PMID: 9480984Mar 28, 1998

A novel sialic acid binding site on factor H mediates serum resistance of sialylated Neisseria gonorrhoeae

The Journal of Experimental Medicine
Sanjay RamPeter A Rice

Abstract

Factor H (fH), a key alternative complement pathway regulator, is a cofactor for factor I-mediated cleavage of C3b. fH consists of 20 short consensus repeat (SCR) domains. Sialic acid binding domains have previously been localized to fH SCRs 6-10 and 13. To examine fH binding on a sialylated microbial surface, we grew Neisseria gonorrhoeae in the presence of 5'-cytidinemonophospho-N-acetylneuraminic acid, which sialylates lipooligosaccharide and converts to serum resistance gonococci previously sensitive to nonimmune serum killing. fH domains necessary for binding sialylated gonococci were determined by incubating organisms with recombinant human fH (rH) and nine mutant rH molecules (deletions spanning the entire fH molecule). rH and all mutant rH molecules that contained SCRs 16-20 bound to the sialylated strain; no mutant molecule bound to serum-sensitive nonsialylated organisms. Sialic acid was demonstrated to be the fH target by flow cytometry that showed a fourfold increase in fH binding that was reversed by neuraminidase-mediated cleavage of sialic acid off gonococci. Functional specificity of fH was confirmed by decreased total C3 binding and almost complete conversion to iC3b on sialylated gonococci. Sialic acid can the...Continue Reading

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Related Concepts

lipo-chitin oligosaccharide
Complement factor H, human
Antigens, Bacterial
Complement C3b
Gonorrhea
Lipopolysaccharides
Neisseria gonorrhoeae
Neuraminidase
Selfish DNA
Sialic Acids

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