dc.contributor.author |
Stockdale, Stephen R. |
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dc.contributor.author |
Collins, Barry |
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dc.contributor.author |
Spinelli, Silvia |
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dc.contributor.author |
Douillard, François P. |
en |
dc.contributor.author |
Mahony, Jennifer |
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dc.contributor.author |
Cambillau, Christian |
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dc.contributor.author |
van Sinderen, Douwe |
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dc.date.accessioned |
2016-02-17T10:07:57Z |
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dc.date.available |
2016-02-17T10:07:57Z |
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dc.date.issued |
2015 |
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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 |
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dc.identifier.volume |
10 |
en |
dc.identifier.issued |
7 |
en |
dc.identifier.issn |
1932-6203 |
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dc.identifier.uri |
http://hdl.handle.net/10468/2303 |
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dc.identifier.doi |
10.1371/journal.pone.0131676 |
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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. |
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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) |
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dc.format.mimetype |
application/pdf |
en |
dc.language.iso |
en |
en |
dc.publisher |
Public Library of Science |
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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 |
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dc.rights.uri |
http://creativecommons.org/licenses/by/4.0/ |
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dc.subject |
Lactococcal bacteriophage TP901-1 |
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dc.subject |
Secondary structure prediction |
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dc.subject |
Multiple sequence alignment |
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dc.subject |
Protein homology detection |
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dc.subject |
Tail-terminator protein |
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dc.subject |
Lactic acid bacteria |
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dc.subject |
Phage lambda |
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dc.subject |
Crystal structure |
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dc.subject |
Binding protein |
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dc.subject |
3-dimensional structure |
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dc.title |
Structure and assembly of TP901-1 virion unveiled by mutagenesis |
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dc.type |
Article (peer-reviewed) |
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dc.internal.authorcontactother |
Douwe van Sinderen, School of Microbiology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: d.vansinderen@ucc.ie |
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dc.internal.availability |
Full text available |
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dc.description.version |
Published Version |
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dc.internal.wokid |
WOS:000358157600126 |
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dc.contributor.funder |
Science Foundation Ireland |
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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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