Porins
Bacterial Outer Membrane Proteins
Salmonella typhimurium
Voltage-Dependent Anion Channels
Mycobacterium smegmatis
Cell Membrane Permeability
Delftia acidovorans
Ion Channels
beta-Lactams
Lipid Bilayers
Rhodobacter
Neisseria meningitidis
Molecular Sequence Data
Amino Acid Sequence
Neisseria
Enterobacter
Gene Expression Regulation, Bacterial
Safety and immunogenicity of a Pseudomonas aeruginosa hybrid outer membrane protein F-I vaccine in human volunteers. (1/1946)
A hybrid protein [Met-Ala-(His)6OprF190-342-OprI21-83] consisting of the mature outer membrane protein I (OprI) and amino acids 190 to 342 of OprF of Pseudomonas aeruginosa was expressed in Escherichia coli and purified by Ni2+ chelate-affinity chromatography. After safety and pyrogenicity evaluations in animals, four groups of eight adult human volunteers were vaccinated intramuscularly three times at 4-week intervals and revaccinated 6 months later with either 500, 100, 50, or 20 microg of OprF-OprI adsorbed onto A1(OH)3. All vaccinations were well tolerated. After the first vaccination, a significant rise of antibody titers against P. aeruginosa OprF and OprI was measured in volunteers receiving the 100- or the 500-microg dose. After the second vaccination, significant antibody titers were measured for all groups. Elevated antibody titers against OprF and OprI could still be measured 6 months after the third vaccination. The capacity of the elicited antibodies to promote complement binding and opsonization could be demonstrated by a C1q-binding assay and by the in vitro opsonophagocytic uptake of P. aeruginosa bacteria. These data support the continued development of an OprF-OprI vaccine for use in humans. (+info)Distinct sensitivities of OmpF and PhoE porins to charged modulators. (2/1946)
The inhibition of the anion-selective PhoE porin by ATP and of the cation-selective OmpF porin by polyamines has been previously documented. In the present study, we have extended the comparison of the inhibitor-porin pairs by investigating the effect of anions (ATP and aspartate) and positively charged polyamines (spermine and cadaverine) on both OmpF and PhoE with the patch-clamp technique, and by comparing directly the gating kinetics of the channels modulated by their respective substrates. The novel findings reported here are (1) that the activity of PhoE is completely unaffected by polyamines, and (2) that the kinetic changes induced by ATP on PhoE or polyamines on OmpF suggest different mechanisms of inhibition. ATP induces a high degree of flickering in the PhoE-mediated current and appears to behave as a blocker of ion flow during its presumed transport through PhoE. Polyamines modulate the kinetics of openings and closings of OmpF, in addition to promoting a blocker-like flickering activity. The strong correlation between sensitivity to inhibitors and ion selectivity suggests that some common molecular determinants are involved in these two properties and is in agreement with the hypothesis that polyamines bind inside the pore of cationic porins. (+info)Enhanced bioaccumulation of heavy metal ions by bacterial cells due to surface display of short metal binding peptides. (3/1946)
Metal binding peptides of sequences Gly-His-His-Pro-His-Gly (named HP) and Gly-Cys-Gly-Cys-Pro-Cys-Gly-Cys-Gly (named CP) were genetically engineered into LamB protein and expressed in Escherichia coli. The Cd2+-to-HP and Cd2+-to-CP stoichiometries of peptides were 1:1 and 3:1, respectively. Hybrid LamB proteins were found to be properly folded in the outer membrane of E. coli. Isolated cell envelopes of E. coli bearing newly added metal binding peptides showed an up to 1.8-fold increase in Cd2+ binding capacity. The bioaccumulation of Cd2+, Cu2+, and Zn2+ by E. coli was evaluated. Surface display of CP multiplied the ability of E. coli to bind Cd2+ from growth medium fourfold. Display of HP peptide did not contribute to an increase in the accumulation of Cu2+ and Zn2+. However, Cu2+ ceased contribution of HP for Cd2+ accumulation, probably due to the strong binding of Cu2+ to HP. Thus, considering the cooperation of cell structures with inserted peptides, the relative affinities of metal binding peptide and, for example, the cell wall to metal ion should be taken into account in the rational design of peptide sequences possessing specificity for a particular metal. (+info)In-vitro selection of porin-deficient mutants of two strains of Klebsiella pneumoniae with reduced susceptibilities to meropenem, but not to imipenem. (4/1946)
We have evaluated the ability of imipenem and meropenem to select, in vitro, resistant mutants of two clinical isolates of Klebsiella pneumoniae producing both SHV and TEM beta-lactamases. Only meropenem selected mutants of both isolates for which the MICs of meropenem, but not imipenem, were markedly higher than those for the parent strains; the MICs of several other beta-lactam antibiotics, including beta-lactam/beta-lactamase inhibitor combinations, for these mutants were also higher than those for the parent strains. In contrast, the MICs for the imipenem-selected mutants were the same as, or similar to, those for the parent strains. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis revealed that an outer membrane protein in both parent strains was absent in the meropenem-selected mutants, but not in the imipenem-selected mutants. This protein is likely to be a porin, the absence of which is presumably associated with impaired beta-lactam permeability and, therefore, the reduced susceptibilities to these antibiotics exhibited by the mutant strains. We believe that this is the first report of the in-vitro selection of porin-deficient mutants of K. pneumoniae following exposure to meropenem. (+info)Single channel analysis of recombinant major outer membrane protein porins from Chlamydia psittaci and Chlamydia pneumoniae. (5/1946)
