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.contributor.funder	Science Foundation Ireland
dc.date.accessioned	2016-02-17T10:07:57Z
dc.date.available	2016-02-17T10:07:57Z
dc.date.issued	2015
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.description.status	Peer reviewed	en
dc.description.version	Published Version	en
dc.format.mimetype	application/pdf	en
dc.identifier.articleid	e0131676
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.doi	10.1371/journal.pone.0131676
dc.identifier.issn	1932-6203
dc.identifier.issued	7	en
dc.identifier.journaltitle	PLOS ONE	en
dc.identifier.uri	https://hdl.handle.net/10468/2303
dc.identifier.volume	10	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

Structure and assembly of TP901-1 virion unveiled by mutagenesis

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