Journal
VIROLOGY
Volume 434, Issue 2, Pages 242-250Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2012.08.031
Keywords
Molecular piracy; Virus assembly; Size determination; Procapsid; Electron microscopy; Scaffolding protein; Ribosomal protein L27; Co-expression; Staphylococcus aureus pathogenicity island 1
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Funding
- National Institutes of Health [R01 AI083255, R56 AI081837]
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80 alpha is a temperate, double-stranded DNA bacteriophage of Staphylococcus aureus that can act as a helper for the mobilization of S. aureus pathogenicity islands (SaPIs), including SaPI1. When SaPI1 is mobilized by 80 alpha, the SaPI genomes are packaged into capsids that are composed of phage proteins, but that are smaller than those normally formed by the phage. This size determination is dependent on SaPI1 proteins CpmA and CpmB. Here, we show that co-expression of the 80 alpha capsid and scaffolding proteins in S. aureus, but not in E. coli, leads to the formation of procapsid-related structures, suggesting that a host co-factor is required for assembly. The capsid and scaffolding proteins also undergo normal N-terminal processing upon expression in S. aureus, implicating a host protease. We also find that SaPI1 proteins CpmA and CpmB promote the formation of small capsids upon co-expression with 80 alpha capsid and scaffolding proteins in S. aureus. (C) 2012 Elsevier Inc. All rights reserved.
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