Structure and assembly of TP901-1 virion unveiled by mutagenesis

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dc.contributor.author Stockdale, Stephen R.
dc.contributor.author Collins, Barry
dc.contributor.author Spinelli, Silvia
dc.contributor.author Douillard, François P. en
dc.contributor.author Mahony, Jennifer
dc.contributor.author Cambillau, Christian
dc.contributor.author van Sinderen, Douwe
dc.date.accessioned 2016-02-17T10:07:57Z
dc.date.available 2016-02-17T10:07:57Z
dc.date.issued 2015
dc.identifier.citation Stockdale SR, Collins B, Spinelli S, Douillard FP, Mahony J, Cambillau C, et al. (2015) Structure and Assembly of TP901-1 Virion Unveiled by Mutagenesis. PLoS ONE 10(7): e0131676. doi:10.1371/journal.pone.0131676
dc.identifier.volume 10 en
dc.identifier.issued 7 en
dc.identifier.issn 1932-6203
dc.identifier.uri http://hdl.handle.net/10468/2303
dc.identifier.doi 10.1371/journal.pone.0131676
dc.description.abstract Bacteriophages of the Siphoviridae family represent the most abundant viral morphology in the biosphere, yet many molecular aspects of their virion structure, assembly and associated functions remain to be unveiled. In this study, we present a comprehensive mutational and molecular analysis of the temperate Lactococcus lactis-infecting phage TP901-1. Fourteen mutations located within the structural module of TP901-1 were created; twelve mutations were designed to prevent full length translation of putative proteins by non-sense mutations, while two additional mutations caused aberrant protein production. Electron microscopy and Western blot analysis of mutant virion preparations, as well as in vitro assembly of phage mutant combinations, revealed the essential nature of many of the corresponding gene products and provided information on their biological function(s). Based on the information obtained, we propose a functional and assembly model of the TP901-1 Siphoviridae virion. en
dc.description.sponsorship Science Foundation Ireland (SFI Principal Investigator Award 08/IN.1/B1909); Agence Nationale de la Recherche (ANR), France (Grant No. ANR-11-BSV8-004-01 Lacto-Phages) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Public Library of Science en
dc.rights © 2015 Stockdale et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited en
dc.rights.uri http://creativecommons.org/licenses/by/4.0/ en
dc.subject Lactococcal bacteriophage TP901-1 en
dc.subject Secondary structure prediction en
dc.subject Multiple sequence alignment en
dc.subject Protein homology detection en
dc.subject Tail-terminator protein en
dc.subject Lactic acid bacteria en
dc.subject Phage lambda en
dc.subject Crystal structure en
dc.subject Binding protein en
dc.subject 3-dimensional structure en
dc.title Structure and assembly of TP901-1 virion unveiled by mutagenesis en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Douwe van Sinderen, School of Microbiology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: d.vansinderen@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.internal.wokid WOS:000358157600126
dc.contributor.funder Science Foundation Ireland
dc.description.status Peer reviewed en
dc.identifier.journaltitle PLOS ONE en
dc.internal.IRISemailaddress d.vansinderen@ucc.ie en
dc.identifier.articleid e0131676


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© 2015 Stockdale et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted 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 © 2015 Stockdale et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited
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