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PorinsBacterial Outer Membrane ProteinsSalmonella typhimuriumBacterial ProteinsVoltage-Dependent Anion ChannelsMycobacterium smegmatisCell Membrane PermeabilityCadaverineDelftia acidovoransIon Channelsbeta-LactamsLipid BilayersRhodobacterNeisseria meningitidisMolecular Sequence DataEscherichia coli ProteinsAmino Acid SequenceNeisseriaEnterobacterSalmonella typhiGene Expression Regulation, BacterialAnti-Bacterial AgentsBorrelia burgdorferiBorrelia burgdorferi GroupLyme DiseaseBorrelia InfectionsArthropod VectorsResearch ReportEscherichia coliStaphylococcaceaeCrystallizationCrystallography, X-RayCrystallographyNegative StainingOxalobacter formigenesColicinsVibrio choleraeVibrionaceaeVirulenceBileSucroseSignal TransductionModels, MolecularPhotographyImage Processing, Computer-AssistedAdjuvants, ImmunologicNeisseria gonorrhoeaeB-LymphocytesLymphocytesVoltage-Dependent Anion Channel 2Voltage-Dependent Anion Channel 1Mitochondrial Membrane Transport ProteinsPubMed
Porins: Porins are protein molecules that were originally found in the outer membrane of GRAM-NEGATIVE BACTERIA and that form multi-meric channels for the passive DIFFUSION of WATER; IONS; or other small molecules. Porins are present in bacterial CELL WALLS, as well as in plant, fungal, mammalian and other vertebrate CELL MEMBRANES and MITOCHONDRIAL MEMBRANES.Bacterial Outer Membrane Proteins: Proteins isolated from the outer membrane of Gram-negative bacteria.Salmonella typhimurium: A serotype of Salmonella enterica that is a frequent agent of Salmonella gastroenteritis in humans. It also causes PARATYPHOID FEVER.Bacterial Proteins: Proteins found in any species of bacterium.Voltage-Dependent Anion Channels: A family of voltage-gated eukaryotic porins that form aqueous channels. They play an essential role in mitochondrial CELL MEMBRANE PERMEABILITY, are often regulated by BCL-2 PROTO-ONCOGENE PROTEINS, and have been implicated in APOPTOSIS.Mycobacterium smegmatis: A rapid-growing, nonphotochromogenic species of MYCOBACTERIUM originally isolated from human smegma and found also in soil and water. (From Dorland, 28th ed)Cell Membrane Permeability: A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.Cadaverine: A foul-smelling diamine formed by bacterial decarboxylation of lysine.Delftia acidovorans: A species of gram-negative rod-shaped bacteria found ubiquitously and formerly called Comamonas acidovorans and Pseudomonas acidovorans. It is the type species of the genus DELFTIA.Ion Channels: Gated, ion-selective glycoproteins that traverse membranes. The stimulus for ION CHANNEL GATING can be due to a variety of stimuli such as LIGANDS, a TRANSMEMBRANE POTENTIAL DIFFERENCE, mechanical deformation or through INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS.beta-Lactams: Four-membered cyclic AMIDES, best known for the PENICILLINS based on a bicyclo-thiazolidine, as well as the CEPHALOSPORINS based on a bicyclo-thiazine, and including monocyclic MONOBACTAMS. The BETA-LACTAMASES hydrolyze the beta lactam ring, accounting for BETA-LACTAM RESISTANCE of infective bacteria.Lipid Bilayers: Layers of lipid molecules which are two molecules thick. Bilayer systems are frequently studied as models of biological membranes.Rhodobacter: A genus of gram-negative bacteria widely distributed in fresh water as well as marine and hypersaline habitats.Neisseria meningitidis: 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.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Neisseria: A genus of gram-negative, aerobic, coccoid bacteria whose organisms are part of the normal flora of the oropharynx, nasopharynx, and genitourinary tract. Some species are primary pathogens for humans.Enterobacter: Gram-negative gas-producing rods found in feces of humans and other animals, sewage, soil, water, and dairy products.Salmonella typhi: A serotype of SALMONELLA ENTERICA which is the etiologic agent of TYPHOID FEVER.Gene Expression Regulation, Bacterial: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.Anti-Bacterial Agents: Substances that reduce the growth or reproduction of BACTERIA.Borrelia burgdorferi: A specific species of bacteria, part of the BORRELIA BURGDORFERI GROUP, whose common name is Lyme disease spirochete.Borrelia burgdorferi Group: Gram-negative helical bacteria, in the genus BORRELIA, that are the etiologic agents of LYME DISEASE. The group comprises many specific species including Borrelia afzelii, Borellia garinii, and BORRELIA BURGDORFERI proper. These spirochetes are generally transmitted by several species of ixodid ticks.Lyme Disease: An infectious disease caused by a spirochete, BORRELIA BURGDORFERI, which is transmitted chiefly by Ixodes dammini (see IXODES) and pacificus ticks in the United States and Ixodes ricinis (see IXODES) in Europe. It is a disease with early and late cutaneous manifestations plus involvement of the nervous system, heart, eye, and joints in variable combinations. The disease was formerly known as Lyme arthritis and first discovered at Old Lyme, Connecticut.Borrelia Infections: Infections with bacteria of the genus BORRELIA.Arthropod Vectors: Arthropods, other than insects and arachnids, which transmit infective organisms from one host to another or from an inanimate reservoir to an animate host.Research Report: Detailed account or statement or formal record of data resulting from empirical inquiry.Escherichia coli: 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.Staphylococcaceae: Family of gram-positive, facultatively anaerobic bacteria, in the order Bacillales. Genera include Gemella, Macrococcus, Salinicoccus, and STAPHYLOCOCCUS.Crystallization: The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Crystallography: The branch of science that deals with the geometric description of crystals and their internal arrangement. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Negative Staining: The technique of washing tissue specimens with a concentrated solution of a heavy metal salt and letting it dry. The specimen will be covered with a very thin layer of the metal salt, being excluded in areas where an adsorbed macromolecule is present. The macromolecules allow electrons from the beam of an electron microscope to pass much more readily than the heavy metal; thus, a reversed or negative image of the molecule is created.Oxalobacter formigenes: The sole species of the genus Oxalobacter consisting of straight or curved gram-negative rods with rounded ends. Cells are nonmotile, nonsporing, and use oxylates as the only source of CARBON and energy, with formate and CARBON DIOXIDE as end products. They are isolated from lake sediments and from the rumen or large bowel of humans and animals. (From Bergey's Manual of Determinative Bacteriology, 9th ed)Colicins: Bacteriocins elaborated by strains of Escherichia coli and related species. They are proteins or protein-lipopolysaccharide complexes lethal to other strains of the same species.Vibrio cholerae: The etiologic agent of CHOLERA.Vibrionaceae: A family of gram-negative bacteria whose members predominate in the bacterial flora of PLANKTON; FISHES; and SEAWATER. Some members are important pathogens for humans and animals.Virulence: The degree of pathogenicity within a group or species of microorganisms or viruses as indicated by case fatality rates and/or the ability of the organism to invade the tissues of the host. The pathogenic capacity of an organism is determined by its VIRULENCE FACTORS.Bile: An emulsifying agent produced in the LIVER and secreted into the DUODENUM. Its composition includes BILE ACIDS AND SALTS; CHOLESTEROL; and ELECTROLYTES. It aids DIGESTION of fats in the duodenum.Sucrose: A nonreducing disaccharide composed of GLUCOSE and FRUCTOSE linked via their anomeric carbons. It is obtained commercially from SUGARCANE, sugar beet (BETA VULGARIS), and other plants and used extensively as a food and a sweetener.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Photography: Method of making images on a sensitized surface by exposure to light or other radiant energy.Image Processing, Computer-Assisted: A technique of inputting two-dimensional images into a computer and then enhancing or analyzing the imagery into a form that is more useful to the human observer.Adjuvants, Immunologic: Substances that augment, stimulate, activate, potentiate, or modulate the immune response at either the cellular or humoral level. The classical agents (Freund's adjuvant, BCG, Corynebacterium parvum, et al.) contain bacterial antigens. Some are endogenous (e.g., histamine, interferon, transfer factor, tuftsin, interleukin-1). Their mode of action is either non-specific, resulting in increased immune responsiveness to a wide variety of antigens, or antigen-specific, i.e., affecting a restricted type of immune response to a narrow group of antigens. The therapeutic efficacy of many biological response modifiers is related to their antigen-specific immunoadjuvanticity.Neisseria gonorrhoeae: A species of gram-negative, aerobic bacteria primarily found in purulent venereal discharges. It is the causative agent of GONORRHEA.B-Lymphocytes: Lymphoid cells concerned with humoral immunity. They are short-lived cells resembling bursa-derived lymphocytes of birds in their production of immunoglobulin upon appropriate stimulation.Lymphocytes: White blood cells formed in the body's lymphoid tissue. The nucleus is round or ovoid with coarse, irregularly clumped chromatin while the cytoplasm is typically pale blue with azurophilic (if any) granules. Most lymphocytes can be classified as either T or B (with subpopulations of each), or NATURAL KILLER CELLS.Voltage-Dependent Anion Channel 2: Voltage-dependent anion channel 2 is a low abundance mammalian isoform of VDAC that interacts with the inactive form of BAK PROTEIN.Voltage-Dependent Anion Channel 1: Voltage-dependent anion channel 1 is the major pore-forming protein of the mitochondrial outer membrane. It also functions as a ferricyanide reductase in the PLASMA MEMBRANE.Mitochondrial Membrane Transport Proteins: Proteins involved in the transport of specific substances across the membranes of the MITOCHONDRIA.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.

