ArticleInfection and immunity2008
The periplasmic disulfide oxidoreductase DsbA contributes to Haemophilus influenzae pathogenesis.
Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Article
- Exploiting haem-iron dependence of nontypeableFrontiers in cellular and infection microbiology · 2025Review
- Functional annotation of Candida albicans hypothetical proteins: a bioinformatics approach.Archives of microbiology · 2024Article
- The Periplasmic Oxidoreductase DsbA Is Required for Virulence of the PhytopathogenInternational journal of molecular sciences · 2022Article
- Discovery and Contribution of Nontypeable Haemophilus influenzae NTHI1441 to Human Respiratory Epithelial Cell Invasion.Infection and immunity · 2019Article
- Insights into the Periplasmic Proteins ofInternational journal of molecular sciences · 2019Article
- Disulfide bond formation in prokaryotes.Nature microbiology · 2018Review
- Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.The Journal of biological chemistry · 2017Article
- The Landscape of Realized Homologous Recombination in Pathogenic Bacteria.Molecular biology and evolution · 2016Article
- Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.Journal of bacteriology · 2015Review
- Structure of the Acinetobacter baumannii dithiol oxidase DsbA bound to elongation factor EF-Tu reveals a novel protein interaction site.The Journal of biological chemistry · 2014Article
- Outer membrane protein P5 is required for resistance of nontypeable Haemophilus influenzae to both the classical and alternative complement pathways.Infection and immunity · 2014Article
- The two CcdA proteins of Bacillus anthracis differentially affect virulence gene expression and sporulation.Journal of bacteriology · 2013Article
- Genome-scale approaches to identify genes essential for Haemophilus influenzae pathogenesis.Frontiers in cellular and infection microbiology · 2012Review
- A novel zinc binding system, ZevAB, is critical for survival of nontypeable Haemophilus influenzae in a murine lung infection model.Infection and immunity · 2011Article
- Article
- Glutathione import in Haemophilus influenzae Rd is primed by the periplasmic heme-binding protein HbpA.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Article
- The heme-binding protein (HbpA) of Haemophilus influenzae as a virulence determinant.International journal of medical microbiology : IJMM · 2009Article
- Tracking insertion mutants within libraries by deep sequencing and a genome-wide screen for Haemophilus genes required in the lung.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.