Vitamin B6 Is Required for Full Motility and Virulence in Helicobacter pylori
Identifieur interne : 007341 ( Main/Merge ); précédent : 007340; suivant : 007342Vitamin B6 Is Required for Full Motility and Virulence in Helicobacter pylori
Auteurs : Alexandra Grubman ; Alexandra Phillips ; Marie Thibonnier ; Maria Kaparakis-Liaskos ; Chad Johnson ; Jean-Michel Thiberge ; Fiona J. Radcliff ; Chantal Ecobichon ; Agnès Labigne ; Hilde De Reuse ; George L. Mendz ; Richard L. FerreroSource :
- mBio [ 2150-7511 ] ; 2010.
Abstract
Despite recent advances in our understanding of how
Url:
DOI: 10.1128/mBio.00112-10
PubMed: 21151756
PubMed Central: 3000542
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PMC:3000542Le document en format XML
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Is Required for Full Motility and Virulence in <italic>Helicobacter pylori</italic>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Vitamin B<sub>6</sub>
Is Required for Full Motility and Virulence in <italic>Helicobacter pylori</italic>
</title>
<author><name sortKey="Grubman, Alexandra" sort="Grubman, Alexandra" uniqKey="Grubman A" first="Alexandra" last="Grubman">Alexandra Grubman</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Phillips, Alexandra" sort="Phillips, Alexandra" uniqKey="Phillips A" first="Alexandra" last="Phillips">Alexandra Phillips</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Thibonnier, Marie" sort="Thibonnier, Marie" uniqKey="Thibonnier M" first="Marie" last="Thibonnier">Marie Thibonnier</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Kaparakis Liaskos, Maria" sort="Kaparakis Liaskos, Maria" uniqKey="Kaparakis Liaskos M" first="Maria" last="Kaparakis-Liaskos">Maria Kaparakis-Liaskos</name>
<affiliation><nlm:aff id="aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Johnson, Chad" sort="Johnson, Chad" uniqKey="Johnson C" first="Chad" last="Johnson">Chad Johnson</name>
<affiliation><nlm:aff id="aff3"></nlm:aff>
</affiliation>
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<author><name sortKey="Thiberge, Jean Michel" sort="Thiberge, Jean Michel" uniqKey="Thiberge J" first="Jean-Michel" last="Thiberge">Jean-Michel Thiberge</name>
<affiliation><nlm:aff id="aff4"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Radcliff, Fiona J" sort="Radcliff, Fiona J" uniqKey="Radcliff F" first="Fiona J." last="Radcliff">Fiona J. Radcliff</name>
<affiliation><nlm:aff id="aff5"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Ecobichon, Chantal" sort="Ecobichon, Chantal" uniqKey="Ecobichon C" first="Chantal" last="Ecobichon">Chantal Ecobichon</name>
<affiliation><nlm:aff id="aff4"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Labigne, Agnes" sort="Labigne, Agnes" uniqKey="Labigne A" first="Agnès" last="Labigne">Agnès Labigne</name>
<affiliation><nlm:aff id="aff4"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="De Reuse, Hilde" sort="De Reuse, Hilde" uniqKey="De Reuse H" first="Hilde" last="De Reuse">Hilde De Reuse</name>
<affiliation><nlm:aff id="aff2"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Mendz, George L" sort="Mendz, George L" uniqKey="Mendz G" first="George L." last="Mendz">George L. Mendz</name>
<affiliation><nlm:aff id="aff6"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Ferrero, Richard L" sort="Ferrero, Richard L" uniqKey="Ferrero R" first="Richard L." last="Ferrero">Richard L. Ferrero</name>
</author>
</analytic>
<series><title level="j">mBio</title>
<idno type="eISSN">2150-7511</idno>
<imprint><date when="2010">2010</date>
</imprint>
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<front><div type="abstract" xml:lang="en"><p>Despite recent advances in our understanding of how <italic>Helicobacter pylori</italic>
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 <italic>H. pylori</italic>
, we generated low-infectivity variants of a mouse-colonizing <italic>H. pylori</italic>
strain using the classical technique of <italic>in vitro</italic>
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 <italic>Escherichia coli</italic>
vitamin B<sub>6</sub>
biosynthesis enzymes PdxA and PdxJ. Functional complementation studies with <italic>E. coli</italic>
confirmed <italic>H. pylori</italic>
PdxA and PdxJ to be <italic>bona fide</italic>
homologs of vitamin B<sub>6</sub>
biosynthesis enzymes. Importantly, <italic>H. pylori</italic>
PdxA was required for optimal growth <italic>in vitro</italic>
and was shown to be essential for chronic colonization in mice. In addition to having a well-known metabolic role, vitamin B<sub>6</sub>
is necessary for the synthesis of glycosylated flagella and for flagellum-based motility in <italic>H. pylori</italic>
. Thus, for the first time, we identify vitamin B<sub>6</sub>
biosynthesis enzymes as novel virulence factors in bacteria. Interestingly, <italic>pdxA</italic>
and <italic>pdxJ</italic>
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.</p>
</div>
</front>
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</TEI>
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