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)

Neisserial porins induce B lymphocytes to express costimulatory B7-2 molecules and to proliferate. | JEMNeisserial porins induce B lymphocytes to express costimulatory B7-2 molecules and to proliferate. | JEM
The neisserial porins are the major protein components of the outer membrane of the pathogenic Neisseria (N. meningitidis and N. gonorrhoeae). They have been shown to be able to enhance the immune response to poorly immunogenic substances (e.g., polysaccharides, peptides, glycolipids, etc.). To explore the basis of their potent adjuvant activity, the effect of the neisserial porins on T-B cell interactions and T cell costimulation was examined. Neisserial porins increased the surface expression of the costimulatory ligand B7-2 (CD86) but did not affect the expression of B7-1 (CD80). In addition, incubation with the neisserial porins increased the T lymphocyte costimulatory ability of B lymphocytes, which was inhibited by anti-B7-2 but not anti-B7-1 monoclonal antibodies. Upregulation of B7-2 on the surface of B lymphocytes may be the mechanism behind the immunopotentiating activity of neisserial porins. ...
Lipopolysaccharide-free Escherichia coli OmpF and Pseudomonas aeruginosa protein P porins are functionally active in lipid...Lipopolysaccharide-free Escherichia coli OmpF and Pseudomonas aeruginosa protein P porins are functionally active in lipid...
TY - JOUR. T1 - Lipopolysaccharide-free Escherichia coli OmpF and Pseudomonas aeruginosa protein P porins are functionally active in lipid bilayer membranes. AU - Parr, T. R.. AU - Poole, K.. AU - Crockford, G. W.K.. AU - Hancock, R. E.W.. PY - 1986/1/1. Y1 - 1986/1/1. UR - http://www.scopus.com/inward/record.url?scp=0022466549&partnerID=8YFLogxK. U2 - 10.1128/jb.165.2.523-526.1986. DO - 10.1128/jb.165.2.523-526.1986. M3 - Article. C2 - 3003028. AN - SCOPUS:0022466549. VL - 165. SP - 523. EP - 526. JO - Journal of bacteriology. JF - Journal of bacteriology. SN - 0021-9193. IS - 2. ER - ...
Identification of membrane spanning beta strands in bacterial porins. - Semantic ScholarIdentification of membrane spanning beta strands in bacterial porins. - Semantic Scholar
The membrane assembly of outer membrane proteins is more complex than that of transmembrane helical proteins owing to the intervention of many charged and polar residues in the membrane. Accordingly, the predictive accuracy of transmembrane beta strands is considerably lower than that of transmembrane alpha helices. In this paper we develop a set of conformational parameters for membrane spanning beta strands. We formulate an algorithm to predict the transmembrane beta strands in the family of bacterial porins based on the conformational parameters and surrounding hydrophobicities of amino acid residues. A Fortran program has been developed which takes the amino acid sequence as the input file and gives the predicted transmembrane beta strand as output. The present method predicts at an accuracy level of 82% for all the bacterial porins considered.
Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate | ScienceActivation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate | Science
The Tar chemoreceptor of Escherichia coli is a membrane-bound sensory protein that facilitates bacterial chemotaxis in response to aspartate. The EnvZ molecule has a membrane topology similar to Tar and is a putative osmosensor that is required for osmoregulation of the genes for the major outer membrane porin proteins, OmpF and OmpC. The cytoplasmic signaling domain of Tar was replaced with the carboxyl portion of EnvZ, and the resulting chimeric receptor activated transcription of the ompC gene in response to aspartate. The activation of ompC by the chimeric receptor was absolutely dependent on OmpR, a transcriptional activator for ompF and ompC. ...
Structural relatedness of enteric bacterial porins assessed wi...Structural relatedness of enteric bacterial porins assessed wi...
Structural relatedness of enteric bacterial porins assessed with monoclonal antibodies to Salmonella typhimurium OmpD and OmpC.: The immunochemistry and structu
Outer membrane porin D - WikipediaOuter membrane porin D - Wikipedia
Outer membrane porin D is a protein family containing bacterial outer membrane porins which are involved in transport of cationic amino acids, peptides, antibiotics and other compounds. It was also described as having some serine protease activity. However many of these proteins are not peptidases and are classified as non-peptidase homologues as they either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity of peptidases in the S43 family. Yoshihara E, Yoneyama H, Ono T, Nakae T (June 1998). "Identification of the catalytic triad of the protein D2 protease in Pseudomonas aeruginosa". Biochem. Biophys. Res. Commun. 247 (1): 142-5. doi:10.1006/bbrc.1998.8745. PMID 9636669. This article incorporates text from the public domain Pfam and InterPro ...
Overexpression of Protease-Deficient DegPS210ARescues the Lethal Phenotype of Escherichia coli OmpF Assembly Mutants in a degP...Overexpression of Protease-Deficient DegPS210ARescues the Lethal Phenotype of Escherichia coli OmpF Assembly Mutants in a degP...
The proper functioning of proteins requires their correct localization to predetermined cellular locations. In the gram-negative bacterium Escherichia coliK-12, a special class of proteins known as porins (24) must be properly targeted and assembled in the outer membrane to form channels that facilitate the diffusion of hydrophilic solutes. The atomic structure showed that porins primarily consist of antiparallel β strands that are arranged in a pseudocyclic β-barrel structure, which encloses a water-filled channel (6, 29). On the periplasmic side, β strands are adjoined by short turns, whereas long loops provide connections on the medium-exposed side. Although the majority of loops are surface exposed, one or more loops fold inward thus restricting the channel. Surface-exposed loops are often utilized by bacteriophages as their receptors (35, 36, 37).. Outer membrane proteins (OMPs) are synthesized in the cytoplasm as precursors with an amino-terminal signal sequence that assists in exiting ...
Antibiotics translocation through porins: an MD study | IRIS Univ. CagliariAntibiotics translocation through porins: an MD study | IRIS Univ. Cagliari
Gram-negative bacteria are protected against external attack by an outer membrane. However, general diffusion porins located in this membrane allow the entry, by simple diffusion, of small molecules and, among them, antibiotics (beta-lactams and fluoroquinolones). Strains of bacteria resistant to beta-lactams have shown either a low porin density in the outer membrane, or some mutations at the level of porins affecting their internal size. Understand how antibiotics diffuse through these porins can help researcher to develop new antibiotics with an improved penetration especially when resistance becomes a serious problem for infectious disease. Recent experimental investigations pointed out how the diffusion of antibiotics through a porin is a molecular-based process: during diffusion the antibiotics interact strongly with the amino acids of the porin. Changing either the charge or the hydrophobicity of antibiotics the interaction strenght with the porin changes as well. Using a recent algorithm ...
