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Cited by 165Bacterial Genetics and BiotechnologyDrug Transport and Resistance MechanismsAntibiotic Resistance in Bacteria

Formation of a Gated Channel by a Ligand-Specific Transport Protein in the Bacterial Outer Membrane

Rutz, Jeanette M., Liu, Jun, Lyons, Jeri Ann, Goranson, Joanne, Armstrong, Sandra K., McIntosh, Mark A., Feix, Jimmy B., Klebba, Phillip E.·1992·Science
DOI 10.1126/science.1411544
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Abstract

The ferric enterobactin receptor (FepA) is a high-affinity ligand-specific transport protein in the outer membrane of Gram-negative bacteria. Deletion of the cell-surface ligand-binding peptides of FepA generated mutant proteins that were incapable of high-affinity uptake but that instead formed nonspecific, passive channels in the outer membrane. Unlike native FepA, these pores acted independently of the accessory protein TonB, which suggests that FepA is a gated porin and that TonB acts as its gatekeeper by facilitating the entry of ligands into the FepA channel. The sequence homology among TonB-dependent proteins suggests that all ligand-specific outer membrane receptors may function by this gated-porin mechanism.

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  • OM ferric siderophore receptors are TonB-dependent members of the porin superfamily, called TonB-dependent transporters or ligand-gated porins.

    “OM ferric siderophore receptors are TonB-dependent members of the porin superfamily.Hence, they are called TonB-dependent transporters (14) or ligand-gated porins [LGP (15)], in the latter case because ligand binding activates their TonB-depend ent transport process.”

    From Siderophore-mediated iron acquisition by <i>Klebsiella pneumoniae</i> (2024) · cites this paper as [15]

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Authors
Rutz, J. M., Liu, J., Lyons, J. A., Goranson, J., Armstrong, S. K., McIntosh, M. A., Feix, J. B., & Klebba, P. E.
Affiliations
  • Medical College of Wisconsin (US)
  • Department of Microbiology, Medical College of Wisconsin, Milwaukee, WI 53226.
  • East Carolina University (US)
  • University of Missouri (US)
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1992-10-16
Volume
258
Issue
5081
Pages
471-475
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.1411544
OpenAlex
W1969795354
Cited by
165
References
43
Citations by year
2025: 1 · 2024: 3 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2017: 2 · 2016: 1 · 2015: 1 · 2014: 4 · 2013: 1 · 2012: 1
FWCI
9.61
Type
journal article
Language
en
Open access
closed
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (7r01ai022608-03, 5r01gm040565-04)
  • National Institute of General Medical Sciences (GM22923, GM40565)
  • National Institute of Allergy and Infectious Diseases (AI22608)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Antibiotic Resistance in Bacteria
Keywords
FepA, TonB, outer membrane receptor, Gram-negative bacterial outer membrane, iron absorption
MeSH terms
Amino Acid Sequence, Antigens, Bacterial, Antigens, Surface, Bacterial Outer Membrane Proteins, Carrier Proteins, DNA Mutational Analysis, Enterobactin, Escherichia coli, Microbial Sensitivity Tests, Molecular Sequence Data, Receptors, Cell Surface, Structure-Activity Relationship, Ion Channel Gating

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