We recently demonstrated that the major outer membrane protein of Chlamydia psittaci, the primary vaccine candidate for combating chlamydial infections, functions as a porin-like ion channel. In this study, we have cloned, expressed and functionally reconstituted recombinant major outer membrane proteins from C. psittaci and Chlamydia pneumoniae and analysed them at the single channel level. Both form porin-like ion channels that are functionally similar to those formed by native C. psittaci major outer membrane protein. Also, like the native channels, recombinant C. psittaci channels are modified by a native major outer membrane protein-specific monoclonal antibody. This is the first time that native function has been demonstrated for recombinant chlamydial major outer membrane proteins. Future bilayer reconstitution will provide a strategy for detailed structure/function studies of this new subclass of bacterial porins and the work also has important implications for successful protein refolding and the development of improved subunit vaccines. (+info)Site-directed mutagenesis of loop L3 of sucrose porin ScrY leads to changes in substrate selectivity. (6/1946)
The difference in substrate selectivity of the maltodextrin (LamB) and sucrose (ScrY) porins is attributed mainly to differences in loop L3, which is supposed to constrict the lumen of the pores. We show that even a single mutation (D201Y) in loop L3 leads to a narrowing of the substrate range of ScrY to that resembling LamB. In addition, we removed the putative N-terminal coiled-coil structure of ScrY and studied the effect of this deletion on sucrose transport. (+info)Escherichia coli outer membrane protein TolC is involved in production of the peptide antibiotic microcin J25. (7/1946)
A Tn5 insertion in tolC eliminated microcin J25 production. The mutation had little effect on the expression of the microcin structural gene and presumably acted by blocking microcin secretion. The tolC mutants carrying multiple copies of the microcin genes were less immune to the microcin. TolC is thus likely a component of a microcin export complex containing the McjD immunity protein, an ABC exporter. (+info)Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange. (8/1946)
Growth factor withdrawal is associated with a metabolic arrest that can result in apoptosis. Cell death is preceded by loss of outer mitochondrial membrane integrity and cytochrome c release. These mitochondrial events appear to follow a relative increase in mitochondrial membrane potential. This change in membrane potential results from the failure of the adenine nucleotide translocator (ANT)/voltage-dependent anion channel (VDAC) complex to maintain ATP/ADP exchange. Bcl-xL expression allows growth factor-deprived cells to maintain sufficient mitochondrial ATP/ADP exchange to sustain coupled respiration. These data demonstrate that mitochondrial adenylate transport is under active regulation. Efficient exchange of ADP for ATP is promoted by Bcl-xL expression permitting oxidative phosphorylation to be regulated by cellular ATP/ADP levels and allowing mitochondria to adapt to changes in metabolic demand. (+info)Porins are a type of protein found in the outer membrane of gram-negative bacteria. They form water-filled channels, or pores, that allow small molecules such as ions, nutrients, and waste products to pass through the otherwise impermeable outer membrane. Porins are important for the survival of gram-negative bacteria, as they enable the selective transport of essential molecules while providing a barrier against harmful substances.
There are different types of porins, classified based on their structure and function. Some examples include:
1. General porins (also known as nonspecific porins): These are the most common type of porins and form large, water-filled channels that allow passive diffusion of small molecules up to 600-700 Da in size. They typically have a trimeric structure, with three identical or similar subunits forming a pore in the membrane.
2. Specific porins: These porins are more selective in the molecules they allow to pass through and often have smaller pores than general porins. They can be involved in the active transport of specific molecules or ions, requiring energy from the cell.
3. Autotransporters: While not strictly considered porins, autotransporter proteins share some structural similarities with porins and are involved in the transport of protein domains across the outer membrane. They consist of an N-terminal passenger domain and a C-terminal translocator domain, which forms a β-barrel pore in the outer membrane through which the passenger domain is transported.
Porins have attracted interest as potential targets for antibiotic development, as they play crucial roles in bacterial survival and virulence. Inhibiting porin function or blocking the pores could disrupt essential processes in gram-negative bacteria, providing a new approach to treating infections caused by these organisms.
Bacterial outer membrane proteins (OMPs) are a type of protein found in the outer membrane of gram-negative bacteria. The outer membrane is a unique characteristic of gram-negative bacteria, and it serves as a barrier that helps protect the bacterium from hostile environments. OMPs play a crucial role in maintaining the structural integrity and selective permeability of the outer membrane. They are involved in various functions such as nutrient uptake, transport, adhesion, and virulence factor secretion.
OMPs are typically composed of beta-barrel structures that span the bacterial outer membrane. These proteins can be classified into several groups based on their size, function, and structure. Some of the well-known OMP families include porins, autotransporters, and two-partner secretion systems.
Porins are the most abundant type of OMPs and form water-filled channels that allow the passive diffusion of small molecules, ions, and nutrients across the outer membrane. Autotransporters are a diverse group of OMPs that play a role in bacterial pathogenesis by secreting virulence factors or acting as adhesins. Two-partner secretion systems involve the cooperation between two proteins to transport effector molecules across the outer membrane.
