Omp35, a New Enterobacter aerogenes Porin Involved in Selective Susceptibility to Cephalosporins
Autor: | Nathalie Saint, Anne Davin-Regli, C. Bollet, Myrielle Dupont, Jean-Marie Pagès, Lilia Fetnaci, Charléric Bornet |
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Rok vydání: | 2004 |
Předmět: |
Models
Molecular Patch-Clamp Techniques Protein Conformation Immunoblotting Lipid Bilayers Molecular Sequence Data Porins Microbial Sensitivity Tests Enterobacter aerogenes Porina Ion Channels Microbiology Mechanisms of Resistance Pharmacology (medical) Amino Acid Sequence Antibacterial agent Pharmacology biology Strain (chemistry) biochemical phenomena metabolism and nutrition biology.organism_classification Enterobacteriaceae Cephalosporins Infectious Diseases Biochemistry Liposomes Porin bacteria Electrophoresis Polyacrylamide Gel Bacterial outer membrane Bacteria Bacterial Outer Membrane Proteins |
Zdroj: | Antimicrobial Agents and Chemotherapy. 48:2153-2158 |
ISSN: | 1098-6596 0066-4804 |
DOI: | 10.1128/aac.48.6.2153-2158.2004 |
Popis: | In Enterobacter aerogenes , β-lactam resistance often involves a decrease in outer membrane permeability induced by modifications of porin synthesis. In ATCC 15038 strain, we observed a different pattern of porin production associated with a variable antibiotic susceptibility. We purified Omp35, which is expressed under conditions of low osmolality and analyzed its pore-forming properties in artificial membranes. This porin was found to be an OmpF-like protein with high conductance values. It showed a noticeably higher conductance compared to Omp36 and a specific location of WNYT residues in the L3 loop. The importance of the constriction region in the porin function suggests that this organization is involved in the level of susceptibility to negative large cephalosporins such as ceftriaxone by bacteria producing the Omp35 porin subfamily. |
Databáze: | OpenAIRE |
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