A conserved acetyl esterase domain targets diverse bacteriophages to the Vi capsular receptor of Salmonella enterica serovar typhi
Pickard, D
Toribio, AL
Petty, NK
Van Tonder, A
Yu, L
Goulding, D
Barrell, B
Rance, R
Harris, D
Wetter, M
Wain, J
Choudhary, J
Thomson, N
Dougan, G
- Publication Type:
- Journal Article
- Citation:
- Journal of Bacteriology, 2010, 192 (21), pp. 5746 - 5754
- Issue Date:
- 2010-01-01
Closed Access
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2012007780OK.pdf | 3.77 MB | Adobe PDF |
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Pickard, D | en_US |
dc.contributor.author | Toribio, AL | en_US |
dc.contributor.author |
Petty, NK https://orcid.org/0000-0001-6528-9886 |
en_US |
dc.contributor.author | Van Tonder, A | en_US |
dc.contributor.author | Yu, L | en_US |
dc.contributor.author | Goulding, D | en_US |
dc.contributor.author | Barrell, B | en_US |
dc.contributor.author | Rance, R | en_US |
dc.contributor.author | Harris, D | en_US |
dc.contributor.author | Wetter, M | en_US |
dc.contributor.author | Wain, J | en_US |
dc.contributor.author | Choudhary, J | en_US |
dc.contributor.author | Thomson, N | en_US |
dc.contributor.author | Dougan, G | en_US |
dc.date.issued | 2010-01-01 | en_US |
dc.identifier.citation | Journal of Bacteriology, 2010, 192 (21), pp. 5746 - 5754 | en_US |
dc.identifier.issn | 0021-9193 | en_US |
dc.identifier.uri | http://hdl.handle.net/10453/27801 | |
dc.description.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. | en_US |
dc.relation.ispartof | Journal of Bacteriology | en_US |
dc.relation.isbasedon | 10.1128/JB.00659-10 | en_US |
dc.subject.classification | Microbiology | en_US |
dc.subject.mesh | Salmonella typhi | en_US |
dc.subject.mesh | Salmonella Phages | en_US |
dc.subject.mesh | Acetylesterase | en_US |
dc.subject.mesh | Polysaccharides, Bacterial | en_US |
dc.subject.mesh | Viral Proteins | en_US |
dc.subject.mesh | Gene Expression Regulation, Viral | en_US |
dc.subject.mesh | Protein Structure, Tertiary | en_US |
dc.subject.mesh | Synteny | en_US |
dc.subject.mesh | Genome, Viral | en_US |
dc.subject.mesh | Molecular Sequence Data | en_US |
dc.title | A conserved acetyl esterase domain targets diverse bacteriophages to the Vi capsular receptor of Salmonella enterica serovar typhi | en_US |
dc.type | Journal Article | |
utslib.citation.volume | 21 | en_US |
utslib.citation.volume | 192 | en_US |
utslib.for | 0605 Microbiology | en_US |
utslib.for | 06 Biological Sciences | en_US |
utslib.for | 07 Agricultural and Veterinary Sciences | en_US |
utslib.for | 11 Medical and Health Sciences | en_US |
pubs.embargo.period | Not known | en_US |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation | |
utslib.copyright.status | closed_access | |
pubs.issue | 21 | en_US |
pubs.publication-status | Published | en_US |
pubs.volume | 192 | en_US |
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.
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