dc.contributor.author |
Grubman, A |
en |
dc.contributor.author |
Phillips, A |
en |
dc.contributor.author |
Thibonnier, M |
en |
dc.contributor.author |
Kaparakis-Liaskos, M |
en |
dc.contributor.author |
Johnson, C |
en |
dc.contributor.author |
Thiberge, J-M |
en |
dc.contributor.author |
Radcliff, Fiona |
en |
dc.contributor.author |
Ecobichon, C |
en |
dc.contributor.author |
Labigne, A |
en |
dc.contributor.author |
de Reuse, H |
en |
dc.contributor.author |
Mendz, GL |
en |
dc.contributor.author |
Ferrero, RL |
en |
dc.contributor.editor |
Rappouli, R |
en |
dc.date.accessioned |
2012-03-25T20:50:55Z |
en |
dc.date.issued |
2010 |
en |
dc.identifier.citation |
MBIO 1(3):9 pages Article number ARTN e00112-10 01 Jul 2010 |
en |
dc.identifier.issn |
2150-7511 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/15218 |
en |
dc.description.abstract |
Despite recent advances in our understanding of how Helicobacter pylori causes disease, the factors that allow this pathogen to persist in the stomach have not yet been fully characterized. To identify new virulence factors in H. pylori, we generated low-infectivity variants of a mouse-colonizing H. pylori strain using the classical technique of in vitro attenuation. The resulting variants and their highly infectious progenitor bacteria were then analyzed by global gene expression profiling. The gene expression levels of five open reading frames (ORFs) were significantly reduced in low-infectivity variants, with the most significant changes observed for ORFs HP1583 and HP1582. These ORFs were annotated as encoding homologs of the Escherichia coli vitamin B6 biosynthesis enzymes PdxA and PdxJ. Functional complementation studies with E. coli confirmed H. pylori PdxA and PdxJ to be bona fide homologs of vitamin B6 biosynthesis enzymes. Importantly, H. pylori PdxA was required for optimal growth in vitro and was shown to be essential for chronic colonization in mice. In addition to having a well-known metabolic role, vitamin B6 is necessary for the synthesis of glycosylated flagella and for flagellum-based motility in H. pylori. Thus, for the first time, we identify vitamin B6 biosynthesis enzymes as novel virulence factors in bacteria. Interestingly, pdxA and pdxJ orthologs are present in a number of human pathogens, but not in mammalian cells. We therefore propose that PdxA/J enzymes may represent ideal candidates for therapeutic targets against bacterial pathogens. |
en |
dc.publisher |
American Society for Microbiology |
en |
dc.relation.ispartofseries |
mBio |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/2150-7511/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.title |
Vitamin B6 is required for full motility and virulence in Helicobacter pylori |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1128/mBio.00112-10 |
en |
pubs.issue |
3 |
en |
pubs.volume |
1 |
en |
dc.rights.holder |
Copyright: American Society for Microbiology |
en |
dc.identifier.pmid |
21151756 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
165624 |
en |
pubs.org-id |
Medical and Health Sciences |
en |
pubs.org-id |
Medical Sciences |
en |
pubs.org-id |
Molecular Medicine |
en |
pubs.number |
e00112-10 |
en |
pubs.record-created-at-source-date |
2010-10-22 |
en |
pubs.dimensions-id |
21151756 |
en |