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• W2011071036 abstract "Editorials1 October 1984The Possible Role of Porins in Bacterial Antibiotic ResistanceLAURENT GUTMANN, M.D., RUSSELL WILLIAMSON, PH.D., EKKEHARD COLLATZ, M.D.LAURENT GUTMANN, M.D.Search for more papers by this author, RUSSELL WILLIAMSON, PH.D.Search for more papers by this author, EKKEHARD COLLATZ, M.D.Search for more papers by this authorAuthor, Article, and Disclosure Informationhttps://doi.org/10.7326/0003-4819-101-4-554 SectionsAboutPDF ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinkedInRedditEmail ExcerptAntibiotic agents are thought to diffuse freely through the cell wall of gram-positive bacteria. However, in gram-negative bacteria the diffusion of a given antibiotic agent depends on the permeability of the outer membrane. This permeability is determined by the particular structure of the membrane, which is composed of proteins and an asymmetric lipid bilayer. The outer layer consists mainly of lipopolysaccharides and the inner layer of phospholipids (1). Some outer membrane proteins are attached to the underlying peptidoglycan. This membrane structure allows for different pathways of diffusion into the periplasmic space. Hydrophobic molecules are normally excluded, but may diffuse through...References1. NIKAIDONAKAE HT. The outer membrane of Gram-negative bacteria. Adv Microb Physiol. 1979;20:163-250. CrossrefMedlineGoogle Scholar2. NAKAE T. Identification of the outer membrane protein of E. coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem Biophys Res Commun. 1976;71:877-84. CrossrefMedlineGoogle Scholar3. NIKAIDOLUCKEYROSENBERG HME. Nonspecific and specific diffusion channels in the outer membrane of Escherichia coli. J Supramol Struct. 1980;13:305-13. CrossrefMedlineGoogle Scholar4. VAN ALPHENVAN BOXTELVAN SELMLUGTENBERG WRNB. 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Porin channels in Escherichia colli: studies with liposomes reconstituted from purified proteins. J Bacteriol. 1983;153:241-52. CrossrefMedlineGoogle Scholar10. NIKAIDOSONGSHALTIELNURMINEN HSLM. Outer membrane of Salmonella: XIV. Reduced transmembrane diffusion rates in porindeficient mutants. Biochem Biophys Res Commun. 1977;76:324-30. CrossrefGoogle Scholar11. NICASHANCOCK TR. Pseudomonas aeruginosa outer membrane permeability: isolation of a porin protein F-deficient mutant. J Bacteriol. 1983;153:281-5. CrossrefMedlineGoogle Scholar12. LUNDRIGANEARHART MC. Gene envY of Escherichia coli K-12 affects thermoregulation of major porin expression. J Bacteriol. 1984;157:262-8. CrossrefMedlineGoogle Scholar13. HALLSILHAVY MT. Genetic analysis of the major outer membrane proteins of Escherichia coli. Annu Rev Genet. 1981;15:91-142. CrossrefMedlineGoogle Scholar14. ZIMMERMANNROSSELET WA. Function of the outer membrane of Escherichia coli as a permeability barrier to beta-lactam antibiotics. 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KOMATSUMURAKAMINISHIKAWA YKT. Penetration of moxalactam into its target proteins in Escherichia coli K-12: Comparison of a highly moxalactam-resistant mutant with its parent strain. Antimicrob Agents Chemother. 1981;20:613-9. CrossrefMedlineGoogle Scholar21. SAWAIHIRUMAKAWANAKANEKOTANIYASUINAMI TRNMFA. Outer membrane permeation of β-lactam antibiotics in Escherichia coli, Proteus mirabilis and Enterobacter cloacae. Antimicrob Agents Chemother. 1982;22:585-92. CrossrefMedlineGoogle Scholar22. CURTISORRROSSBOULTON NDGM. Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K-12 and their antibactericidal activity. Antimicrob Agents Chemother. 1979;16:533-9. CrossrefMedlineGoogle Scholar23. TRAUBSPOHRBAUER WMD. Plasmid-independent resistance of gray colony variants of a strain of Serratia marcescens resistant to amikacin, cefotaxime and lamoxactam. Chemotherapy. 1983;29:265-74. CrossrefMedlineGoogle Scholar24. GOLDSTEINGUTMANNWILLIAMSONCOLLATZACAR FLREJ. In vivo and in vitro emergence of simultaneous resistance to both β-lactam and aminoglycoside antibiotics in a strain of Serratia marcescens. Ann Microbiol (Paris). 1983;134:329-37. Google Scholar25. MIRELMANNUCHAMOWITZRUBINSTEIN DYE. Insensitivity of peptidoglycan biosynthetic reactions to β-lactam antibiotics in a clinical isolate of Pseudomonas aeruginosa. Antimicrob Agents Chemother. 1981;19:687-95. CrossrefMedlineGoogle Scholar26. RODRIGUEZ-TEBARROJODAMASOVASQUEZ AFDD. Carbenicillin resistance of Pseudomonas aeruginosa. Antimicrob Agents Chemother. 1982;22:255-61. CrossrefMedlineGoogle Scholar This content is PDF only. To continue reading please click on the PDF icon. Author, Article, and Disclosure InformationAffiliations: Laboratoire de Microbiologie Medicale Université Pierre et Marie Curie Paris France PreviousarticleNextarticle Advertisement FiguresReferencesRelatedDetails Metrics Cited byA Biosurfactant-Sophorolipid Acts in Synergy with Antibiotics to Enhance Their EfficiencyDescription of Complex Forms of a Porin in Bacteroides fragilis and Possible Implication of this Protein in Antibiotic ResistanceAntibiotic Resistance in the Intensive Care UnitIsolation and characterization of a porin-like protein of 45 kilodaltons from Bacteroides fragilisCharacterization ofCardiobacterium hominis: Antibiotic susceptibility, morphological variations, plasmid and membrane analysisPenicillinsRole of the Outer Membrane of Gram-Negative Bacteria in Antimicrobial ResistanceNorfloxacin: A New Targeted Fluoroquinolone Antimicrobial AgentJOHN S. WOLFSON, M.D., DAVID C. HOOPER, M.D.Bêta-lactamases : identification, rôle, aspects épidémiologiquesGenetic and biochemical characterization of norfloxacin resistance in Escherichia coli 1 October 1984Volume 101, Issue 4Page: 554-557KeywordsAntibiotic resistanceAntibioticsCell wallsGram negative bacteriaGram positive bacteriaLipidsMembrane proteinsOuter membrane proteinsPhospholipidsProtein structure Issue Published: 1 October 1984 PDF downloadLoading ..." @default.
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