Structural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli | PNASStructural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli | PNAS
A strain of Escherichia coli, selected on the basis of its resistance to colicin N, reveals distinct structural and functional alterations in unspecific OmpF porin. A single mutation [Gly-119--,Asp (G119D)] was identified in the internal loop L3 that contributes critically to the formation of the construction inside the lumen of the pore. X-ray structure analysis to a resolution of 3.0 A reveals a locally altered peptide backbone, with the side chain of residue Asp-119 protruding into the channel, causing the area of the constriction (7 x 11 A in the wild type) to be subdivided into two intercommunicating subcompartments of 3-4 A in diameter. The functional consequences of this structural modification consist of a reduction of the channel conductance by about one-third, of altered ion selectivity and voltage gating, and of a decrease of permeation rates of various sugars by factors of 2-12. The structural modification of the mutant protein affects neither the beta-barrel structure nor those ...
Sucrose-specific porin molecule - Stock Image F009/5873 - Science Photo LibrarySucrose-specific porin molecule - Stock Image F009/5873 - Science Photo Library
Sucrose-specific porin, molecular model. Porins are proteins that span cell membranes and act as a channel through which specific molecules can diffuse. - Stock Image F009/5873
Projection structure of the monomeric porin OmpG at 6 A resolutionProjection structure of the monomeric porin OmpG at 6 A resolution
The Escherichia coli porin OmpG, which acts as an efficient unspecific channel for mono-, di- and trisaccharides, has been purified and crystallized in two dimensions. Projection maps of two different crystal forms of OmpG at 6 A resolution show that the protein has a beta-barrel structure character …
RCSB PDB - 1GFM: OMPF PORIN (MUTANT D113G) Structure Summary PageRCSB PDB - 1GFM: OMPF PORIN (MUTANT D113G) Structure Summary Page
1GFM: Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis.
Life of a Lab Rat: Bacterial evolution: negative to positive?Life of a Lab Rat: Bacterial evolution: negative to positive?
figure taken from the reference below). Murein means peptidoglycan cell wall and the cytoplasm denotes the inside of the cell. In this scenario, the double-membraned proto-bacteria (which has spend the last half-a-billion years or so evolving a well adjusted double membrane system) suddenly looses the outer membrane. A very simple genetic change would lead to a massively overgrown cell wall, which would rip the outer membrane away. The cell looses all its outer membrane porins, and signal systems, but in return gains a highly protective cell wall, which potentially allows it to survive in different niches. How these aspects are lost genetically is another matter, and the paper rather hand-waves away by saying that unused genes tend to get lost eventually. Which is true in bacteria, they have such a small genome they dont want it getting filled up with unnecessary genes, but I have a feeling genes tend to leave something behind. Even so, the question of where the now-unnecessary genes go is ...
RCSB PDB for 1GFNRCSB PDB for 1GFN
1GFN: Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis.
Translocation mechanism of long sugar chains across the maltoporin membrane channelTranslocation mechanism of long sugar chains across the maltoporin membrane channel
Maltoporin allows permeation of long maltodextrin chains. It tightly binds the amphiphilic sugar, offering both hydrophobic interactions with a helical lane of aromatic residues and H bonds with ionic side chains. The minimum-energy path of maltohexaose translocation is obtained by the conjugate pea …
Phylogenetic Analysis of the Chlamydia trachomatis Major Outer Membrane Protein and Examination of Potential Pathogenic...Phylogenetic Analysis of the Chlamydia trachomatis Major Outer Membrane Protein and Examination of Potential Pathogenic...
Phylogenetic analysis was utilized to investigate biological relationships (tissue tropism, disease presentation, and epidemiologic success), as evidenced by coevolution, among human strains ofChlamydia trachomatis. Nucleotide sequences ofomp1, the gene encoding the major outer membrane protein (MOMP) of C. trachomatis, were determined for 40 strains representing 11 serovars. These data were combined with availableomp1 sequences from GenBank for an analysis encompassing a total of 69 strains representing 17 serovars infecting humans. Phylogenetic analysis of the nucleotide and inferred amino acid sequences showed no evolutionary relationships among serovars that corresponded to biological or pathological phenotypes (tissue tropism, disease presentation, and epidemiologic success). In addition, no specific residues that may have evolved to play a role in determining biologically relevant characteristics of chlamydia, such as tissue specificity, disease presentation, and epidemiologic success, ...
Priming with Chlamydia trachomatis Major Outer Membrane Protein (MOMP) DNA followed by MOMP ISCOM Boosting Enhances Protection...Priming with Chlamydia trachomatis Major Outer Membrane Protein (MOMP) DNA followed by MOMP ISCOM Boosting Enhances Protection...
A vaccine against C. trachomatis infection has proven difficult to develop. Early vaccine studies showed that whole inactivated bacterial cells administered intramuscularly were partially protective in human and primate trials. Primate vaccine trials and human experimental infection studies suggested that C. trachomatis immunity was in part strain specific, and the identification of MOMP as the strain-specific antigen of C. trachomatis quickly focused vaccine efforts on this protein. In general, use of MOMP or peptide epitopes derived from it as a vaccine has engendered variable or no protective immunity in a variety of animal model systems. The best results were observed when MOMP was used as a structurally intact molecule, suggesting that conformationally intact antigenic sites on the molecule are important for protective immunity.. We previously reported that MOMP DNA administered parenterally was also partially effective in inducing protective immunity against lung infection with MoPn. The ...
SMART: Pfam domain Porin 3SMART: Pfam domain Porin 3
This entry represents both eukaryotic mitochondrial porins and Tom40 proteins.. Eukaryotic mitochondrial porins are voltage-dependent anion-selective channels (VDAC) that behave as general diffusion pores for small hydrophilic molecules [ (PUBMED:8031826) (PUBMED:1384178) (PUBMED:1689252) (PUBMED:2442148) ]. The channels adopt an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The eukaryotic mitochondrial porins are beta-barrel proteins, composed of between 12 to 16 beta-strands that span the mitochondrial outer membrane. Yeast contains two members of this family (genes POR1 and POR2); vertebrates have at least three members (genes VDAC1, VDAC2 and VDAC3) [ (PUBMED:8812436) ]. They are related to the mitochondrial import receptor subunit Tom40 proteins, sharing a common evolutionary origin and structure [ (PUBMED:22178864) ]. Tom40 is a mitochondrion outer membrane protein and a component of the TOM (translocator of the outer ...
The role of mitochondrial porins and the permeability transition pore in learning and synaptic plasticity<...The role of mitochondrial porins and the permeability transition pore in learning and synaptic plasticity<...
TY - JOUR. T1 - The role of mitochondrial porins and the permeability transition pore in learning and synaptic plasticity. AU - Weeber, Edwin J.. AU - Levy, Michael. AU - Sampson, Margaret J.. AU - Anflous, Keltoum. AU - Armstrong, Dawna L.. AU - Brown, Sarah E.. AU - David Sweatt, J.. AU - Craigen, William J.. PY - 2002/5/24. Y1 - 2002/5/24. N2 - Mitochondrial outer membrane permeability is conferred by a family of porin proteins. Mitochondrial porins conduct small molecules and constitute one component of the permeability transition pore that opens in response to apoptotic signals. Because mitochondrial porins have significant roles in diverse cellular processes including regulation of mitochondrial ATP and calcium flux, we sought to determine their importance in learning and synaptic plasticity in mice. We show that fear conditioning and spatial learning are disrupted in porin-deficient mice. Electrophysiological recordings of porin-deficient hippocampal slices reveal deficits in long and ...
