Microbiol Mol Biol Rev 67(4): 593-656

Molecular Basis of Bacterial Outer Membrane Permeability Revisited

Department of Molecular and Cell Biology, University of California, Berkeley, California

^{Mailing address: Department of Molecular and Cell Biology, 426 Barker Hall, University of California, Berkeley, CA 94720-3202. Phone: (510) 642-2027. Fax: (510) 643-6334. E-mail:}ude.yelekreb.4knilcu@ihsorihn.

Abstract

Gram-negative bacteria characteristically are surrounded by an additional membrane layer, the outer membrane. Although outer membrane components often play important roles in the interaction of symbiotic or pathogenic bacteria with their host organisms, the major role of this membrane must usually be to serve as a permeability barrier to prevent the entry of noxious compounds and at the same time to allow the influx of nutrient molecules. This review summarizes the development in the field since our previous review (H. Nikaido and M. Vaara, Microbiol. Rev. 49:1-32, 1985) was published. With the discovery of protein channels, structural knowledge enables us to understand in molecular detail how porins, specific channels, TonB-linked receptors, and other proteins function. We are now beginning to see how the export of large proteins occurs across the outer membrane. With our knowledge of the lipopolysaccharide-phospholipid asymmetric bilayer of the outer membrane, we are finally beginning to understand how this bilayer can retard the entry of lipophilic compounds, owing to our increasing knowledge about the chemistry of lipopolysaccharide from diverse organisms and the way in which lipopolysaccharide structure is modified by environmental conditions.

Abstract

Acknowledgments

I am indebted to many colleagues, too numerous to mention, who provided invaluable help by answering my questions or by reading and correcting parts of the manuscript. I thank my coworkers, especially for their patience during the long period needed to write this review. I also thank the anonymous reviewers of this article for many constructive and useful suggestions. I benefited greatly from the information in Milton Saier's website (http://www.biology.ucsd.edu/∼msaier/transport/), which presents an up-to-date classification of transport proteins.

The studies in my laboratory have been supported by U.S. Public Health Service grant AI-09644.

Acknowledgments

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