TY - JOUR
T1 - Structure and assembly of TP901-1 virion unveiled by mutagenesis
AU - Stockdale, Stephen R.
AU - Collins, Barry
AU - Spinelli, Silvia
AU - Douillard, François P.
AU - Mahony, Jennifer
AU - Cambillau, Christian
AU - Van Sinderen, Douwe
N1 - Publisher Copyright:
© 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.
PY - 2015/7/6
Y1 - 2015/7/6
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/84940093463
U2 - 10.1371/journal.pone.0131676
DO - 10.1371/journal.pone.0131676
M3 - Article
C2 - 26147978
AN - SCOPUS:84940093463
SN - 1932-6203
VL - 10
JO - PLOS ONE
JF - PLOS ONE
IS - 7
M1 - e0131676
ER -