The atomic structure of the phage Tuc2009 baseplate tripod suggests that host recognition involves two different carbohydrate binding modules

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dc.contributor.author Legrand, Pierre
dc.contributor.author Collins, Barry
dc.contributor.author Blangy, Stéphanie
dc.contributor.author Murphy, James
dc.contributor.author Spinelli, Silvia
dc.contributor.author Gutierrez, Carlos
dc.contributor.author Richet, Nicolas
dc.contributor.author Kellenberger, Christine
dc.contributor.author Desmyter, Aline
dc.contributor.author Mahony, Jennifer
dc.contributor.author van Sinderen, Douwe
dc.contributor.author Cambillau, Christian
dc.date.accessioned 2017-02-22T11:48:15Z
dc.date.available 2017-02-22T11:48:15Z
dc.date.issued 2016-01-26
dc.identifier.citation Legrand, P., Collins, B., Blangy, S., Murphy, J., Spinelli, S., Gutierrez, C., Richet, N., Kellenberger, C., Desmyter, A., Mahony, J., van Sinderen, D. and Cambillau, C. (2016) 'The Atomic Structure of the Phage Tuc2009 Baseplate Tripod Suggests that Host Recognition Involves Two Different Carbohydrate Binding Modules', mBio, 7(1). doi:10.1128/mBio.01781-15 en
dc.identifier.volume 7 en
dc.identifier.issued 1 en
dc.identifier.startpage e01781-15: 1 en
dc.identifier.endpage e01781-15: 11 en
dc.identifier.issn 2150-7511
dc.identifier.uri http://hdl.handle.net/10468/3664
dc.identifier.doi 10.1128/mBio.01781-15
dc.description.abstract The Gram-positive bacterium Lactococcus lactis, used for the production of cheeses and other fermented dairy products, falls victim frequently to fortuitous infection by tailed phages. The accompanying risk of dairy fermentation failures in industrial facilities has prompted in-depth investigations of these phages. Lactococcal phage Tuc2009 possesses extensive genomic homology to phage TP901-1. However, striking differences in the baseplate-encoding genes stimulated our interest in solving the structure of this host’s adhesion device. We report here the X-ray structures of phage Tuc2009 receptor binding protein (RBP) and of a “tripod” assembly of three baseplate components, BppU, BppA, and BppL (the RBP). These structures made it possible to generate a realistic atomic model of the complete Tuc2009 baseplate that consists of an 84-protein complex: 18 BppU, 12 BppA, and 54 BppL proteins. The RBP head domain possesses a different fold than those of phages p2, TP901-1, and 1358, while the so-called “stem” and “neck” domains share structural features with their equivalents in phage TP901-1. The BppA module interacts strongly with the BppU N-terminal domain. Unlike other characterized lactococcal phages, Tuc2009 baseplate harbors two different carbohydrate recognition sites: one in the bona fide RBP head domain and the other in BppA. These findings represent a major step forward in deciphering the molecular mechanism by which Tuc2009 recognizes its saccharidic receptor(s) on its host. en
dc.description.sponsorship Agence Nationale de la Recherche (grants ANR-11-BSV8-004-01 “Lactophages” and French Infrastructure for Integrated Structural Biology [FRISBI]); Science Foundation Ireland (SFI Principal Investigator award (reference no. 13/IA/1953), SFI Technology Innovation Development Award (TIDA) (reference no. 14/TIDA/2287)) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher American Society for Microbiology en
dc.rights © 2016 Legrand et al. This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license, which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited. en
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/3.0/ en
dc.subject Lactococcus lactis en
dc.subject Lactococcal phage Tuc2009 en
dc.subject Dairy fermentation en
dc.title The atomic structure of the phage Tuc2009 baseplate tripod suggests that host recognition involves two different carbohydrate binding modules en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Douwe Van Sinderen, Microbiology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: d.vansinderen@ucc.ie en
dc.internal.availability Full text available en
dc.date.updated 2017-02-22T11:38:16Z
dc.description.version Published Version en
dc.internal.rssid 384563545
dc.contributor.funder Agence Nationale de la Recherche en
dc.contributor.funder Science Foundation Ireland en
dc.description.status Peer reviewed en
dc.identifier.journaltitle Mbio en
dc.internal.copyrightchecked No !!CORA!! en
dc.internal.licenseacceptance Yes en
dc.internal.IRISemailaddress d.vansinderen@ucc.ie en


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© 2016 Legrand et al. This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license, which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited. Except where otherwise noted, this item's license is described as © 2016 Legrand et al. This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license, which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited.
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