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Virology. 2008 Jul 5;376(2):330-8. doi: 10.1016/j.virol.2008.04.004. Epub 2008 May 13.

Characterization of Pseudomonas chlororaphis myovirus 201varphi2-1 via genomic sequencing, mass spectrometry, and electron microscopy.

Author information

1
Department of Biochemistry, The University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, Texas 78229-3900, USA.

Abstract

Pseudomonas chlororaphis phage 201varphi2-1 is a relative of Pseudomonas aeruginosa myovirus phiKZ. Phage 201 phi2-1 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 phiKZ, 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 201 phi2-1 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 beta or beta' subunits. Comparison between the genomes of 201 phi2-1 and phiKZ revealed substantial conservation of the genome plan, and a large region with an especially high rate of gene replacement. The phiKZ-like phages exhibited a two-fold higher rate of divergence than for T4-like phages or host genomes.

PMID:
18474389
PMCID:
PMC2577825
DOI:
10.1016/j.virol.2008.04.004
[Indexed for MEDLINE]
Free PMC Article

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