Binding of Complement Factor H to Loop 5 of Porin Protein 1A: A Molecular Mechanism of Serum Resistance of Nonsialylated Neisseria gonorrhoeae

@article{Ram1998BindingOC,
  title={Binding of Complement Factor H to Loop 5 of Porin Protein 1A: A Molecular Mechanism of Serum Resistance of Nonsialylated Neisseria gonorrhoeae},
  author={S. Ram and D. McQuillen and S. Gulati and C. Elkins and M. Pangburn and P. Rice},
  journal={Journal of Experimental Medicine},
  year={1998},
  volume={188},
  pages={671-680}
}
Neisseria gonorrhoeae isolated from patients with disseminated infection are often of the porin (Por1A) serotype and resist killing by nonimmune normal human serum. The molecular basis of this resistance (termed stable serum resistance) in these strains has not been fully defined but is not related to sialylation of lipooligosaccharide. Here we demonstrate that Por1A bearing gonococcal strains bind more factor H, a critical downregulator of the alternative complement pathway, than their Por1B… Expand
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The contrasting mechanisms of serum resistance of Neisseria gonorrhoeae and group B Neisseria meningitidis.
TLDR
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