Molecular Basis of Bacterial Outer Membrane Permeability Revisited

Nikaido, Hiroshi

doi:10.1128/mmbr.67.4.593-656.2003

Cited by 4,316Bacterial Genetics and BiotechnologyEscherichia coli research studiesBacterial Infections and Vaccines

Molecular Basis of Bacterial Outer Membrane Permeability Revisited

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Nikaido, Hiroshi·2003·Microbiology and Molecular Biology Reviews

DOI 10.1128/mmbr.67.4.593-656.2003PMC PMC309051

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Abstract

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 E. coli proteins OmpF, OmpC and PhoE and the P. aeruginosa OprD are classical examples of porin-mediated antibiotic resistance.
“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]
Changes in permeability through porin alteration mechanisms frequently result in low-level resistance and are often associated with other resistance mechanisms such as increased efflux pump expression.
“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]
Alterations of porins can be achieved by three general processes: a shift in the type of porins expressed, a change in the level of porin expression, and impairment of porin function.
“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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Protein D2 channel of the Pseudomonas aeruginosa outer membrane has a binding site for basic amino acids and peptides.
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Antimicrobial Resistance and the Alternative Resources with Special Emphasis on Plant-Based Antimicrobials—A Review
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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
DOI: 10.1128/mmbr.67.4.593-656.2003
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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 › Biochemistry, Genetics and Molecular Biology › Endocrinology › 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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