Altered expression of the ToxR-regulated porins OmpU and OmpT diminishes Vibrio cholerae bile resistance, virulence factor...Altered expression of the ToxR-regulated porins OmpU and OmpT diminishes Vibrio cholerae bile resistance, virulence factor...
In the current study, the construction of a toxR+ V. cholerae strain that expresses the ToxR-repressed porin OmpT in place of the ToxR-activated porin OmpU has allowed us to dissect the role these porins play in V. cholerae pathogenesis. Amazingly, merely substituting one outer membrane porin for another resulted in a number of attenuated pathogenic properties, including bile resistance, virulence factor expression, and intestinal colonization. ToxR-dependent regulation of outer membrane porins appears to have preceded the evolution of V. cholerae, because ToxR performs similar functions in other members of the Vibrionaceae (14, 17). However, these other bacteria do not have the additional regulatory factors TcpP and ToxT whose genes are located on the V. cholerae-specific pathogenicity island VPI (30). The recruitment of the ancestral ToxR protein into the virulence regulatory cascade involving recently acquired elements ties porin regulation to pathogenesis. We suggest that the contribution of ...
Role of β-Lactamases and Porins in Resistance to Ertapenem and Other β-Lactams in Klebsiella pneumoniae | Antimicrobial Agents...Role of β-Lactamases and Porins in Resistance to Ertapenem and Other β-Lactams in Klebsiella pneumoniae | Antimicrobial Agents...
Ertapenem is a potent carbapenem antibiotic for most clinical isolates of Klebsiella pneumoniae, with a typical MIC at which 90% of the isolates tested are inhibited of 0.03 to 0.06 μg/ml (6, 9), but occasional strains for which the MICs are ≥16 μg/ml have been detected (6, 7). In one such strain resistance was dependent on the presence of the plasmid-mediated extended-spectrum β-lactamase (ESBL) SHV-2 and additional host events presumably affecting ertapenem permeativity (7). Further studies were undertaken to elucidate the contribution of β-lactamase and host mutation to such exceptional resistance.. The K. pneumoniae strain for which the ertapenem MIC was 16 μg/ml was treated with ethidium bromide to cure the resident plasmid. The ertapenem MIC for the resulting strain, C2, was still elevated at l μg/ml, and the strain was found to be defective in expression of outer membrane porins OmpK35 and OmpK36 (10). To evaluate the influence of different β-lactamases on the ertapenem ...
Roles of the Carboxy-Terminal Half of Pseudomonas aeruginosa Major Outer Membrane Protein OprF in Cell Shape, Growth in Low...Roles of the Carboxy-Terminal Half of Pseudomonas aeruginosa Major Outer Membrane Protein OprF in Cell Shape, Growth in Low...
Our results provide some important confirmation of theories regarding OprF structure and function. We have demonstrated that residues in the C-terminal domain of OprF are required for strong peptidoglycan association, as previously proposed (9). Expression of our truncated OprF mutants in E. coli orP. aeruginosa suggests that the first 154 to 163 aa of OprF are needed to produce a stable protein. This possibility is in strong agreement with the proposal that the first 160 aa of OprF form a β-barrel structure and suggests that residues critical to proper conformation of this domain are present between aa 154 and 163. The residues between aa 150 and 160 conform to the consensus sequence of the 16th C-terminal β strand of the porin superfamily (21, 22). Studies of other porins, such as E. coli PhoE, suggest that a phenylalanine residue in this terminal strand (equivalent to OprF residue 160) is critical for protein stability and proper folding (8). Our results may thus reflect deletion of such a ...
Major outer membrane protein elisa and antibodyMajor outer membrane protein elisa and antibody
Shop Major outer membrane protein ELISA Kit, Recombinant Protein and Major outer membrane protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Page:Studies in the Scriptures - Series I - The Plan of the Ages (1909).djvu/271 - Wikisource, the free online libraryPage:Studies in the Scriptures - Series I - The Plan of the Ages (1909).djvu/271 - Wikisource, the free online library
As we compare the condition of the world to-day with its condition at any former period, we find a marked differ- ence in the sentiments of the masses. The spirit of inde- pendence is now abroad, and men are not so easily blind- folded, deceived and led by rulers and politicians, and therefore they will not submit to the yokes of former days. This change of public sentiment has not been a gradual one from the very beginning of mans effort to govern L t pi- self, but clearly marked only as far back as the sixteenth century ; and its progress has been most rapid within the last fifty years. This change, therefore, is not the result of the experience of past ages, but is the natural result of the recent increase and general diffusion of knowledge among the masses of mankind. The preparation for this general diffusion of knowledge began with the invention of printing, about 1440 A. D., and the consequent multiplica- tion of books and news periodicals. The influence of this invention in the general ...
PublicationsPublications
2017. Trebosc, V. et al. "Reversion of Antibiotic Resistance in Mycobacterium tubercolosis by spiroisoxazoline SMARt-420″. Science 2017. Mar 2017 Vol. 355, Issue 6330, pp. 1206-1211 doi: 10.1126/science.aag1006. A. Gilardi, S.P. Bhamidimarri, M. Broenstrup, U. Bilitewski, R.K.R. Marreddy, K.M. Pos, L. Benier, P. Gribbon, M. Winterhalter, B. Windshuegel. "Biophysical characterization of E. coli TolC interaction with the known blocker hexaamminecobalt".Biochim Biophys Acta. 2017 Nov;1861(11 Pt A):2702-2709. Epub 2017 Jul 23. doi: 10.1016/j.bbagen.2017.07.014. Ramaswamy, V. K., Vargiu, A.V., Malloci, G., Dreier, J. G., & Ruggerone, P. "Molecular rationale behind the differential substrate specificity of bacterial RND multi-drug transporters". Scientific Reports 7, Article number: 8075(2017) doi:10.1038/s41598-017-08747-8. Harsha Bajaj, Silvia Acosta-Gutiérrez, Igor Bodrenko, Giuliano Malloci, Mariano Andrea Scorciapino, Mathias Winterhalter and Matteo Ceccarelli. "Bacterial Outer Membrane Porins ...
Simulations contribute to study on critical bacterial outer membrane protein - University of Oxford, Medical Sciences DivisionSimulations contribute to study on critical bacterial outer membrane protein - University of Oxford, Medical Sciences Division
Molecular dynamics simulations by Department of Biochemistrys Dr Phillip Stansfeld, in the lab of Professor Mark Sansom, have helped to reveal how bacteria construct a barrier against antibiotics and the bodys immune system.
Dynamics and Interactions of OmpF and LPS : Influence on Pore Accessibility and Ion PermeabilityDynamics and Interactions of OmpF and LPS : Influence on Pore Accessibility and Ion Permeability
The asymmetric outer membrane of Gram-negative bacteria is formed of the inner leaflet with phospholipids and the outer leaflet with lipopolysaccharides (LPS). Outer membrane protein F (OmpF) is a trimeric porin responsible for the passive transport of small molecules across the outer membrane of Escherichia coli. Here, we report the impact of different levels of heterogeneity in LPS environments on the structure and dynamics of OmpF using all-atom molecular dynamics simulations. The simulations provide insight into the flexibility and dynamics of LPS components that are highly dependent on local environments, with lipid A being the most rigid and O-antigen being the most flexible. Increased flexibility of O-antigen polysaccharides is observed in heterogeneous LPS systems, where the adjacent O-antigen repeating units are weakly interacting and thus more dynamic, compared to homogeneous LPS systems in which LPS interacts strongly with each other with limited overall flexibility due to dense ...
JCI - Volume 115, Issue 5JCI - Volume 115, Issue 5
Pseudomonas aeruginosa is an important opportunistic pathogen that can cause chronic and often life-threatening infections of the respiratory tract, particularly in individuals with cystic fibrosis (CF). Because infections with P. aeruginosa remain the major cause of the high morbidity and mortality of CF, a vaccine against P. aeruginosa would be very useful for preventing this disorder. The outer membrane protein F (OprF) of P. aeruginosa is a promising vaccine candidate and various B cell epitopes within OprF have been identified. Given that adenovirus (Ad) vectors have strong immunogenic potential and can function as adjuvants for genetic vaccines, the present study evaluates the immunogenic and protective properties of a novel replication-deficient Ad vector in which the Ad hexon protein was modified to include a 14-amino acid epitope of P. aeruginosa OprF (Epi8) in loop 1 of the hypervariable region 5 of the hexon (AdZ.Epi8). Immunization of C57BL/6 mice with AdZ.Epi8 resulted in detectable ...