Understanding the structure and function of bacterial OMPs is essential for developing new antibiotics and therapies that target gram-negative bacteria, which are often resistant to conventional treatments.
"Salmonella enterica" serovar "Typhimurium" is a subspecies of the bacterial species Salmonella enterica, which is a gram-negative, facultatively anaerobic, rod-shaped bacterium. It is a common cause of foodborne illness in humans and animals worldwide. The bacteria can be found in a variety of sources, including contaminated food and water, raw meat, poultry, eggs, and dairy products.
The infection caused by Salmonella Typhimurium is typically self-limiting and results in gastroenteritis, which is characterized by symptoms such as diarrhea, abdominal cramps, fever, and vomiting. However, in some cases, the infection can spread to other parts of the body and cause more severe illness, particularly in young children, older adults, and people with weakened immune systems.
Salmonella Typhimurium is a major public health concern due to its ability to cause outbreaks of foodborne illness, as well as its potential to develop antibiotic resistance. Proper food handling, preparation, and storage practices can help prevent the spread of Salmonella Typhimurium and other foodborne pathogens.
Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.
Bacterial proteins can be classified into different categories based on their function, such as:
1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.
Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.
Voltage-Dependent Anion Channels (VDACs) are large protein channels found in the outer mitochondrial membrane. They play a crucial role in the regulation of metabolite and ion exchange between the cytosol and the mitochondria. VDACs are permeable to anions such as chloride, phosphate, and bicarbonate ions, as well as to small molecules and metabolites like ATP, ADP, NADH, and others.
The voltage-dependent property of these channels arises from the fact that their permeability can be modulated by changes in the membrane potential across the outer mitochondrial membrane. At low membrane potentials, VDACs are predominantly open and facilitate the flow of metabolites and ions. However, as the membrane potential becomes more positive, VDACs can transition to a closed or partially closed state, which restricts ion and metabolite movement.
VDACs have been implicated in various cellular processes, including apoptosis, calcium homeostasis, and energy metabolism. Dysregulation of VDAC function has been associated with several pathological conditions, such as neurodegenerative diseases, cancer, and ischemia-reperfusion injury.
"Mycobacterium smegmatis" is a species of fast-growing, non-tuberculous mycobacteria (NTM). It is commonly found in the environment, including soil and water. This bacterium is known for its ability to form resistant colonies called biofilms. While it does not typically cause disease in humans, it can contaminate medical equipment and samples, potentially leading to misdiagnosis or infection. In rare cases, it has been associated with skin and soft tissue infections. It is often used in research as a model organism for studying mycobacterial biology and drug resistance due to its relatively harmless nature and rapid growth rate.
Cell membrane permeability refers to the ability of various substances, such as molecules and ions, to pass through the cell membrane. The cell membrane, also known as the plasma membrane, is a thin, flexible barrier that surrounds all cells, controlling what enters and leaves the cell. Its primary function is to protect the cell's internal environment and maintain homeostasis.
The permeability of the cell membrane depends on its structure, which consists of a phospholipid bilayer interspersed with proteins. The hydrophilic (water-loving) heads of the phospholipids face outward, while the hydrophobic (water-fearing) tails face inward, creating a barrier that is generally impermeable to large, polar, or charged molecules.
However, specific proteins within the membrane, called channels and transporters, allow certain substances to cross the membrane. Channels are protein structures that span the membrane and provide a pore for ions or small uncharged molecules to pass through. Transporters, on the other hand, are proteins that bind to specific molecules and facilitate their movement across the membrane, often using energy in the form of ATP.
The permeability of the cell membrane can be influenced by various factors, such as temperature, pH, and the presence of certain chemicals or drugs. Changes in permeability can have significant consequences for the cell's function and survival, as they can disrupt ion balances, nutrient uptake, waste removal, and signal transduction.
Cadaverine is a foul-smelling organic compound that is produced by the breakdown of certain amino acids in dead bodies. It is formed through the decarboxylation of lysine, an essential amino acid, and is characterized by its strong, unpleasant odor. Cadaverine is often used as a forensic indicator of decomposition and is also being studied for its potential role in various physiological processes, such as inflammation and cancer.
"Delftia acidovorans" is a species of gram-negative, motile, aerobic bacteria that is commonly found in various environments such as soil, water, and clinical settings. It is a rod-shaped bacterium that is known to be able to degrade a wide range of organic compounds, including aromatic hydrocarbons and other pollutants.
In clinical settings, "Delftia acidovorans" has been isolated from various types of human infections, including respiratory tract infections, urinary tract infections, and bacteremia. However, it is considered to be a rare cause of infection, and its clinical significance is not well understood.
It's worth noting that the genus "Delftia" was previously classified as part of the genus "Comamonas," but was reclassified based on genetic and biochemical evidence. Therefore, some older literature may refer to this bacterium as "Comamonas acidovorans."
