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Cited by 32Advanced Electron Microscopy Techniques and ApplicationsBacteriophages and microbial interactionsBacterial Genetics and Biotechnology

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CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage

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Conners, Rebecca, McLaren, Mathew, Łapińska, Urszula, Sanders, Kelly, Stone, M. Rhia L., Blaskovich, Mark A. T., Pagliara, Stefano, Daum, Bertram, Rakonjac, Jasna, Gold, Vicki A. M.·2021·Nature Communications
DOI 10.1038/s41467-021-26610-3PMC PMC8563730

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Abstract

The Ff family of filamentous bacteriophages infect gram-negative bacteria, but do not cause lysis of their host cell. Instead, new virions are extruded via the phage-encoded pIV protein, which has homology with bacterial secretins. Here, we determine the structure of pIV from the f1 filamentous bacteriophage at 2.7 Å resolution by cryo-electron microscopy, the first near-atomic structure of a phage secretin. Fifteen f1 pIV subunits assemble to form a gated channel in the bacterial outer membrane, with associated soluble domains projecting into the periplasm. We model channel opening and propose a mechanism for phage egress. By single-cell microfluidics experiments, we demonstrate the potential for secretins such as pIV to be used as adjuvants to increase the uptake and efficacy of antibiotics in bacteria. Finally, we compare the f1 pIV structure to its homologues to reveal similarities and differences between phage and bacterial secretins.

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Metadata

Authors
Conners, R., McLaren, M., Łapińska, U., Sanders, K., Stone, M. R. L., Blaskovich, M. A. T., Pagliara, S., Daum, B., Rakonjac, J., & Gold, V. A. M.
Affiliations
  • University of Exeter (GB)
  • The University of Queensland (AU)
  • Massey University (NZ)
Corresponding author
Gold, Vicki A. M.
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2021-11-02
Volume
12
Issue
1
Pages
6316-6316
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-021-26610-3
PMC
PMC8563730
OpenAlex
W3209565305
Cited by
32
References
2
Citations by year
2025: 9 · 2024: 3 · 2023: 10 · 2022: 6 · 2021: 4
FWCI
2.41
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Massey Research Online (Massey University) (acceptedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Figshare (submittedVersion, cc-by)
  • Open Research Exeter (University of Exeter) (submittedVersion, cc-by)
Funders
  • Wellcome Trust (210363/Z/18/Z)
  • RCUK | Biotechnology and Biological Sciences Research Council (BB/R008639/1, BB/V008021/1)
  • Gordon and Betty Moore Foundation (GBMF5514)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
  • Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
outer membrane, channel gating, phage assembly, periplasmic domain, antibiotic adjuvants, phage-bacteria interactions
MeSH terms
Protein Structural Elements, Amino Acid Sequence, Biological Transport, Secretin, Sequence Alignment, Viral Nonstructural Proteins, Inovirus, Cryoelectron Microscopy

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