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.authorLegrand, Pierre
dc.contributor.authorCollins, Barry
dc.contributor.authorBlangy, Stéphanie
dc.contributor.authorMurphy, James
dc.contributor.authorSpinelli, Silvia
dc.contributor.authorGutierrez, Carlos
dc.contributor.authorRichet, Nicolas
dc.contributor.authorKellenberger, Christine
dc.contributor.authorDesmyter, Aline
dc.contributor.authorMahony, Jennifer
dc.contributor.authorvan Sinderen, Douwe
dc.contributor.authorCambillau, Christian
dc.contributor.funderAgence Nationale de la Rechercheen
dc.contributor.funderScience Foundation Irelanden
dc.date.accessioned2017-02-22T11:48:15Z
dc.date.available2017-02-22T11:48:15Z
dc.date.issued2016-01-26
dc.date.updated2017-02-22T11:38:16Z
dc.description.abstractThe 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.sponsorshipAgence 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.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationLegrand, 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.01781-15en
dc.identifier.doi10.1128/mBio.01781-15
dc.identifier.endpagee01781-15: 11en
dc.identifier.issn2150-7511
dc.identifier.issued1en
dc.identifier.journaltitleMbioen
dc.identifier.startpagee01781-15: 1en
dc.identifier.urihttps://hdl.handle.net/10468/3664
dc.identifier.volume7en
dc.language.isoenen
dc.publisherAmerican Society for Microbiologyen
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.urihttps://creativecommons.org/licenses/by-nc-sa/3.0/en
dc.subjectLactococcus lactisen
dc.subjectLactococcal phage Tuc2009en
dc.subjectDairy fermentationen
dc.titleThe atomic structure of the phage Tuc2009 baseplate tripod suggests that host recognition involves two different carbohydrate binding modulesen
dc.typeArticle (peer-reviewed)en
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