Ion channels are specialized transmembrane proteins that form hydrophilic pores or gaps in the lipid bilayer of cell membranes. They regulate the movement of ions (such as sodium, potassium, calcium, and chloride) across the cell membrane by allowing these charged particles to pass through selectively in response to various stimuli, including voltage changes, ligand binding, mechanical stress, or temperature changes. This ion movement is essential for many physiological processes, including electrical signaling, neurotransmission, muscle contraction, and maintenance of resting membrane potential. Ion channels can be categorized based on their activation mechanisms, ion selectivity, and structural features. Dysfunction of ion channels can lead to various diseases, making them important targets for drug development.
Beta-lactams are a class of antibiotics that include penicillins, cephalosporins, carbapenems, and monobactams. They contain a beta-lactam ring in their chemical structure, which is responsible for their antibacterial activity. The beta-lactam ring inhibits the bacterial enzymes necessary for cell wall synthesis, leading to bacterial death. Beta-lactams are commonly used to treat a wide range of bacterial infections, including respiratory tract infections, skin and soft tissue infections, urinary tract infections, and bone and joint infections. However, some bacteria have developed resistance to beta-lactams through the production of beta-lactamases, enzymes that can break down the beta-lactam ring and render the antibiotic ineffective. To overcome this resistance, beta-lactam antibiotics are often combined with beta-lactamase inhibitors, which protect the beta-lactam ring from degradation.
A lipid bilayer is a thin membrane made up of two layers of lipid molecules, primarily phospholipids. The hydrophilic (water-loving) heads of the lipids face outwards, coming into contact with watery environments on both sides, while the hydrophobic (water-fearing) tails point inward, away from the aqueous surroundings. This unique structure allows lipid bilayers to form a stable barrier that controls the movement of molecules and ions in and out of cells and organelles, thus playing a crucial role in maintaining cellular compartmentalization and homeostasis.
Rhodobacter is not a medical term, but a genus of bacteria found in the environment. It is commonly found in aquatic environments and can perform photosynthesis, although it is not classified as a plant. Some species of Rhodobacter are capable of fixing nitrogen gas from the atmosphere, making them important contributors to the global nitrogen cycle.
While there may be some medical research into the potential uses or impacts of certain species of Rhodobacter, there is no widely recognized medical definition for this term. If you have any specific concerns about bacteria or infections, it's best to consult with a healthcare professional for accurate information and advice.
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.
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.
'Escherichia coli (E. coli) proteins' refer to the various types of proteins that are produced and expressed by the bacterium Escherichia coli. These proteins play a critical role in the growth, development, and survival of the organism. They are involved in various cellular processes such as metabolism, DNA replication, transcription, translation, repair, and regulation.
E. coli is a gram-negative, facultative anaerobe that is commonly found in the intestines of warm-blooded organisms. It is widely used as a model organism in scientific research due to its well-studied genetics, rapid growth, and ability to be easily manipulated in the laboratory. As a result, many E. coli proteins have been identified, characterized, and studied in great detail.
Some examples of E. coli proteins include enzymes involved in carbohydrate metabolism such as lactase, sucrase, and maltose; proteins involved in DNA replication such as the polymerases, single-stranded binding proteins, and helicases; proteins involved in transcription such as RNA polymerase and sigma factors; proteins involved in translation such as ribosomal proteins, tRNAs, and aminoacyl-tRNA synthetases; and regulatory proteins such as global regulators, two-component systems, and transcription factors.
Understanding the structure, function, and regulation of E. coli proteins is essential for understanding the basic biology of this important organism, as well as for developing new strategies for combating bacterial infections and improving industrial processes involving bacteria.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
"Neisseria" is a genus of gram-negative, aerobic bacteria that are commonly found as part of the normal flora in the human body, particularly in the mouth, nose, and genital tract. Some species of Neisseria can cause diseases in humans, the most well-known being Neisseria meningitidis (meningococcus), which can cause meningitis and sepsis, and Neisseria gonorrhoeae (gonococcus), which causes the sexually transmitted infection gonorrhea. These bacteria are named after German physician and bacteriologist Albert Neisser, who first described them in the late 19th century.
Enterobacter is a genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that are commonly found in the environment, including in soil, water, and the gastrointestinal tracts of humans and animals. These bacteria are members of the family Enterobacteriaceae and are known to cause a variety of infections in humans, particularly in healthcare settings.
Enterobacter species are capable of causing a range of infections, including urinary tract infections, pneumonia, bacteremia, and wound infections. They are often resistant to multiple antibiotics, which can make treatment challenging. Infections with Enterobacter are typically treated with broad-spectrum antibiotics that are effective against gram-negative bacteria.
It's worth noting that while Enterobacter species can cause infections, they are also a normal part of the microbiota found in the human gut and usually do not cause harm in healthy individuals. However, if the bacterium enters the bloodstream or other sterile sites in the body, it can cause infection and illness.
Salmonella typhi is a bacterium that causes typhoid fever, a severe and sometimes fatal infectious disease. It is a human-specific pathogen, which means it only infects humans and is not carried in animals or birds. The bacteria are spread through the fecal-oral route, often through contaminated food or water. Once ingested, Salmonella typhi can invade the intestinal tract, causing symptoms such as high fever, headache, abdominal pain, constipation, and rose-colored spots on the chest. If left untreated, typhoid fever can lead to serious complications, including intestinal perforation, bacteremia, and death.