Massive antibody discovery used to probe structure-function relationships of the essential outer membrane protein LptD | eLifeMassive antibody discovery used to probe structure-function relationships of the essential outer membrane protein LptD | eLife
Dispensable loops shield the functionally-important extracellular loops of the essential Gram-negative bacterial outer membrane protein LptD from antibody interference.
Nanoparticles | Profiles RNSNanoparticles | Profiles RNS
Anand A, LeDoyt M, Karanian C, Luthra A, Koszelak-Rosenblum M, Malkowski MG, Puthenveetil R, Vinogradova O, Radolf JD. Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL ß-BARREL DOMAIN. J Biol Chem. 2015 May 08; 290(19):12313-31 ...
Protein trimer - WikipediaProtein trimer - Wikipedia
In biochemistry, a protein trimer is a macromolecular complex formed by three, usually non-covalently bound, macromolecules like proteins or nucleic acids. A homo-trimer would be formed by three identical molecules. A hetero-trimer would be formed by three different macromolecules. Type II Collagen is an example of homo-trimeric protein. Porins usually arrange themselves in membranes as trimers. ...
Oligogalacturonate-specific porin elisa and antibodyOligogalacturonate-specific porin elisa and antibody
Shop Oligogalacturonate-specific porin ELISA Kit, Recombinant Protein and Oligogalacturonate-specific porin Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
4ctd » Outer membrane protein G (OMPG), with truncated extracellular loops - Orientations of Proteins in Membranes (OPM)...4ctd » Outer membrane protein G (OMPG), with truncated extracellular loops - Orientations of Proteins in Membranes (OPM)...
A - Tilt: 3° - Segments: 1( 6- 16), 2( 31- 39), 3( 43- 50), 4( 68- 78), 5( 85- 92), 6( 111- 120), 7( 128- 136), 8( 151- 160), 9( 167- 174), 10( 192- 201), 11( 204- 214), 12( 223- 230), 13( 237- 244), 14( 259- 268 ...
2x9k » Outer membrane protein G (OMPG), open state 2 - Orientations of Proteins in Membranes (OPM) database2x9k » Outer membrane protein G (OMPG), open state 2 - Orientations of Proteins in Membranes (OPM) database
A - Tilt: 5° - Segments: 1( 6- 16), 2( 31- 41), 3( 42- 50), 4( 68- 78), 5( 84- 92), 6( 111- 122), 7( 127- 135), 8( 151- 161), 9( 166- 173), 10( 192- 200), 11( 204- 212), 12( 234- 244), 13( 247- 256), 14( 271- 279 ...
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Systémová enzýmoterapia pre odborníkovSystémová enzýmoterapia pre odborníkov
Phlogenzym je obvykle dobre znášaný, ani pri dlhodobom užívaní vysokých dávok neboli pozorované nežiaduce účinky. Pôsobením enzýmov môžu nastať neškodné zmeny farby, pachu a konzistencie stolice. Počas užívania vyšších jednorázových dávok sa môžu objaviť pocity plnosti, nafukovania a výnimočne pocit nevoľnosti. Tomu sa dá zabrániť rozdelením dávky na viacero dávok v priebehu dňa. Ak tieto príznaky aj po znížení dávky pretrvávajú, poraďte sa s lekárom. Zriedka pozorované alergické reakcie (kožná vyrážka) odoznejú po vysadení lieku. Pri ich prípadnom výskyte prerušte užívanie Phlogenzymu a poraďte sa s lekárom. Zriedkavými nežiaducimi účinkami sú: bolesť hlavy, pocit hladu a zvýšená potivosť. S lekárom sa o ďalšom užívaní Phlogenzymu poraďte aj v prípade výskytu akýchkoľvek neobvyklých reakcií ...
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vdac-1 - Probable voltage-dependent anion-selective channel - Caenorhabditis elegans - vdac-1 gene & proteinvdac-1 - Probable voltage-dependent anion-selective channel - Caenorhabditis elegans - vdac-1 gene & protein
Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules (By similarity). Plays a role in maintaining mitochondrial morphology (PubMed:25190516).
VDAC3 - Voltage-dependent anion-selective channel protein 3 - Homo sapiens (Human) - VDAC3 gene & proteinVDAC3 - Voltage-dependent anion-selective channel protein 3 - Homo sapiens (Human) - VDAC3 gene & protein
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
BAX Polyclonal Antibody (KO Validated) | GoldBioBAX Polyclonal Antibody (KO Validated) | GoldBio
The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein forms a heterodimer with BCL2, and functions as an apoptotic activator. This protein is reported to interact with, and increase the opening of, the mitochondrial voltage-dependent anion channel (VDAC), which leads to the loss in membrane potential and the release of cytochrome c. The expression of this gene is regulated by the tumor suppressor P53 and has been shown to be involved in P53-mediated apoptosis. Multiple alternatively spliced transcript variants, which encode different isoforms, have been reported for this gene. Product Name ...
BAX Polyclonal Antibody (KO Validated) | GoldBioBAX Polyclonal Antibody (KO Validated) | GoldBio
The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein forms a heterodimer with BCL2, and functions as an apoptotic activator. This protein is reported to interact with, and increase the opening of, the mitochondrial voltage-dependent anion channel (VDAC), which leads to the loss in membrane potential and the release of cytochrome c. The expression of this gene is regulated by the tumor suppressor P53 and has been shown to be involved in P53-mediated apoptosis. Multiple alternatively spliced transcript variants, which encode different isoforms, have been reported for this gene. Product Name ...
BAK1 antibodies | AntibodypediaBAK1 antibodies | Antibodypedia
The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein localizes to mitochondria, and functions to induce apoptosis. It interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, which leads to a loss in membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 after exposure to cell stress. [provided by RefSeq, Jul 2008] ...
Probing sugar translocation through maltoporin at the single channel level.Probing sugar translocation through maltoporin at the single channel level.
Sugar permeation through maltoporin of Escherichia coli, a trimer protein that facilitates maltodextrin translocation across outer bacterial membranes, was investigated at the single channel level. For large sugars, such as maltohexaose, elementary e
A Bacteria and a Nematode: Natural Born Pest KillersA Bacteria and a Nematode: Natural Born Pest Killers
Khandelwal and colleagues succeeded in identifying the insecticidal factor. The active component was found in a large complex normally associated with the bacterial outer membrane, and was also present in or on outer membrane vesicles (OMVs) released from the bacterial surface, says Khandelwal. They then searched through OMV components and identified a small (17 kDa) toxic protein. When purified, this protein was toxic to cultured larval cells and directly killed H. armigera larvae. Gene cloning and sequencing showed this protein is related to a class of bacterial outer membrane proteins that form protrusions, called pili or fimbriae, which often help bacteria attach to host cells during infection. Similar to pili proteins, the purified 17 kDa protein self-associated to form oligomers, each of which was connected to the next by a strand. Most importantly, the recombinant 17 kDa protein killed H. armigera larvae, demonstrating its potential as a biological control agent in a world desperately in ...
Multi-zone fixed-bed or moving-bed reactor with an integrated heat exchanger - Patent # 8609913 - PatentGeniusMulti-zone fixed-bed or moving-bed reactor with an integrated heat exchanger - Patent # 8609913 - PatentGenius
An axial flow staged zone oligomerization reaction process includes the steps of passing a hydrocarbon feedstock into the lower portion of the axial flow staged zone reactor which includes axial circulation of the hydrocarbon reaction fluid serially in each of the reaction zones, passing catalyst through a constriction zone located between successive upper and lower catalytic reaction zones which includes heat exchanging of the fluids being the constriction zone within the reactor and further includes withdrawing the oligomerized product from the top of the reactor.
