Characterization of Pseudomonas chlororaphis myovirus 201φ{symbol}2-1 via genomic sequencing, mass spectrometry, and electron microscopy

Julie A. Thomas, Mandy R. Rolando, Christopher A. Carroll, Peter S. Shen, David M. Belnap, Susan T. Weintraub, Philip Serwer, Stephen C. Hardies

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

Abstract

Pseudomonas chlororaphis phage 201φ{symbol}2-1 is a relative of Pseudomonas aeruginosa myovirus φ{symbol}KZ. Phage 201φ{symbol}2-1 was examined by complete genomic sequencing (316,674 bp), by a comprehensive mass spectrometry survey of its virion proteins and by electron microscopy. Seventy-six proteins, of which at least 69 have homologues in φ{symbol}KZ, were identified by mass spectrometry. Eight proteins, in addition to the major head, tail sheath and tail tube proteins, are abundant in the virion. Electron microscopy of 201φ{symbol}2-1 revealed a multitude of long, fine fibers apparently decorating the tail sheath protein. Among the less abundant virion proteins are three homologues to RNA polymerase β or β′ subunits. Comparison between the genomes of 201φ{symbol}2-1 and φ{symbol}KZ revealed substantial conservation of the genome plan, and a large region with an especially high rate of gene replacement. The φ{symbol}KZ-like phages exhibited a two-fold higher rate of divergence than for T4-like phages or host genomes.

Original languageEnglish (US)
Pages (from-to)330-338
Number of pages9
JournalVirology
Volume376
Issue number2
DOIs
StatePublished - Jul 5 2008

Keywords

  • Accelerated divergence
  • Bacteriophage
  • RNA polymerase
  • Virion proteins

ASJC Scopus subject areas

  • Virology

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