Tail-associated structural protein gp61 of Staphylococcus aureus phage φmR11 has bifunctional lytic activity

Mohammad Rashel, Jumpei Uchiyama, Iyo Takemura, Hiroshi Hoshiba, Takako Ujihara, Hiroyoshi Takatsuji, Koichi Honke, Shigenobu Matsuzaki

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)

Abstract

A tailed bacteriophage, φMR11 (siphovirus), was selected as a candidate therapeutic phage against Staphylococcus aureus infections. Gene 61, one of the 67 ORFs identified, is located in the morphogenic module. The gene product (gp61) has lytic domains homologous to CHAP (corresponding to an amidase function) at its N-terminus and lysozyme subfamily 2 (LYZ2) at its C-terminus. Each domain of gp61 was purified as a recombinant protein. Both the amidase [amino acids (aa) 1-150] and the lysozyme (aa 401-624) domains but not the linker domain (aa 151-400) caused efficient lysis of S. aureus. Immunoelectron microscopy localized gp61 to the tail tip of the φMR11 phage. These data strongly suggest that gp61 is a tail-associated lytic factor involved in local cell-wall degradation, allowing the subsequent injection of φMR11 DNA into the host cytoplasm. Staphylococcus aureus lysogenized with φMR11 was also lysed by both proteins. Staphylococcus aureus strains on which φMR11 phage can only produce spots but not plaques were also lysed by each protein, indicating that gp61 may be involved in 'lysis from without'. This is the first report of the presence of a tail-associated virion protein that acts as a lysin, in an S. aureus phage.

Original languageEnglish
Pages (from-to)9-16
Number of pages8
JournalFEMS Microbiology Letters
Volume284
Issue number1
DOIs
Publication statusPublished - Jul 2008
Externally publishedYes

Keywords

  • Bacteriophage
  • Staphylococcus aurerus
  • Tail-associated lysin

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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