Most recent papers with the keyword Salmonella porins | Read by QxMDMost recent papers with the keyword Salmonella porins | Read by QxMD
Introduction. The marA, soxS, ramA, acrB and ompF genes have been studied in order to characterize mechanisms of AcrAB-TolC active efflux pumps and membrane permeability alterations that reduce fluoroquinolones susceptibility in Salmonella spp. Methods. Mutations in marA, soxS, ramA, acrB and ompF genes were detected, as well as their expression levels in presence and absence of ciprofloxacin, calculating the level of change between them by qPCR. Data were analysed by using SPSS 19.0. Results. No mutations in these genes were found, but both AcrAB-TolC regulatory genes and structural acrB gene expression were affected by ciprofloxacin in both mutant strains and wild type bacterial strains (WT ...
University of Birmingham research gatewayUniversity of Birmingham research gateway
TY - JOUR. T1 - The effect of altered porin expression in Escherichia coli upon susceptibility to 4-quinolones. AU - Piddock, L J. AU - Wise, R. PY - 1986/10. Y1 - 1986/10. KW - Bacterial Proteins. KW - Escherichia coli. KW - Gene Expression Regulation. KW - Microbial Sensitivity Tests. KW - Quinolines. M3 - Article. C2 - 3533892. VL - 18. SP - 547. EP - 549. JO - Journal of Antimicrobial Chemotherapy. JF - Journal of Antimicrobial Chemotherapy. SN - 0305-7453. IS - 4. ER - ...
Define diffusion. Mention the characters, significance and the factors affecting the rate of diffusion. Differentiate between...Define diffusion. Mention the characters, significance and the factors affecting the rate of diffusion. Differentiate between...
Simple and facilitated diffusion: Diffusion of molecules or ions through a membrane is of two types - simple and facilitated. The simple diffusion refers to the type of transfer in which the diffusing molecules or ions do not combine with the constituents of the membrane. For example, gases like oxygen, carbon dioxide etc., and water molecules diffuse readily through gas created by the random movement of fatty acyl chain of lipids. The facilitated diffusion is the movement through the membrane with the help of certain transport proteins. Membranes have several such proteins which facilitate the diffusion of solutes (Cl-, HCO3- etc.) Plasma membranes of some organisms have protein pores called, porins which are water-filled transmembrane channels.. ...
Import of porin is inhibited into tom40 mutant mitochon | Open-iImport of porin is inhibited into tom40 mutant mitochon | Open-i
Import of porin is inhibited into tom40 mutant mitochondria. (A) Radiolabeled porin precursor (10 μl reticulocyte lysate per lane) was incubated with isolated
RegulonDBRegulonDB
The expression of the clpP gene, and probably the expression of the complete clpPX operon that codes for a protease, is affected by antibiotic pressure. As the antibiotic (tetracycline) concentration increases, the gene expression also increases. The role of the induced protease could be the degradation of porins to protect the cell against the antibiotic ,CITS: [17426813],. ...
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Modne Diagnozy: 95. Publikacje naukowe z okresu poradni nadciśnieniowejModne Diagnozy: 95. Publikacje naukowe z okresu poradni nadciśnieniowej
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Opacity porins - WikipediaOpacity porins - Wikipedia
Porin - WikipediaPorin - Wikipedia
Putative porin-10 (IPR025631) | InterPro | EMBL-EBIPutative porin-10 (IPR025631) | InterPro | EMBL-EBI
Outer membrane porin, bacterial (IPR005318) | InterPro | EMBL-EBIOuter membrane porin, bacterial (IPR005318) | InterPro | EMBL-EBI
GC37X64 Porin pirunkirnu (Traditional Cache) in Finland created by PorilainenGC37X64 Porin pirunkirnu (Traditional Cache) in Finland created by Porilainen
Porins of Borrelia burgdorferiPorins of Borrelia burgdorferi
RCSB PDB - Protein Feature View - Probable porin - Q9HZH0 (Q9HZH0 PSEAE)RCSB PDB - Protein Feature View - Probable porin - Q9HZH0 (Q9HZH0 PSEAE)
RCSB PDB - 1GFM: OMPF PORIN (MUTANT D113G) Structure Summary PageRCSB PDB - 1GFM: OMPF PORIN (MUTANT D113G) Structure Summary Page
Porin tutorial textPorin tutorial text
Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. - PubMed - NCBIIntrinsically disordered protein threads through the bacterial outer-membrane porin OmpF. - PubMed - NCBI
Projection structure of the monomeric porin OmpG at 6 A resolutionProjection structure of the monomeric porin OmpG at 6 A resolution
Anti-VDAC1 / Porin antibody [20B12AF2] (ab14734) ReferencesAnti-VDAC1 / Porin antibody [20B12AF2] (ab14734) References
Detection of β-Lactamases and Outer Membrane Porins among Klebsiella pneumoniae Strains Isolated in IranDetection of β-Lactamases and Outer Membrane Porins among Klebsiella pneumoniae Strains Isolated in Iran
Novel Mechanism of Escherichia coli Porin Regulation | Journal of BacteriologyNovel Mechanism of Escherichia coli Porin Regulation | Journal of Bacteriology
Annotation of Transmembrane Segments of Experimentally Solved Bacterial Porins and AdhesinsAnnotation of Transmembrane Segments of Experimentally Solved Bacterial Porins and Adhesins
VDAC1 / Porin antibody - Mitochondrial Loading Control (ab15895) | AbcamVDAC1 / Porin antibody - Mitochondrial Loading Control (ab15895) | Abcam
Dynamics of carbon nanotube porins | Philosophical Transactions of the Royal Society B: Biological SciencesDynamics of carbon nanotube porins | Philosophical Transactions of the Royal Society B: Biological Sciences
Porin molecule - Stock Image C035/8390 - Science Photo LibraryPorin molecule - Stock Image C035/8390 - Science Photo Library
Structural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli | PNASStructural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli | PNAS
Membrane-derived oligosaccharides (MDOs) promote closing of an E. coli porin channel. - PubMed - NCBIMembrane-derived oligosaccharides (MDO's) promote closing of an E. coli porin channel. - PubMed - NCBI
Altered expression of the ToxR-regulated porins OmpU and OmpT diminishes Vibrio cholerae bile resistance, virulence factor...Altered expression of the ToxR-regulated porins OmpU and OmpT diminishes Vibrio cholerae bile resistance, virulence factor...
