ArticleThe Journal of infectious diseases2016
Desialylation of Neisseria gonorrhoeae Lipooligosaccharide by Cervicovaginal Microbiome Sialidases: The Potential for Enhancing Infectivity in Men.
Article in The Journal of infectious diseases, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 36 citations in OpenAlex.
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- Gardnerella Vaginolysin Potentiates Glycan Molecular Mimicry by Neisseria gonorrhoeae.The Journal of infectious diseases · 2023Article
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- Comparison of lipooligosaccharides from human challenge strains ofFrontiers in microbiology · 2023Article
- Bacterial vaginosis and health-associated bacteria modulate the immunometabolic landscape in 3D model of human cervix.NPJ biofilms and microbiomes · 2021Article
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- Members of Prevotella Genus Distinctively Modulate Innate Immune and Barrier Functions in a Human Three-Dimensional Endometrial Epithelial Cell Model.The Journal of infectious diseases · 2020Article
- Therapeutic CMP-Nonulosonates against Multidrug-ResistantJournal of immunology (Baltimore, Md. : 1950) · 2020Article
- Evolution of the exclusively human pathogenEvolutionary applications · 2019Article
- Sialidases FromFrontiers in cellular and infection microbiology · 2019Review
- Progress Toward a Gonococcal Vaccine: The Way Forward.Frontiers in immunology · 2019Review
- Human Factor H Domains 6 and 7 Fused to IgG1 Fc Are Immunotherapeutic againstJournal of immunology (Baltimore, Md. : 1950) · 2018Article
- Structure of the RecombinantmSphere · 2018Article
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8 authors at 3 institutions in 1 country.
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Abstract
Previous studies have demonstrated that Neisseria gonorrhoeae sialylates the terminal N-acetyllactosamine present on its lipooligosaccharide (LOS) by acquiring CMP-N-acetyl-5-neuraminic acid upon entering human cells during infection. This renders the organism resistant to killing by complement in normal human serum. N-acetyllactosamine residues on LOS must be free of N-acetyl-5-neuraminc acid (Neu5Ac; also known as "sialic acid") in order for organisms to bind to and enter urethral epithelial cells during infection in men. This raises the question of how the gonococcus infects men if N-acetyllactosamine residues are substituted by Neu5Ac during infection in women. Here, we demonstrate that women with gonococcal infections have levels of sialidases present in cervicovaginal secretions that can result in desialylation of (sialylated) gonococcal LOS. The principle sialidases responsible for this desialylation appear to be bacterial in origin. These studies suggest that members of the cervicovaginal microbiome can modify N. gonorrhoeae, which will enhance successful transmission to men.
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