycan-lectin interactions to the initiation, execution and resolution of apoptosis and their emerging roles in other cell death programs including autophagy. (nature.com)
Failure1
- Is Plasma Level of Mannose Binding Lectin Associated With Reproductive Failure? (who.int)
Assay1
- The binding sites of miR-128-3p and TGFBR2 were predicted by Targetscan online software and confirmed by dual-luciferase reporter assay and RNA immunoprecipitation (RIP) assay. (degruyter.com)
Investigate2
- OBJECTIVE: To investigate whether single nucleotide polymorphisms (SNPs) within the mannose-binding lectin (MBL) gene are associated with small vessel vasculitis (SVV) and are a risk factor for intercurrent infection, as described previously in other autoimmune diseases. (ox.ac.uk)
- The aim of this study was to investigate the role of ArtinM lectin in AFB1-induced hepatocarcinogenesis in rats. (usp.br)
Blood cells1
- Although lectins were already known because of their ability to agglutinate red blood cells, 3 the involvement of lectins and glycans in PCD had not been elucidated. (nature.com)
Cell2
- The emergence of functional studies on animal lectins during the 1990s has provided the appropriate framework to better understand their roles in cell death. (nature.com)
- Understanding the function of lectin-glycan recognition systems in cell death will facilitate the implementation of novel therapeutic strategies aimed at controlling unbalanced cell proliferation and survival in several pathologic conditions. (nature.com)
Activity1
- After delivery, the specialists from Gentaur/Genprice recommend you to store the Human Mannma binding protein/mannan binding lectin,MBP/MBL ELISA Kit between two and eight degrees Celsius to keep the quality and activity of the reagents included in the kit. (assayspro.com)
Error1
- This is the Bhattacharya bound on pairwise error probability with ML decoding. (forextrading-madeeasy.com)