Assembly of bacteriophage 80[alpha] capsids in a Staphylococcus aureus expression system

80[alpha] is a temperate, double-stranded DNA bacteriophage of Staphylococcus aureus that can act as a ahelpera 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 phag...

Full description

Saved in:
Bibliographic Details
Published inVirology (New York, N.Y.) Vol. 434; no. 2; pp. 242 - 250
Main Authors Spilman, Michael S, Damle, Priyadarshan K, Dearborn, Altaira D, Rodenburg, Cynthia M, Chang, Jenny R, Wall, Erin A, Christie, Gail E, Dokland, Terje
Format Journal Article
LanguageEnglish
Published 20.12.2012
Subjects
Capsids
DNA
Escherichia coli
Genomes
pathogenicity islands
Phages
Proteinase
Staphylococcus aureus
Online AccessGet full text

Cover

More Information
Summary:80[alpha] is a temperate, double-stranded DNA bacteriophage of Staphylococcus aureus that can act as a ahelpera 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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
content type line 23
ObjectType-Feature-1
ISSN:0042-6822