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Article

Factor H binding and function in sialylated pathogenic neisseriae is influenced by gonococcal, but not meningococcal, porin.

Journal of immunology (Baltimore, Md. : 1950) - 1 Apr 2007

Madico Guillermo, Ngampasutadol Jutamas, Gulati Sunita, Vogel Ulrich, Rice Peter A, Ram Sanjay

Abstract excerpt

Neisseria gonorrhoeae and Neisseria meningitidis both express the lacto-N-neotetraose (LNT) lipooligosaccharide (LOS) molecule that can be sialylated. Although gonococcal LNT LOS sialylation enhances binding of the alternative pathway complement inhibitor factor H and renders otherwise serum-sensitive bacteria resistant to complement-dependent killing, the role of LOS sialylation in meningococcal serum resistance...

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Identifiers

PMID: 17372007
DOI: 10.4049/jimmunol.178.7.4489

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Factor H binding and function in sialylated pathogenic neisseriae is influenced by gonococcal, but not meningococcal, porin.PMID 17372007Read ↗

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