kdgM - Oligogalacturonate-specific porin KdgM precursor - Dickeya dadantii (strain 3937) - kdgM gene & proteinkdgM - Oligogalacturonate-specific porin KdgM precursor - Dickeya dadantii (strain 3937) - kdgM gene & protein
Sucrose-specific porin molecule - Stock Image F009/5873 - Science Photo LibrarySucrose-specific porin molecule - Stock Image F009/5873 - Science Photo Library
Function and Structure of OmpF PorinFunction and Structure of OmpF Porin
porin deficiency | Antimicrobial Agents and Chemotherapyporin deficiency | Antimicrobial Agents and Chemotherapy
Mouse Anti-Human Porin 31HL Monoclonal Antibody, Unconjugated, Clone 89-173/016 from CalbiochemMouse Anti-Human Porin 31HL Monoclonal Antibody, Unconjugated, Clone 89-173/016 from Calbiochem
Neisserial porins induce B lymphocytes to express costimulatory B7-2 molecules and to proliferate. | JEMNeisserial porins induce B lymphocytes to express costimulatory B7-2 molecules and to proliferate. | JEM
Comment on Enhanced water permeability and tunable ion selectivity in subnanometer carbon nanotube porins | ScienceComment on "Enhanced water permeability and tunable ion selectivity in subnanometer carbon nanotube porins" | Science
Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins. | Journal of BacteriologyPorin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins. | Journal of Bacteriology
Porins in prokaryotes and eukaryotes: common themes and variations | Biochemical JournalPorins in prokaryotes and eukaryotes: common themes and variations | Biochemical Journal
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PorinsBacterial Outer Membrane ProteinsSalmonella typhimuriumBacterial ProteinsVoltage-Dependent Anion ChannelsMycobacterium smegmatisCell Membrane PermeabilityCadaverineDelftia acidovoransIon Channelsbeta-LactamsLipid BilayersRhodobacterNeisseria meningitidisMolecular Sequence DataEscherichia coli ProteinsAmino Acid SequenceNeisseriaEnterobacterSalmonella typhiGene Expression Regulation, BacterialAnti-Bacterial AgentsBorrelia burgdorferiBorrelia burgdorferi GroupLyme DiseaseBorrelia InfectionsArthropod VectorsResearch ReportEscherichia coliStaphylococcaceaeCrystallizationCrystallography, X-RayCrystallographyNegative StainingOxalobacter formigenesColicinsVibrio choleraeVibrionaceaeVirulenceBileSucroseSignal TransductionModels, MolecularPhotographyImage Processing, Computer-AssistedAdjuvants, ImmunologicNeisseria gonorrhoeaeB-LymphocytesLymphocytesVoltage-Dependent Anion Channel 2Voltage-Dependent Anion Channel 1Mitochondrial Membrane Transport ProteinsPubMed
ProteinsMembranesGenesAbstractPseudomonasPermeabilityOmpC and OmpFTrimersSmall MoleculesHuman VDAC1MolecularMoleculesMutantsBacterial outer membrane porinsTrimericBacteriaCharacterizationOmpK35Functions as a porinInsertion into the outer membraneSalmonellaPutativeAnion-selective porinCarbon nanotube porinsGeneVoltage-DependeConductanceOmpF PorinStability of porinTransmembraneRegulationOmpUTranslocationColi porinMutantLiposomesExpressionMycobacteriumPrecursorSolutesMajor outer membrane proteinResistanceMitochondrial outerImmunogenTyphimurium
Proteins32
Membranes9
Genes11
  • However, ToxR, independently of TcpP and ToxT, activates and represses transcription of the genes encoding two outer-membrane porins, OmpU and OmpT. (pnas.org)
  • Although genes encoding TcpP, ToxT, CT, and TCP are specifically associated with V. cholerae , ToxR is found in other Vibrio and Photobacterium species and regulates porin expression in these other bacteria as well ( 13 , 14 ). (pnas.org)
  • The sizes of PCR-amplified products from ompF -type genes are different from those of other porin genes (data not shown). (asm.org)
  • Expression levels of efflux and porin genes were mesured by real-time reverse transcription PCR. (jidc.org)
  • However, the regulation of porin genes and its own gene by CRP remains unclear in Y. pestis . (biomedcentral.com)
  • It is likely that Y. pestis OmpR and CRP respectively sense different signals (medium osmolarity, and cellular cAMP levels) to regulate porin genes independently. (biomedcentral.com)
  • Data presented here indicate a remarkable remodeling of the CRP-mediated regulation of porin genes and of its own one between these two bacteria. (biomedcentral.com)
  • Decreased susceptibility to fluoroquinolones could be partly explained by decreased expression of the outer membrane porin genes ompA and ompF with a concomitant increase in the expression of the ciprofloxacin resistance efflux pump gene acrB in Δcrp cells. (readbyqxmd.com)
  • 4 mg l -1 ), 60.5 % (115/190) showed mutation in both porin genes. (cdc.gov)
  • Occurrence of porin genes in M. fortuitum . (biomedcentral.com)
  • 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)
Abstract1
Pseudomonas5
Permeability13
OmpC and OmpF3
  • The two classical porins OmpC and OmpF consist of three 16-stranded β barrels, each of which forms a channel that is restricted in the middle due to the inward folding of a loop ( 8 ). (asm.org)
  • Much of our knowledge of the regulatory activities of EnvZ/OmpR has been derived from studies on the regulation of the outer membrane (OM) OmpC and OmpF porins in response to changes in the osmolarity of the environment ( Russo and Silhavy, 1991 ). (frontiersin.org)
  • OmpC and OmpF are general porins that facilitate the passive and non-specific diffusion of low molecular weight hydrophilic substances across the OM ( Nikaido, 2003 ). (frontiersin.org)
Trimers4
Small Molecules2
Human VDAC12
Molecular9
Molecules8
  • A generally accepted view of the porin assembly pathway is that after the removal of the signal peptide from precursors, mature porin molecules transiently exist in the periplasm as soluble or peripherally membrane-associated, thermolabile intermediates. (asm.org)
  • OmpF porin is a non-specific transport channel that allows for the passive diffusion of small, polar molecules (600-700 Da in size) through the cell's outer membrane. (davidson.edu)
  • Neisserial porins induce B lymphocytes to express costimulatory B7-2 molecules and to proliferate. (rupress.org)
  • However, the OmpF porin channel allowed influx of more solute molecules per unit time than did the equivalent weight of the OmpC porin when the flux was driven by a concentration gradient of the same size. (asm.org)
  • Paper I: In Silico Structure and Sequence Analysis of Bacterial Porins and Specific Diffusion Channels for Hydrophilic Molecules: Conservation, Multimericity and Multifunctionality. (uio.no)
  • The two major porins of Escherichia coli , namely OmpF and OmpC, form non-specific transport channels and allow for the passive diffusion of small, polar molecules (such as water, ions, amino acids, and other nutrients, as well as waste products) across the cell membrane. (biomedcentral.com)
  • The over-expression of OmpX can balance the decreased expression of non-specific porins, OmpF and OmpC, for the exclusion of small harmful molecules. (biomedcentral.com)
  • Moreover, S. Typhi porins induce the expression of costimulatory molecules on antigen-presenting cells through toll-like receptor canonical signaling pathways. (readbyqxmd.com)
Mutants5
  • Among a panel of independent V. cholerae rpoE mutants, more than 75% contain suppressor mutations that reduce production of OmpU, V. cholerae's principal outer membrane porin. (harvard.edu)
  • ATR-FTIR spectroscopy proved to reliably distinguish between several E. coli porin mutants with an accuracy not replicated by FTIR in transmission mode (using previously optimized procedures). (spectroscopynow.com)
  • In addition, mutants of OmpF and NanC have been generated to modify ion conductance properties of these porins. (jacobs-university.de)
  • Although we confirm the findings of Fiedler and Rotering, we find that the regulation of OmpF and OmpC expression in mdoA mutants is normal in cells grown on other low- osmolarity media, eliminating the possibility that MDO itself might control porin expression. (princeton.edu)
  • Characterization of -Lactamase and Porin Mutants of Enterobacteriaceae Selected with Ceftaroline + Avibactam (NXL104). (uea.ac.uk)
Bacterial outer membrane porins1
Trimeric2
Bacteria5
Characterization3
OmpK3511
  • The outer membrane porins such as OmpK35 and OmpK36 were analysed by SDS-PAGE, PCR, and sequencing methods. (hindawi.com)
  • Outer membrane porin, OmpK35, was detected in 30 (62.5%) of 48 ESBL-producing isolates while OmpK36 was found in 35 (72.91%) of 48 ESBL-producing isolates. (hindawi.com)
  • Carbapenem resistance in K. pneumoniae is based on various mechanisms that may involve carbapenemase production, upregulation of efflux pumps, or loss of porins, including OmpK35, OmpK36, and OmpK37. (hindawi.com)
