CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage
dc.contributor.author | Conners, R | |
dc.contributor.author | McLaren, M | |
dc.contributor.author | Łapińska, U | |
dc.contributor.author | Sanders, K | |
dc.contributor.author | Stone, MRL | |
dc.contributor.author | Blaskovich, MAT | |
dc.contributor.author | Pagliara, S | |
dc.contributor.author | Daum, B | |
dc.contributor.author | Rakonjac, J | |
dc.contributor.author | Gold, VAM | |
dc.date.accessioned | 2021-11-10T15:52:01Z | |
dc.date.issued | 2021-11-02 | |
dc.date.updated | 2021-11-09T15:14:40Z | |
dc.description.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. | en_GB |
dc.description.sponsorship | Wellcome Trust | en_GB |
dc.description.sponsorship | Biotechnology and Biological Sciences Research Council (BBSRC) | en_GB |
dc.description.sponsorship | Medical Research Council (MRC) | en_GB |
dc.description.sponsorship | Gordon and Betty Moore Foundation | en_GB |
dc.description.sponsorship | European Research Council (ERC) | en_GB |
dc.description.sponsorship | Biotechnology and Biological Sciences Research Council | en_GB |
dc.description.sponsorship | Australian Postgraduate Award (APA) | en_GB |
dc.description.sponsorship | IMB Research Advancement Award | en_GB |
dc.identifier.citation | Vol. 12, article 6316 | en_GB |
dc.identifier.doi | https://doi.org/10.1038/s41467-021-26610-3 | |
dc.identifier.grantnumber | 210363/Z/18/Z | en_GB |
dc.identifier.grantnumber | 210363/Z/18/Z | en_GB |
dc.identifier.grantnumber | BB/V008021/1 | en_GB |
dc.identifier.grantnumber | MCPC17189 | en_GB |
dc.identifier.grantnumber | GBMF5514 | en_GB |
dc.identifier.grantnumber | 803894 | en_GB |
dc.identifier.grantnumber | BB/R008639/1 | en_GB |
dc.identifier.uri | http://hdl.handle.net/10871/127767 | |
dc.identifier | ORCID: 0000-0002-8653-1771 (Conners, Rebecca) | |
dc.identifier | ORCID: 0000-0001-9387-4433 (Sanders, Kelly) | |
dc.identifier | ORCID: 0000-0002-3767-264X (Daum, Bertram) | |
dc.identifier | ORCID: 0000-0002-6908-0745 (Gold, Vicki) | |
dc.language.iso | en | en_GB |
dc.publisher | Nature Research | en_GB |
dc.rights | © The Author(s) 2021. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/. | en_GB |
dc.subject | Cryoelectron microscopy | en_GB |
dc.subject | Membrane proteins | en_GB |
dc.subject | Permeation and transport | en_GB |
dc.subject | Phage biology | en_GB |
dc.title | CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2021-11-10T15:52:01Z | |
dc.description | This is the final version. Available on open access from Nature Research via the DOI in this record. | en_GB |
dc.identifier.eissn | 2041-1723 | |
dc.identifier.journal | Nature Communications | en_GB |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | en_GB |
dcterms.dateAccepted | 2021-10-13 | |
rioxxterms.version | VoR | en_GB |
rioxxterms.licenseref.startdate | 2021-07-21 | |
rioxxterms.type | Journal Article/Review | en_GB |
refterms.dateFCD | 2021-11-10T15:42:14Z | |
refterms.versionFCD | VoR | |
refterms.dateFOA | 2021-11-10T15:52:08Z | |
refterms.panel | A | en_GB |
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