Inactivation of Haemophilus influenzae Lipopolysaccharide Biosynthesis Genes Interferes with Outer Membrane Localization of the Hap Autotransporter
Identifieur interne : 000862 ( Main/Exploration ); précédent : 000861; suivant : 000863Inactivation of Haemophilus influenzae Lipopolysaccharide Biosynthesis Genes Interferes with Outer Membrane Localization of the Hap Autotransporter
Auteurs : Nicole A. Spahich [États-Unis] ; Derek W. Hood [Royaume-Uni] ; E. Richard Moxon [Royaume-Uni] ; Joseph W. St. Geme [États-Unis]Source :
- Journal of Bacteriology [ 0021-9193 ] ; 2012.
Abstract
Nontypeable
Url:
DOI: 10.1128/JB.06316-11
PubMed: 22287523
PubMed Central: 3302475
Affiliations:
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Le document en format XML
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Lipopolysaccharide Biosynthesis Genes Interferes with Outer Membrane Localization of the Hap Autotransporter</title>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Inactivation of <named-content content-type="genus-species">Haemophilus influenzae</named-content>
Lipopolysaccharide Biosynthesis Genes Interferes with Outer Membrane Localization of the Hap Autotransporter</title>
<author><name sortKey="Spahich, Nicole A" sort="Spahich, Nicole A" uniqKey="Spahich N" first="Nicole A." last="Spahich">Nicole A. Spahich</name>
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<front><div type="abstract" xml:lang="en"><p>Nontypeable <named-content content-type="genus-species">Haemophilus influenzae</named-content>
is a major cause of localized respiratory tract disease and initiates infection by colonizing the nasopharynx. Colonization requires adherence to host epithelial cells, which is mediated by surface proteins such as the Hap adhesin. In this study, we identified a relationship between Hap levels in the outer membrane and lipopolysaccharide (LPS) biosynthesis enzymes. We found that mutation of the <italic>rfaF</italic>
, <italic>pgmB</italic>
, <italic>lgtC</italic>
, <italic>kfiC</italic>
, <italic>orfE</italic>
, <italic>rfbP</italic>
, <italic>lsgB</italic>
, or <italic>lsgD</italic>
genes, which are involved in the synthesis of the LPS oligosaccharide core in <named-content content-type="genus-species">H. influenzae</named-content>
strain Rd/HapS243A, resulted in loss of Hap in the bacterial outer membrane and a decrease in <italic>hap</italic>
transcript levels. In contrast, the same mutations had no effect on outer membrane localization of <named-content content-type="genus-species">H. influenzae</named-content>
P5 or IgA1 protease or levels of <italic>p5</italic>
or <italic>iga1</italic>
transcripts, suggesting a Hap-specific effect. Elimination of the HtrA periplasmic protease resulted in a return of Hap to the outer membrane and restoration of <italic>hap</italic>
transcript levels. Consistently, in <italic>lgtC</italic>
phase-off bacteria, Hap was absent from the outer membrane, and <italic>hap</italic>
transcript levels were reduced. Hap localization and <italic>hap</italic>
transcript levels were not related to LPS size but to the functions of the LPS biosynthesis enzymes themselves. We speculate that the lack of certain LPS biosynthesis enzymes causes Hap to mislocalize and accumulate in the periplasm, where it is degraded by HtrA. This degradation then leads to a decrease in <italic>hap</italic>
transcript levels. Together, these data highlight a novel interplay between Hap and LPS biosynthesis that can influence <named-content content-type="genus-species">H. influenzae</named-content>
interactions with the host.</p>
</div>
</front>
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