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PMID: 2443611 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

A major outer-membrane protein functions as a porin in Haemophilus influenzae.

Journal of general microbiology ·Vol. 133 ·No. 5 ·1987-05-00 ·Pages 1273-7

Burns JL, Smith AL

Abstract

Porins are pore-forming outer-membrane proteins which serve as a non-specific pathway for the entry of hydrophilic molecules into Gram-negative bacteria. We studied four strains of Haemophilus influenzae that had decreased permeability to chloramphenicol associated with diminished quantities of a 40 kDa major outer-membrane protein. Isogenic pairs of organisms containing and lacking this protein were compared. The latter strains grew more slowly and were less permeable to sucrose and raffinose. They were also more resistant to multiple hydrophilic antibiotics than an isogenic strain containing the 40 kDa protein and were less permeable to penicillin G and chloramphenicol. We conclude that the 40 kDa outer-membrane protein functions as a porin in H. influenzae.

MeSH Terms
Anti-Bacterial Agents/pharmacology Bacterial Outer Membrane Proteins/metabolism Cell Membrane Permeability/drug effects Drug Resistance, Microbial Haemophilus influenzae/drug effects,growth & development Ion Channels/drug effects Oligosaccharides/metabolism Penicillin G/pharmacology Penicillin Resistance Porins
Chemicals
Anti-Bacterial Agents Bacterial Outer Membrane Proteins Ion Channels Oligosaccharides Porins Penicillin G
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Burns J L
Department of Pediatrics, University of Washington, Seattle.
Smith A L
Article Info
Journal
Journal of general microbiology
Abbr.
J Gen Microbiol
ISSN
0022-1287
Published
1987-05-00
Pages
1273-7
Language
English
Region
England
NLM ID
0375371
Subset
IM
Grants
NIAID NIH HHS · AI 06726 · United States
NIAID NIH HHS · AI 20625 · United States
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