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TitleA multivalent adsorption apparatus explains the broad host range of phage phi92: a comprehensive genomic and structural analysis.
Journal, issue, pagesJ Virol, Vol. 86, Issue 19, Page 10384-10398, Year 2012
Publish dateJul 11, 2012
AuthorsDavid Schwarzer / Falk F R Buettner / Christopher Browning / Sergey Nazarov / Wolfgang Rabsch / Andrea Bethe / Astrid Oberbeck / Valorie D Bowman / Katharina Stummeyer / Martina Mühlenhoff / Petr G Leiman / Rita Gerardy-Schahn /
PubMed AbstractBacteriophage phi92 is a large, lytic myovirus isolated in 1983 from pathogenic Escherichia coli strains that carry a polysialic acid capsule. Here we report the genome organization of phi92, the ...Bacteriophage phi92 is a large, lytic myovirus isolated in 1983 from pathogenic Escherichia coli strains that carry a polysialic acid capsule. Here we report the genome organization of phi92, the cryoelectron microscopy reconstruction of its virion, and the reinvestigation of its host specificity. The genome consists of a linear, double-stranded 148,612-bp DNA sequence containing 248 potential open reading frames and 11 putative tRNA genes. Orthologs were found for 130 of the predicted proteins. Most of the virion proteins showed significant sequence similarities to proteins of myoviruses rv5 and PVP-SE1, indicating that phi92 is a new member of the novel genus of rv5-like phages. Reinvestigation of phi92 host specificity showed that the host range is not limited to polysialic acid-encapsulated Escherichia coli but includes most laboratory strains of Escherichia coli and many Salmonella strains. Structure analysis of the phi92 virion demonstrated the presence of four different types of tail fibers and/or tailspikes, which enable the phage to use attachment sites on encapsulated and nonencapsulated bacteria. With this report, we provide the first detailed description of a multivalent, multispecies phage armed with a host cell adsorption apparatus resembling a nanosized Swiss army knife. The genome, structure, and, in particular, the organization of the baseplate of phi92 demonstrate how a bacteriophage can evolve into a multi-pathogen-killing agent.
External linksJ Virol / PubMed:22787233 / PubMed Central
MethodsEM (single particle)
Resolution19.0 - 26.0 Å
Structure data

EMDB-2063:
A 3-D cryo-electron microscopy structure of bacteriophage phi92 capsid
Method: EM (single particle) / Resolution: 19.0 Å

EMDB-2064:
A 3-D cryo-electron structure of bacteriophage phi92 baseplate
Method: EM (single particle) / Resolution: 26.0 Å

EMDB-5409:
A 3-D cryo-electron structure of bacteriophage phi92 contractile tail
Method: EM (single particle) / Resolution: 26.0 Å

Source
  • Staphylococcus phage 92 (virus)
  • coliphage phi92 (unknown)

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