<it>Salmonella </it>Typhimurium-specific bacteriophage ΦSH19 and the origins of species specificity in the Vi01-like phage family

<p>Abstract</p> <p>Background</p> <p>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 <it>Salmonella </it>Typ...

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Main Authors: Wilson Ray, Rowsell Joanna, Timms Andrew R, Hooton Steven PT, Connerton Ian F
Format: Article
Language:English
Published: BMC 2011-11-01
Series:Virology Journal
Subjects:
Online Access:http://www.virologyj.com/content/8/1/498
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author Wilson Ray
Rowsell Joanna
Timms Andrew R
Hooton Steven PT
Connerton Ian F
author_facet Wilson Ray
Rowsell Joanna
Timms Andrew R
Hooton Steven PT
Connerton Ian F
author_sort Wilson Ray
collection DOAJ
description <p>Abstract</p> <p>Background</p> <p>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 <it>Salmonella </it>Typhimurium in the pig production environment identified one such candidate, ΦSH19.</p> <p>Results</p> <p>This phage was sequenced and analysis of its 157,785 bp circular dsDNA genome revealed a number of interesting features. ΦSH19 constitutes another member of the recently-proposed <it>Myoviridae </it>Vi01-like family of phages, containing <it>S</it>. Typhi-specific Vi01 and <it>Shigella</it>-specific SboM-AG3. At the nucleotide level ΦSH19 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 ΦSH19 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 <it>Salmonella </it>O antigen degradation. Tail spike proteins of Vi01 and SboM-AG3 are predicted to contain conserved right-handed parallel β-helical structures but the internal protein domains are varied allowing different host specificities.</p> <p>Conclusions</p> <p>The addition or exchange of tail spike protein modules is a major contributor to host range determination in the Vi01-like phage family.</p>
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spelling doaj.art-05cdf1bf68de42129c7eb4dde49ecca12022-12-22T01:20:30ZengBMCVirology Journal1743-422X2011-11-018149810.1186/1743-422X-8-498<it>Salmonella </it>Typhimurium-specific bacteriophage ΦSH19 and the origins of species specificity in the Vi01-like phage familyWilson RayRowsell JoannaTimms Andrew RHooton Steven PTConnerton Ian F<p>Abstract</p> <p>Background</p> <p>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 <it>Salmonella </it>Typhimurium in the pig production environment identified one such candidate, ΦSH19.</p> <p>Results</p> <p>This phage was sequenced and analysis of its 157,785 bp circular dsDNA genome revealed a number of interesting features. ΦSH19 constitutes another member of the recently-proposed <it>Myoviridae </it>Vi01-like family of phages, containing <it>S</it>. Typhi-specific Vi01 and <it>Shigella</it>-specific SboM-AG3. At the nucleotide level ΦSH19 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 ΦSH19 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 <it>Salmonella </it>O antigen degradation. Tail spike proteins of Vi01 and SboM-AG3 are predicted to contain conserved right-handed parallel β-helical structures but the internal protein domains are varied allowing different host specificities.</p> <p>Conclusions</p> <p>The addition or exchange of tail spike protein modules is a major contributor to host range determination in the Vi01-like phage family.</p>http://www.virologyj.com/content/8/1/498Phage biocontrolbiosanitizationbacteriophage genomics<it>Salmonella </it>Typhimurium<it>Myoviridae</it>P22-like tail spikepectate lyase tail spike domainlipopolysaccharide
spellingShingle Wilson Ray
Rowsell Joanna
Timms Andrew R
Hooton Steven PT
Connerton Ian F
<it>Salmonella </it>Typhimurium-specific bacteriophage ΦSH19 and the origins of species specificity in the Vi01-like phage family
Virology Journal
Phage biocontrol
biosanitization
bacteriophage genomics
<it>Salmonella </it>Typhimurium
<it>Myoviridae</it>
P22-like tail spike
pectate lyase tail spike domain
lipopolysaccharide
title <it>Salmonella </it>Typhimurium-specific bacteriophage ΦSH19 and the origins of species specificity in the Vi01-like phage family
title_full <it>Salmonella </it>Typhimurium-specific bacteriophage ΦSH19 and the origins of species specificity in the Vi01-like phage family
title_fullStr <it>Salmonella </it>Typhimurium-specific bacteriophage ΦSH19 and the origins of species specificity in the Vi01-like phage family
title_full_unstemmed <it>Salmonella </it>Typhimurium-specific bacteriophage ΦSH19 and the origins of species specificity in the Vi01-like phage family
title_short <it>Salmonella </it>Typhimurium-specific bacteriophage ΦSH19 and the origins of species specificity in the Vi01-like phage family
title_sort it salmonella it typhimurium specific bacteriophage φsh19 and the origins of species specificity in the vi01 like phage family
topic Phage biocontrol
biosanitization
bacteriophage genomics
<it>Salmonella </it>Typhimurium
<it>Myoviridae</it>
P22-like tail spike
pectate lyase tail spike domain
lipopolysaccharide
url http://www.virologyj.com/content/8/1/498
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