Gene expression regulation in bacteria refers to the complex cellular processes that control the production of proteins from specific genes. This regulation allows bacteria to adapt to changing environmental conditions and ensure the appropriate amount of protein is produced at the right time.
Bacteria have a variety of mechanisms for regulating gene expression, including:
1. Operon structure: Many bacterial genes are organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule. The expression of these genes can be coordinately regulated by controlling the transcription of the entire operon.
2. Promoter regulation: Transcription is initiated at promoter regions upstream of the gene or operon. Bacteria have regulatory proteins called sigma factors that bind to the promoter and recruit RNA polymerase, the enzyme responsible for transcribing DNA into RNA. The binding of sigma factors can be influenced by environmental signals, allowing for regulation of transcription.
3. Attenuation: Some operons have regulatory regions called attenuators that control transcription termination. These regions contain hairpin structures that can form in the mRNA and cause transcription to stop prematurely. The formation of these hairpins is influenced by the concentration of specific metabolites, allowing for regulation of gene expression based on the availability of those metabolites.
4. Riboswitches: Some bacterial mRNAs contain regulatory elements called riboswitches that bind small molecules directly. When a small molecule binds to the riboswitch, it changes conformation and affects transcription or translation of the associated gene.
5. CRISPR-Cas systems: Bacteria use CRISPR-Cas systems for adaptive immunity against viruses and plasmids. These systems incorporate short sequences from foreign DNA into their own genome, which can then be used to recognize and cleave similar sequences in invading genetic elements.
Overall, gene expression regulation in bacteria is a complex process that allows them to respond quickly and efficiently to changing environmental conditions. Understanding these regulatory mechanisms can provide insights into bacterial physiology and help inform strategies for controlling bacterial growth and behavior.
Anti-bacterial agents, also known as antibiotics, are a type of medication used to treat infections caused by bacteria. These agents work by either killing the bacteria or inhibiting their growth and reproduction. There are several different classes of anti-bacterial agents, including penicillins, cephalosporins, fluoroquinolones, macrolides, and tetracyclines, among others. Each class of antibiotic has a specific mechanism of action and is used to treat certain types of bacterial infections. It's important to note that anti-bacterial agents are not effective against viral infections, such as the common cold or flu. Misuse and overuse of antibiotics can lead to antibiotic resistance, which is a significant global health concern.
Opacity porins
Porin
Porin maalaiskunta
Porin Palloilijat
Porin Kärpät
Porin (opera)
Porin Lyseo
Porin (protein)
Porin Ässät
Mycobacterial porin
Oligogalacturonate-specific porin
Porin Karhu HT
Nucleoside-specific porin
Protein K (porin)
Porin (music award)
Corynebacterial porin B
Phosphate-selective porin
Porin Ässät (men's football)
Takam Mising Porin Kebang
General bacterial porin family
Outer membrane porin D
Porin Ässät (women's ice hockey)
Porin Ässät (men's ice hockey)
History of Porin Ässät (men's ice hockey)
Symbiogenesis
Penicillin
Tilman Schirmer
VDAC1
Roland Benz
Elemental (music group)
Opacity porins - Wikipedia
Porins Hotel Liepaja | Low rates. No booking fees.
CDD Conserved Protein Domain Family: LbtU sider porin
Comments: Porins, VDACs and gating : The role of conformational plasticity :: Publikationsserver
Bacterial Porin Disrupts Mitochondrial Membrane Potential and Sensitizes Host Cells to Apoptosis | PLOS Pathogens
Pori Jazz avaa uuden ravintolan Porin Kirjurinluotoon - Finland Festivals
WikiGenes - ompF - outer membrane porin 1a (Ia;b;F)
Nominacije za 27. Porin - antena zagreb
Porin Pelipäivä 2023 | Insomnia
Your search "keyword/porin-seudun-kansalaisopisto-1150/keyword/kansalaisopisto-280" returned 0 results - City of Pori
Mitochondrial outer membrane protein porin 2 (Saccharomyces cerevisiae S288C) | Protein Target - PubChem
Liikesivistysrahaston Porin alueen vuosikokous - Liikesivistysrahasto
JYX - Isäntäväet ja palvelusväen pito 1600-luvulla ja 1700-luvun alkupuolella : taloudellispohjainen tutkimus Turun ja Porin...
Educational program | Riječka razvojna agencija PORIN
Chui i Daleka obala okitili se prestižnom nagradom Porin! - Dancing Bear
"Peculiarities of Thermal Denaturation of OmpF Porin from Yersinia Ruck" by Olga D. Novikova, Dmitry K. Chistyulin et al.
