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    The periplasmic disulfide oxidoreductase DsbA contributes to Haemophilus influenzae pathogenesis

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    Authors
    Rosadini, Charles V.
    Wong, Sandy M. S.
    Akerley, Brian J.
    UMass Chan Affiliations
    Department of Molecular Genetics and Microbiology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2008-01-24
    Keywords
    Animals; Bacteremia; Bacterial Proteins; Carrier Proteins; Female; Gene Deletion; Haemophilus Infections; Haemophilus influenzae; development; Heme; Lipoproteins; Mice; Mice, Inbred C57BL; Periplasm; Protein Disulfide-Isomerases; Rats; Rats, Sprague-Dawley; Survival Rate; Virulence
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://dx.doi.org/10.1128/IAI.01378-07
    Abstract
    Haemophilus influenzae is an obligate human pathogen that persistently colonizes the nasopharynx and causes disease when it invades the bloodstream, lungs, or middle ear. Proteins that mediate critical interactions with the host during invasive disease are likely to be secreted. Many secreted proteins require addition of disulfide bonds by the DsbA disulfide oxidoreductase for activity or stability. In this study, we evaluated the role in H. influenzae pathogenesis of DsbA, as well as HbpA, a substrate of DsbA. Mutants of H. influenzae Rd and type b strain Eagan having nonpolar deletions of dsbA were attenuated for bacteremia in animal models, and complemented strains exhibited virulence equivalent to that of the parental strains. Comparison of predicted secreted proteins in H. influenzae to known DsbA substrates in other species revealed several proteins that could contribute to the role of dsbA in virulence. One candidate, the heme transport protein, HbpA, was examined because of the importance of exogenous heme for aerobic growth of H. influenzae. The presence of a dsbA-dependent disulfide bond in HbpA was verified by an alkylation protection assay, and HbpA was less abundant in a dsbA mutant. The hbpA mutant exhibited reduced bacteremia in the mouse model, and complementation restored its in vivo phenotype to that of the parental strain. These results indicate that dsbA is required in vivo and that HbpA and additional DsbA-dependent factors are likely to participate in H. influenzae pathogenesis.
    Source
    Infect Immun. 2008 Apr;76(4):1498-508. Epub 2008 Jan 22. Link to article on publisher's site
    DOI
    10.1128/IAI.01378-07
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32803
    PubMed ID
    18212083
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1128/IAI.01378-07
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    Morningside Graduate School of Biomedical Sciences Scholarly Publications

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