ArticleCellular microbiology2011
Neisseria gonorrhoeae pilin glycan contributes to CR3 activation during challenge of primary cervical epithelial cells.
Article in Cellular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 76 citations in OpenAlex.
- Review
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- Tissue Models forFrontiers in cellular and infection microbiology · 2022Review
- Sexually TransmittedMedicines (Basel, Switzerland) · 2021Review
- Opportunities and Challenges of Bacterial Glycosylation for the Development of Novel Antibacterial Strategies.Frontiers in microbiology · 2021Review
- The Promiscuous Profile of Complement Receptor 3 in Ligand Binding, Immune Modulation, and Pathophysiology.Frontiers in immunology · 2021Review
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- Virulence of the emerging pathogen,Future microbiology · 2020Article
- Exploiting species specificity to understand the tropism of a human-specific toxin.Science advances · 2020Article
- Intimate Relations: Molecular and Immunologic Interactions BetweenFrontiers in microbiology · 2020Review
- Genetic determinants of genus-level glycan diversity in a bacterial protein glycosylation system.PLoS genetics · 2019Article
- Contribution of σJournal of bacteriology · 2019Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Expression of type IV pili by Neisseria gonorrhoeae plays a critical role in mediating adherence to human epithelial cells. Gonococcal pilin is modified with an O-linked glycan, which may be present as a di- or monosaccharide because of phase variation of select pilin glycosylation genes. It is accepted that bacterial proteins may be glycosylated; less clear is how the protein glycan may mediate virulence. Using primary, human, cervical epithelial (i.e. pex) cells, we now provide evidence to indicate that the pilin glycan mediates productive cervical infection. In this regard, pilin glycan-deficient mutant gonococci exhibited an early hyper-adhesive phenotype but were attenuated in their ability to invade pex cells. Our data further indicate that the pilin glycan was required for gonococci to bind to the I-domain region of complement receptor 3, which is naturally expressed by pex cells. Comparative, quantitative, infection assays revealed that mutant gonococci lacking the pilin glycan did not bind to the I-domain when it is in a closed, low-affinity conformation and cannot induce an active conformation to complement receptor 3 during pex cell challenge. To our knowledge, these are the first data to directly demonstrate how a protein-associated bacterial glycan may contribute to pathogenesis.
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Registered trials
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