porin Archives - Total Croatia
A Study on N-terminal Outer Membrane Porin (Pseudomonas Aeru | 15627
Structural Biochemistry/Lipids/Membrane Transport - Wikibooks, open books for an open world
Porin knjižice | Porin
26. Porin | Porin
Meri-Porin uimahalli
Porin Kalustetalo Oy | DUXIANA
Arena :: Porin Lyseo, Pori
Evergreen Inner Jungle - Porin kulttuurisäätö
Nagrade4
- glazbene nagrade Porin su objavljene na ceremoniji u zagrebačkom Matis Absolute Loungeu. (antenazagreb.hr)
- dodjeli glazbene nagrade Porin u Boćarskom domu, dodijeljene su statue i Dancing Bearovim grupama Chui i Daleka obala . (dancingbear.hr)
- Podeljene so bile hrvaške glasbene nagrade Porin. (steklarna-rogaska.si)
- Glazbene nagrade Porin po prvi put u svojoj dugoj povijesti, održi isključivo kao TV emisija na HRT-u, u petak 15. (zgkult.eu)
20231
- Verkkopeliyhdistys Insomnia ry on mukana Porin Pelipäivässä 11.11.2023 Porin nuorisotalolla! (insomnia.fi)
Pori5
- Porin kesäinen ravintolatarjonta saa tänä vuonna uuden tulokkaan, kun Cafe Pori Jazz avautuu toukokuussa Porin Kirjurinluodossa. (festivals.fi)
- Pori Jazz haluaa uuden ravintolan myötä olla osa Porin kesää myös festivaaliviikon ulkopuolella, ja tavoitteena onkin tarjota asiakkaille samaa rentoa tunnelmaa, josta Pori Jazz -festivaali tunnetaan maanlaajuisesti. (festivals.fi)
- Cafe Pori Jazzia pyörittävät yhteistyössä Pori Jazz sekä Petras Cafe, joka on toiminut menestykkäästi Porin kävelykadun varressa jo yli 15 vuoden ajan. (festivals.fi)
- Porin Vuokralukaali is a private company which provides rental apartments in Pori and nearby regions. (edunation.co)
- Porin Paahtimo has roasted coffee in the Puuvilla area in Pori since 2005. (visitpori.fi)
Glazbena nagrada Porin1
- Glazbena nagrada Porin 15. (zgkult.eu)
Nagradu2
- U kategoriji Najbolji album rock glazbe legendarni hrvatski rock sastav Daleka obala osvojio je nagradu Porin s povratničkim studijskim albumom "Kao sad" čiju produkciju potpisuje Leo Anđelković, a koji je objavljen na CD-u , vinilu i u digitalnom obliku . (dancingbear.hr)
- Važno je istaknuti i da je novac kojim bi udruge utemeljitelji (HDS i HGU) podržale glazbenu nagradu Porin, preusmjeren u fondove pomoći glazbenicima u ovim teškim vremenima. (zgkult.eu)
OmpF Porin2
- Peculiarities of Thermal Denaturation of OmpF Porin from Yersinia Ruck" by Olga D. Novikova, Dmitry K. Chistyulin et al. (usf.edu)
- Using SDS-PAGE, spectroscopic methods and differential scanning calorimetry, a detailed study of thermally induced changes in the spatial structure of OmpF porin from the fish pathogen Yersinia ruckeri (Yr-OmpF) was carried out. (usf.edu)
Neisseria2
- Opacity family porins are a family of porins from pathogenic Neisseria. (wikipedia.org)
- Molecular typing of Neisseria meningitidis by DNA sequencing of target porin genes porA . (canada.ca)
Outer membrane protein2
- LbtU, from Legionella pneumophila, a novel TonB-independent siderophore uptake outer membrane protein from a species that lacks TonB, is the founding member of a class of porins that may be involved generally in siderophore-mediated iron acquisition. (nih.gov)
- The outer membrane protein F (OprF), which works as a porin and plays an essential role in virulence, is one of P. aeruginosa's most important antigens. (tsijournals.com)
Genes1
- Intragenic recombination between porin genes of the same allelic family is likely occurring in nature because mosaic gene structure has been reported in porB genes. (cdc.gov)
Turun2
- Turun ja Porin lääni. (nationallibrary.fi)
- Venäjän Federaation Turun pääkonsulaatin pääkonsuli Alexander Y. Gremitskikh ja Suomi-Venäjä-seura Porin osasto ry:n puheenjohtaja Tapio Lammi. (suomivenajaseura.fi)
Najbolji1
- Singrlicama Porin za najbolji etno album! (com.hr)
Protein1
- However, carbapenem resistance may also be mediated by the loss or alteration of porin channels, the expression of efflux pumps, or penicillin-binding protein (PBP) modification. (msdmanuals.com)
Toimii1
- Uusi kahvila-ravintola toimii perinteikkäässä Kirjurinluodon kesäravintolassa, joka on historiallisen arvokas jugendhuvila Porin paraatipaikalla. (festivals.fi)
Conformational1
- There are still some contradictory data on the peculiarities of the conformational changes in the porin structure with temperature. (usf.edu)
Resistance1
- Resistance to carbapenems occurs either through bacterial production of β-lactamase enzymes that hydrolyze (break down) the antimicrobial agent or through porin changes in the bacterial cell wall that reduce the permeability of the drug into the organism. (cdc.gov)
Loss1
- Some authors demonstrated the loss of the porin trimeric structure only after unfolding of monomer subunits. (usf.edu)
Service1
- The service advisor at Porin YH-Asunnot is Patrik Nyman. (porinyhasunnot.fi)
Stay1
- Hope that the Porin Music Awards ceremony will stay in the Dalmatian capital. (total-croatia-news.com)
Event1
- Here at Porin Taitoluistelu Ry we want the sports activity to be a joyful and rewarding event for everyone. (porita.net)
Return1
- Split's Spaladium Arena Will Return as Host for 25th Porin Music Awards! (total-croatia-news.com)
Production1
- RÉSUMÉ L'émergence et la propagation rapide des souches de Klebsiella pneumoniae résistantes aux antibiotiques et porteuses du gène blaKPC codant la production de carbapénèmases ont compliqué la prise en charge des infections des patients. (who.int)
