Genomic organization and molecular characterization of SM1, a temperate bacteriophage of Streptococcus mitis.

Abstract:

:The direct binding of Streptococcus mitis to human platelets is mediated in part by two proteins (PblA and PblB) encoded by a lysogenic bacteriophage (SM1). Since SM1 is the first prophage of S. mitis that has been identified and because of the possible role of these phage-encoded proteins in virulence, we sought to characterize SM1 in greater detail. Sequencing of the SM1 genome revealed that it consisted of 34,692 bp, with an overall G+C content of 39 mol%. Fifty-six genes encoding proteins of 40 or more amino acids were identified. The genes of SM1 appear to be arranged in a modular, life cycle-specific organization. BLAST analysis also revealed that the proteins of SM1 have homologies to proteins from a wide variety of lambdoid phages. Bioinformatic analyses, in addition to N-terminal sequencing of the proteins, led to the assignment of possible functions to a number of proteins, including the integrase, the terminase, and two major structural proteins. Examination of the phage structural components indicates that the phage head may assemble using stable multimers of the major capsid protein, in a process similar to that of phage r1t. These findings indicate that SM1 may be part of a discrete subfamily of the Siphoviridae that includes at least phages r1t of Lactococcus lactis and SF370.3 of Streptococcus pyogenes.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Siboo IR,Bensing BA,Sullam PM

doi

10.1128/jb.185.23.6968-6975.2003

keywords:

subject

Has Abstract

pub_date

2003-12-01 00:00:00

pages

6968-75

issue

23

eissn

0021-9193

issn

1098-5530

journal_volume

185

pub_type

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