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Literature summary extracted from

  • Lewis, L.A.; Shafer, W.M.; Dutta Ray, T.; Ram, S.; Rice, P.A.
    Phosphoethanolamine residues on the lipid A moiety of Neisseria gonorrhoeae lipooligosaccharide modulate binding of complement inhibitors and resistance to complement killing (2013), Infect. Immun., 81, 33-42.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.43 Neisseria gonorrhoeae
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 gene lptA
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Synonyms

EC Number Synonyms Comment Organism
2.7.8.43 LptA
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 Neisseria gonorrhoeae

General Information

EC Number General Information Comment Organism
2.7.8.43 malfunction loss of phosphoethanolamine from lipid A diminishes binding of the complement regulatory protein C4b binding protein (C4BP) to the FA19 porin B (PorB), providing a molecular basis to explain the susceptibility of an lptA null strain of FA19 to killing by normal human serum. Loss of phosphoethanolamine from lipid A also affects binding of the alternative pathway regulator factor H to PorB of some strains, e.g. strains 252 and 1291, but not of strains FA1090 and 273. Complementation of lptA null strains with lptA restores C4BP binding, decreased C4b deposition, and increased resistance to killing by normal human serum Neisseria gonorrhoeae
2.7.8.43 physiological function phosphoethanolamine-lipid A contributes to serum resistance by modulating factor H binding Neisseria gonorrhoeae