Potential1
- The N-terminal porin domain of OprF was explored as a potential vaccination candidate against P. aeruginosa in the current investigation. (tsijournals.com)
Proteins8
- Porins are outer membrane proteins (OMPs) able to form channels allowing the transport of molecules across lipid bilayer membranes. (medscape.com)
- The main difference between porins and aquaporins is that porins are transport proteins that occur in biological membranes, whereas aquaporins are water channels that allow the movement of water. (pediaa.com)
- Porins and aquaporins are two types of channel proteins that form large pores in the cell membrane, outer membranes of cell organelles, such as mitochondria and plastids, and bacteria. (pediaa.com)
- Porins and aquaporins are two types of channel proteins that occur in biological membranes. (pediaa.com)
- Porins refer to the beta-barrel proteins that cross a cellular membrane, acting as a pore through which molecules can diffuse, while aquaporins refer to water channels that form pores in the cell membranes that selectively conduct water molecules through the membrane. (pediaa.com)
- Porins are transport proteins, while aquaporins are types of transport proteins. (pediaa.com)
- In brief, porins and aquaporins are two types of transport proteins that transport different types of molecules across the membrane. (pediaa.com)
- Hydrophilic nutrients can enter by way of transmembrane-channel proteins called porins. (nih.gov)
Outer13
- By applying the principles that have been recognized for them to the four classes of neisserial porins, we have constructed a model for the topology of the porins within the outer membrane. (nih.gov)
- [ 45 ] A. baumannii intrinsically have a smaller number and size of porins compared with other Gram-negative organisms, contributing to the intrinsic outer membrane impermeability. (medscape.com)
- Porins are protein molecules that occur in the outer membrane of cells, organelles, and bacteria. (pediaa.com)
- In addition, the outer membrane of Gram-negative bacteria and some Gram-positive bacteria contain porins. (pediaa.com)
- Previously, we have shown that purified S. Typhimurium porins including outer membrane protein OmpD, which induce both IgG1 and IgG2a in mice, provide protection to S. Typhimurium infection via Ab. (ox.ac.uk)
- One of the most abundant components of the Hib outer membrane is the P2 porin, which has been shown to induce the release of several inflammatory cytokines. (cnr.it)
- Case 1 pharyngeal isolates were indistinguishable, whereas Case 2 pharyngeal isolates were distinguished based on an 18-bp deletion in the major outer membrane porin encoded by the porB gene, questioning the reliability of NG-MAST results. (nih.gov)
- they function as porins, allowing the passage of small molecules through the outer membrane. (cdc.gov)
- Electrophysiological experiments on bilayer lipid membranes showed that the isolated outer membrane major porin of Yersinia ruckeri (YrOmpF) exhibits activity typical of porins from Gram-negative bacteria, forming channels with a mean conductance of 230 pS (in 0.1 M KCl) and slight asymmetry with respect to the applied voltage. (actanaturae.ru)
- Porins, along with lipopolysaccharide, are known to be a quantitatively dominant component of the outer membrane (OM) of Gram-negative bacteria and to play a crucial role in the adaptation of microorganisms to changing environmental conditions. (actanaturae.ru)
- The inner part of the porin monomer channel is the hydrophilic surface of the beta-barrel, and the outer part is formed by adjacent parts of the loops (the pore mouth and vestibule region). (actanaturae.ru)
- Polymer partitioning from semidilute solutions of PEG mixtures studied with a number of membrane-spanning β-barrel channels of different origin: the voltage-dependent anion channel (VDAC) from outer mitochondrial membrane, bacterial porin OmpC, and channel-forming toxin alpha-hemolysin. (nih.gov)
- MspA contains two consecutive beta barrels with nonpolar outer surfaces that form a ribbon around the porin, which is too narrow to fit the thickness of the mycobacterial outer membrane in contemporary models. (nih.gov)
OmpF porin channel1
- For this study we select the ompF porin channel, found in the membrane of the E. coli bacterium. (springer.com)
Bacterial3
- Resistance to carbapenems occurs either through bacterial production of β-lactamase enzymes that hydrolyze (break down) the antimicrobial agent or through porin changes in the bacterial cell wall that reduce the permeability of the drug into the organism. (cdc.gov)
- Structure of the porin from a bacterial stalk. (mpg.de)
- Porins are present in bacterial CELL WALLS, as well as in plant, fungal, mammalian and other vertebrate CELL MEMBRANES and MITOCHONDRIAL MEMBRANES. (bvsalud.org)
PorB1
- Intragenic recombination between porin genes of the same allelic family is likely occurring in nature because mosaic gene structure has been reported in porB genes. (cdc.gov)
Small molecules2
- Porins transport ions and small molecules, while aquaporins transport water molecules. (pediaa.com)
