The Holin protein of bacteriophage PRD1 forms a pore for small-molecule and endolysin translocation.
J Bacteriol
; 187(15): 5397-405, 2005 Aug.
Article
em En
| MEDLINE
| ID: mdl-16030234
ABSTRACT
PRD1 is a bacteriophage with an icosahedral outer protein layer surrounding the viral membrane, which encloses the linear double-stranded DNA genome. PRD1 infects gram-negative cells harboring a conjugative IncP plasmid. Here we studied the lytic functions of PRD1. Using infected cells and plasmid-borne lysis genes, we demonstrated that a two-component lysis system (holin-endolysin) operates to release progeny phage particles from the host cell. Monitoring of ion fluxes and the ATP content of the infected cells allowed us to build a model of the sequence of lysis-related physiological changes. A decrease in the intracellular level of ATP is the earliest indicator of cell lysis, followed by the leakage of K+ from the cytosol approximately 20 min prior to the decrease in culture turbidity. However, the K+ efflux does not immediately lead to the depolarization of the cytoplasmic membrane or leakage of the intracellular ATP. These effects are observed only approximately 5 to 10 min prior to cell lysis. Similar results were obtained using cells expressing the holin and endolysin genes from plasmids.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Bacteriólise
/
Proteínas Virais
/
Salmonella enterica
/
Bacteriófago PRD1
Idioma:
En
Revista:
J Bacteriol
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Finlândia