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PLoS One. 2015 Jul 6;10(7):e0131676. doi: 10.1371/journal.pone.0131676. eCollection 2015.

Structure and Assembly of TP901-1 Virion Unveiled by Mutagenesis.

Author information

1
School of Microbiology, University College Cork, Western Road, Cork, Ireland.
2
Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France.
3
Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France; Centre National de la Recherche Scientifique, AFMB, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France.
4
School of Microbiology, University College Cork, Western Road, Cork, Ireland; Alimentary Pharmabiotic Centre, University College Cork, Western Road, Cork, Ireland.

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.

PMID:
26147978
PMCID:
PMC4493119
DOI:
10.1371/journal.pone.0131676
[Indexed for MEDLINE]
Free PMC Article

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