  • OmpK35 from Klebsiella pneumoniae is the homologue of Escherichia coli OmpF porin. (asm.org)
  • Klebsiella pneumoniae produces two major porins (OmpK35 and OmpK36) and the quiescent porin OmpK37. (asm.org)
  • Most clinical isolates of K. pneumoniae lacking extended-spectrum β-lactamase (ESBL) express both OmpK35 and OmpK36 porins, while most ESBL-expressing K. pneumoniae clinical isolates produce only OmpK36 ( 9 ). (asm.org)
  • Preliminary results ( 6 ) indicate that OmpK35 allows efficient penetration of cefoxitin, cefotaxime, and carbapenems, but there has been some controversy on the role of this porin in cephalosporin penetration in K. pneumoniae ( 18 ). (asm.org)
  • Recombinants were screened for ompK35 by PCR using primers U681 (5′-CGG TTA CGG CCA GTG GGA ATA-3′) and L1316 (5′-GAC GCA GAC CGA AAT CGA ACT-3′), specific for enterobacterial porins and located 215 and 850 bp downstream of the ompK36 start codon, respectively ( 6 ). (asm.org)
  • The expression of OmpK35 was downregulated in a high-osmolarity culture medium, as occurs with the OmpF-like porins ( 9 ), and OmpK35 reacted with anti-OmpK35 in immunoblot experiments (data not shown). (asm.org)
  • The OmpK35 protein expressed by the E. coli clone was extracted by porin extraction methods based on the trypsin resistance of porins and their strong noncovalent association with the peptidoglycan, and it also retained its heat modifiability. (asm.org)
  • To understand the diversity of porin disruption in Klebsiella pneumoniae, the major outer membrane protein (OMP) porins, OmpK35 and OmpK36, were examined in a set of isolates that did not harbour traditional carbapenem-hydrolysing enzymes, but nevertheless tested non-susceptible to ertapenem. (cdc.gov)
Functions as a porin1
Insertion into the outer membrane1
  • The statistical data were combined with experimental knowledge about porin insertion to prepare the model of porin insertion into the outer membrane. (srce.hr)
Salmonella4
Putative1
Anion-selective porin1
  • Omp32, the strongly anion-selective porin from Comamonas acidovorans, has been crystallized. (uni-konstanz.de)
Carbon nanotube porins1
  • We have recently reported simple and versatile artificial membrane pore analogues-carbon nanotube porins (CNTPs)-short segments of single-wall carbon nanotubes that can self-insert into the lipid membrane and form a transmembrane pore [ 10 ]. (royalsocietypublishing.org)
Gene5
  • ipeX was localized within an untranslated region of 247 base pairs between the stop codon of nmpC -a remnant porin gene from the cryptic phage qsr ′ (DLP12) genome-and its predicted Rho-independent transcriptional terminator. (asm.org)
  • The OmpF porin gene contains 1807 nucleotide bases. (davidson.edu)
  • Isolates without obvious genetic lesions in either major porin gene were further examined by outer membrane protein SDS-PAGE. (cdc.gov)
  • The promoter region of the oprB gene was cloned into a lacZ transcriptional fusion vector, and the construct was mobilized into P. aeruginosa OprB-deficient strain, WW100, to evaluate additional environmental factors that influence OprB porin gene expression. (umanitoba.ca)
  • In addition, our data showed that OmpR is responsible for up regulation of the kdgM1 gene encoding the second specific oligogalacturonide porin KdgM1. (frontiersin.org)
Voltage-Depende2
Conductance5
OmpF Porin11
Stability of porin2
  • Earlier we have reported the extreme thermal stability of porin from Paracoccus denitrificans reconstituted into liposomes. (uni-konstanz.de)
  • Our results show that a mixed lipid system (non-uniform bilayer) optimizes the thermal stability of porin as compared to the porin in pure lipids (uniform bilayer) or detergent micelles. (uni-konstanz.de)
Transmembrane3
Regulation7
OmpU4
  • Our results indicate that ToxR-dependent modulation of the outer membrane porins OmpU and OmpT is critical for V. cholerae bile resistance, virulence factor expression, and intestinal colonization. (pnas.org)
  • ToxR, however, independently of the transcriptional activators TcpP and ToxT, modulates expression of two outer membrane porins, OmpU and OmpT ( 8 - 10 ). (pnas.org)
  • Thus, ToxR-dependent modulation of porins apparently preceded, and possibly contributed to, the evolution of V. cholerae as a human pathogen, but little is known about the potential role of OmpU and OmpT in V. cholerae pathogenesis. (pnas.org)
  • V. cholerae strains were genetically manipulated to force a "porin swap," i.e., a toxR + strain that expresses OmpT in place of OmpU and a toxR − strain that expresses OmpU in place of OmpT. (pnas.org)
Translocation1
  • A matrix-destined precursor and the porin precursor compete for the same translocation sites in both normal mitochondria and mitochondria whose surface receptors have been removed, suggesting that both precursors utilize the general import pore. (nih.gov)
Coli porin2
  • The Escherichia coli porin OmpG, which acts as an efficient unspecific channel for mono-, di- and trisaccharides, has been purified and crystallized in two dimensions. (nih.gov)
  • Membrane-derived oligosaccharides (MDO's) promote closing of an E. coli porin channel. (nih.gov)
Mutant6
  • Finally, the biological relevance of two porins, P13 and P66, was demonstrated in a double mutant displaying a stress response as revealed by increased sensitivity to high osmolarity and elevated expression of the B. burgdorferi heat-shock protein HtrA homolog. (diva-portal.org)
  • This mutant porin and its derivative, OmpC R74C,G154C , or OmpC 2Cys ( 17 ), are the subjects of this work and are further discussed below. (asm.org)
  • Considering the colicin resistance of the mutant, it is inferred that in vivo, colicin N traverses the outer membrane through the porin channel or that the dynamics of the exposed loops are affected in the mutant such that these may impede the binding of the toxin. (pnas.org)
  • Hoenger A, Ghosh R, Schoenenberger CA, Aebi U, Engel A. Direct in situ structural analysis of recombinant outer membrane porins expressed in an OmpA-deficient mutant Escherichia coli strain. (ucdenver.edu)
  • When the mitochondria were preincubated at 37°C, the assembly of porin in the tom40 mutant mitochondria was similarly reduced compared with wild-type mitochondria. (nih.gov)
  • The assembly of porin was inhibited in the mutant mitochondria (Fig. 8 A, lanes 4-9). (nih.gov)
Liposomes2
  • This interaction was independent of the immobilized binding partner (porin reconstituted in liposomes or MtCK) or the analyzed isoform (chicken sarcomeric MtCK or human ubiquitous MtCK, human recombinant porin, or purified bovine porin). (inserm.fr)
  • Top: Schematic showing CNT porin preparation and incorporation into liposomes. (lbl.gov)
Expression5
  • Here, the lysogenization event leads to the expression of a phage-encoded porin, Lc, and the inhibition of the host's OmpC porin. (asm.org)
  • The work conducted in this study will shed light on how phage porin expression regulates that of ompC . (asm.org)
  • Neisserial porins increased the surface expression of the costimulatory ligand B7-2 (CD86) but did not affect the expression of B7-1 (CD80). (rupress.org)
  • Herein, both transmission Fourier-transform infrared (FTIR) and attenuated total reflectance (ATR)-FTIR spectroscopy are used to analyse E. coli strains that differ solely in their porin expression profile. (spectroscopynow.com)
  • Growth temperature, pH of the growth medium, salicylate concentration, and carbohydrate source were found to differentially influence porin expression. (umanitoba.ca)
Mycobacterium2
Precursor2
  • Moreover, the porin precursor can be cross-linked to Tom20, Tom22, and Tom40 on its import pathway. (nih.gov)
  • A) Radiolabeled porin precursor (10 μl reticulocyte lysate per lane) was incubated with isolated yeast mitochondria as indicated (50 μg protein per lane) at 25°C. The mitochondria were reisolated, lysed in digitonin-containing buffer, and subjected to BN-PAGE and digital autoradiography. (nih.gov)
Solutes1
Major outer membrane protein1
Resistance1
  • Understand how antibiotics diffuse through these porins can help researcher to develop new antibiotics with an improved penetration especially when resistance becomes a serious problem for infectious disease. (unica.it)
Mitochondrial outer1
Immunogen1
  • The results of this study favour the use of porins as a common immunogen to control salmonellosis since porin patterns were found to be quite similar among the serotypes of salmonellae, unlike other enterobacterial species. (ac.ir)
Typhimurium4
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