A conserved acetyl esterase domain targets diverse bacteriophages to the Vi capsular receptor of Salmonella enterica serovar Typhi

Pickard, Derek, Toribio, Ana Luisa, Petty, Nicola K., van Tonder, Andries, Yu, Lu, Goulding, David, Barrell, Bart, Rance, Richard, Harris, David, Wetter, Michael, Wain, John, Choudhary, Jyoti, Thomson, Nicholas and Dougan, Gordon (2010) A conserved acetyl esterase domain targets diverse bacteriophages to the Vi capsular receptor of Salmonella enterica serovar Typhi. Journal of Bacteriology, 192 21: 5746-5754. doi:10.1128/JB.00659-10

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ242757_OA.pdf Full text (open access) application/pdf 3.61MB 0

Author Pickard, Derek
Toribio, Ana Luisa
Petty, Nicola K.
van Tonder, Andries
Yu, Lu
Goulding, David
Barrell, Bart
Rance, Richard
Harris, David
Wetter, Michael
Wain, John
Choudhary, Jyoti
Thomson, Nicholas
Dougan, Gordon
Title A conserved acetyl esterase domain targets diverse bacteriophages to the Vi capsular receptor of Salmonella enterica serovar Typhi
Formatted title
A conserved acetyl esterase domain targets diverse bacteriophages to the Vi capsular receptor of Salmonella enterica serovar Typhi
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 0021-9193
1067-8832
1098-5530
Publication date 2010-11
Sub-type Article (original research)
DOI 10.1128/JB.00659-10
Open Access Status File (Publisher version)
Volume 192
Issue 21
Start page 5746
End page 5754
Total pages 9
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Formatted abstract
A number of bacteriophages have been identified that target the Vi capsular antigen of Salmonella enterica serovar Typhi. Here we show that these Vi phages represent a remarkably diverse set of phages belonging to three phage families, including Podoviridae and Myoviridae. Genome analysis facilitated the further classifi-cation of these phages and highlighted aspects of their independent evolution. Significantly, a conserved protein domain carrying an acetyl esterase was found to be associated with at least one tail fiber gene for all Vi phages, and the presence of this domain was confirmed in representative phage particles by mass spectrometric analysis. Thus, we provide a simple explanation and paradigm of how a diverse group of phages target a single key virulence antigen associated with this important human-restricted pathogen.
Copyright © 2010, American Society for Microbiology. All Rights Reserved.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 36 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 38 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Wed, 22 Jun 2011, 19:33:11 EST by Dr Nicola Petty on behalf of School of Chemistry & Molecular Biosciences