نتایج جستجو برای: porins
تعداد نتایج: 718 فیلتر نتایج به سال:
The DNA sequence of the ompC gene which encodes one of the outer membrane porins has been determined. The gene appears to encode a secretory precursor of OmpC protein consisting of a total of 367 amino acid residues with a signal peptide of 21 amino acid residues at its NH2-terminal end. The 5' end noncoding region including the promoter of the ompC gene is extremely [A-T]-rich, and the codon u...
We examined the ability of porins from Salmonella enterica serovar typhi to induce a long-term antibody response in BALB/c mice. These porins triggered a strong lifelong production of immunoglobulin G (IgG) antibody in the absence of exogenous adjuvant. Analysis of the IgG subclasses produced during this antibody response revealed the presence of the subclasses IgG2b, IgG1, IgG2a and weak IgG3....
TLR directly induce innate immune responses by sensing a variety of microbial components and are critical for the fine-tuning of subsequent adaptive immune responses. However, their impact and mechanism of action on antibody responses against bacterial antigens are not yet fully understood. Salmonella enterica serovar Typhi (S. typhi) porins have been characterized as inducers of long-lasting s...
The outer membrane of mycobacteria presents an effective permeability barrier for many antibiotics. Transport pathways across this membrane are unknown for most drugs. Here, we examined which antibiotics utilize the porin pathway across the outer membrane of the model organism Mycobacterium smegmatis. Deletion of the porins MspA and MspC drastically increased the resistance of M. smegmatis ML10...
Lipid bilayer experiments indicated that the cell wall of Mycobacterium tuberculosis contains at least two different porins: (i) a cation-selective, heat-sensitive 0.7-nS channel which has a short-lived open state and is probably composed of 15-kDa subunits and (ii) a 3-nS, >60-kDa channel with a long-lived open state, resembling porins from fast-growing mycobacteria.
RjpA in Rhodococcus jostii is the ortholog of a channel-forming porin, MspA. Deletion of rjpA delayed growth of R. jostii on cholate but not on cholesterol. Eventual growth on cholate involved increased expression of other porins, namely, RjpB, RjpC, and RjpD. Porins appear essential for the uptake of bile acids by mycolic acid bacteria.
The accumulation of misfolded porins in the periplasm of bacteria triggers a proteolytic cascade, initiated by activation of DegS, a member of the family of HtrA proteases. Activation of DegS ultimately leads to the expression of genes encoding the periplasmic protein folding machinery. A new study now reveals that binding of exposed C-termini of unassembled porins to the PDZ domain of DegS ind...
Single channel current-voltage (IV) relations were measured from proteins that form channels across the outer membranes of Gram-negative bacteria – porins and their mutants in solutions of KCl. The wild-type porins and some of their specific mutants have known x-rays structures, which lays the foundation for this theoretical work. The ionic strength of KCl ranges from 100mM to 3M. Using the alr...
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