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Molecular Basis of Bacterial Outer Membrane Permeability Revisited
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SUMMARY: 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.
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“Among the best-characterized porins, the three major proteins produced by E. coli (known as OmpF, OmpC and PhoE) and the P. aeruginosa OprD (also known as protein D2) are classical examples of porin-mediated antibiotic resistance.”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [39]
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“Importantly, changes in permeability through any of these mechanisms frequently result in low-level resistance and are often associated with other mechanisms of resistance, such as increased expression of efflux pumps (see below) (39).”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [39]
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“Alterations of porins could be achieved by 3 general processes, i) a shift in the type of porins expressed, ii) a change in the level of porin expression, and iii) impairment of the porin function.”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [39]
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Metadata
- Authors
- Nikaido, H.
- Affiliations
- University of California, Berkeley (US)
- Corresponding author
- Nikaido, Hiroshi
- Venue
- Microbiology and Molecular Biology Reviews
- Publisher
- American Society for Microbiology
- Published
- 2003-12
- Volume
- 67
- Issue
- 4
- Pages
- 593-656
- ISSN
- 1092-2172 (ISSN-L)
- 1098-5557
- PMC
- PMC309051
- OpenAlex
- W2120061656
- Cited by
- 4,316
- References
- 799
- Citations by year
- 2026: 294 · 2025: 242 · 2024: 225 · 2023: 223 · 2022: 267 · 2021: 269 · 2020: 274 · 2019: 238 · 2018: 228 · 2017: 243 · 2016: 227 · 2015: 187 · 2014: 176 · 2013: 162 · 2012: 177
- FWCI
- 8.17
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Microbiology and Molecular Biology Reviews (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service
- National Institute of Allergy and Infectious Diseases (R37AI009644, R01AI009644, AI 09644)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Immunology and Microbiology › Microbiology › Escherichia coli research studies
- Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
- Keywords
- bacterial outer membrane, outer membrane permeability, porin, TonB-dependent receptors, lipopolysaccharide, asymmetric bilayers, Gram-negative bacteria, nutrient uptake
- MeSH terms
- Amino Acid Sequence, Cell Membrane, Cell Membrane Permeability, Gram-Negative Bacteria, Ion Channels, Lipid Bilayers, Molecular Sequence Data, Sequence Alignment, Porins
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