- Generally, porins transport different types of molecules across the membrane, such as ions and small molecules. (pediaa.com)
Pathogenic1
- OmpU porins are increasingly recognized as key determinants of pathogenic host Vibrio interactions. (cee-m.fr)
Sininauhan1
- Hanke on Tampereen yliopiston, Helsingin yliopiston, Diakonia ammattikorkeakoulun ja Porin Sininauhan yhteinen voimannäyte. (porinsininauha.fi)
Yliopistokeskus1
- Porin yliopistokeskus on 1 400 opiskelijan, 150 asiantuntijan ja kahden yliopiston muodostama, verkostomaisesti toimiva monitieteinen yhteisö. (ucpori.fi)
Coli1
- The parameters of YrOmpF were compared with those of the classical OmpF porin from E. coli. (actanaturae.ru)
Mammalian1
- Using HeLa cells, we show that mammalian porins also function in mitochondrial CL metabolism. (elsevierpure.com)
Bacteria1
- The studied channel significantly differed from the porins of other bacteria by high values of its critical closing potential (Vc): Vc = 232 mV at pH = 7.0 and Vc = 164 mV at pH = 5.0. (actanaturae.ru)
Suomi1
- Kirja vapautuu Porin kävelykadulle osana Suomi 90 -haastetta. (bookcrossing.com)
Zagrebu1
- Porin u Zagrebu, u subotu, 23.03.2024. (porin.org)
Obitelji1
- Pjesma "Mali krug velikih ljudi" autora Ivana Dečaka u izvedbi Massima osvojila je Porin za Pjesmu godine, koju je posvetio obitelji, ali i posebno zdravstvenim djelatnicima, dok je Porin u kategoriji Novi izvođač godine osvojila Albina . (tvbec.at)
Determinants1
- The basic determinants of RRA PORIN are the stimulation and development of economic activities in the region, especially in areas with unused natural and economic resources, technological development, increasing competitiveness, and improving the adaptability of economic entities to the global market, increasing exports, attracting foreign investment, etc. (porin.hr)
Hydrophilic1
- Furthermore, the primary function of porins is the passive transport of hydrophilic molecules of various sizes and charges through the membrane. (pediaa.com)
Mice2
- In this study we report the unexpected finding that mice lacking IgG1, but not IgG2a, are substantially less protected after porin immunization than wild-type controls. (ox.ac.uk)
- IgG1-deficient mice produce more porin-specific IgG2a, resulting in total IgG levels that are similar to wild-type mice. (ox.ac.uk)
Mechanism2
- Variations in their structure or regulation of porin expression can provide a mechanism to escape from antibacterial pressure. (medscape.com)
- The results of electrophysiological experiments and theoretical analysis are discussed in terms of the mechanism for voltage-dependent closing of porin channels. (actanaturae.ru)
Regulation1
- We conclude that yeast porins have specific and critical functions in mitochondrial phospholipid metabolism and that porin-mediated regulation of CL metabolism appears to be evolutionarily conserved. (elsevierpure.com)
Nutrients2
- Porins are important for the transport of some nutrients and substrates. (pediaa.com)
- The growth rate of Mycobacterium smegmatis depends on sufficient porin-mediated influx of nutrients. (nih.gov)
Passive2
- The most significant feature of porins is the transport of molecules through passive diffusion . (pediaa.com)
- Furthermore, porins transport molecules through passive diffusion, while aquaporins transport water through simple diffusion or osmosis. (pediaa.com)
Organisms1
- Organisms with decreased susceptibility produced by porin changes alone often have lower MICs (2-8 µg/ml). (cdc.gov)
Structure1
- The transmembrane sequences are highly conserved among these porins and are able to form an amphipathic beta-sheet structure. (nih.gov)
Occur1
- Porins are water-filled pores that occur through the membrane from the exterior to the periplasm. (pediaa.com)
Channel1
- An x-ray analysis of the main porin from Mycobacterium smegmatis, MspA, revealed a homooctameric goblet-like conformation with a single central channel. (nih.gov)
Levels1
- Depletion of the porins Por1 and Por2 destabilized Ups1 and Ups2, decreased CL levels by 90%, and caused loss of Ups2-dependent phosphatidylethanolamine synthesis, but did not affect Ups2-independent phosphatidylethanolamine synthesis in mitochondria. (elsevierpure.com)
Jazz1
- PÄIHTEETÖN JAZZ-LEIRINTÄ 2018 Tervetuloa vieraaksemme Porin A- killan Päihteettömään Jazz- leirintään, joka järjestetään Porin A- killan piha- alueella jo 24. (a-kiltapori.fi)
Model1
- For demonstration, a simple model is assumed for the mobility/diffusivity of each ionic species and we compute the current-voltage relations for ompF porin in a wide range of conditions. (springer.com)
Album1
- Porin za Najbolje likovno oblikovanje osvojio je Filip Gržinčić upravo za album "Ennui", d ok je suradnja Pavela i Tedija Spalata osvojila Porin za Najbolju vokalnu suradnju na pjesmi "Ne daj na nas" . (tvbec.at)
Water1
- Aquaporins are a type of porins that especially transport water molecules across the membrane. (pediaa.com)
Economic1
- Rijeka Development Agency Porin promotes and implements regional economic development projects and creates a quality business climate, promoting regional potentials for the purpose of further growth and development of the region and economic entities through planning and management of sustainable development and cooperation with domestic and foreign investors. (porin.hr)