Salmonella Typhimurium-specific bacteriophage ?SH19 and the origins of species specificity in the Vi01-like phage family

Whole genome sequencing of bacteriophages suitable for biocontrol of pathogens in food products is a pre-requisite to any phage-based intervention procedure. Trials involving the biosanitization of Salmonella Typhimurium in the pig production environment identified one such candidate, ?SH19. This ph...

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Bibliographic Details
Published in:Virology journal 2011-11, Vol.8, p.498
Main Authors: Hooton, Steven PT, Timms, Andrew R, Rowsell, Joanna, Wilson, Ray, Connerton, Ian F
Format: Article
Language:English
Subjects:
Bacteria
Bacteriology
Bacteriophages
Colleges & universities
DNA sequencing
Food
Genetic aspects
Genetic testing
Genomes
Health aspects
Microbiology
Nucleotide sequencing
Salmonella
Salmonella typhimurium
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Summary:Whole genome sequencing of bacteriophages suitable for biocontrol of pathogens in food products is a pre-requisite to any phage-based intervention procedure. Trials involving the biosanitization of Salmonella Typhimurium in the pig production environment identified one such candidate, ?SH19. This phage was sequenced and analysis of its 157,785 bp circular dsDNA genome revealed a number of interesting features. ?SH19 constitutes another member of the recently-proposed Myoviridae Vi01-like family of phages, containing S. Typhi-specific Vi01 and Shigella-specific SboM-AG3. At the nucleotide level ?SH19 is highly similar to phage Vi01 (80-98% pairwise identity over the length of the genome), with the major differences lying in the region associated with host-range determination. Analyses of the proteins encoded within this region by ?SH19 revealed a cluster of three putative tail spikes. Of the three tail spikes, two have protein domains associated with the pectate lyase family of proteins (Tsp2) and P22 tail spike family (Tsp3) with the prospect that these enable Salmonella O antigen degradation. Tail spike proteins of Vi01 and SboM-AG3 are predicted to contain conserved right-handed parallel [beta]-helical structures but the internal protein domains are varied allowing different host specificities. The addition or exchange of tail spike protein modules is a major contributor to host range determination in the Vi01-like phage family.
ISSN:1743-422X
1743-422X
DOI:10.1186/1743-422X-8-498