NDLI: The relative roles of fHbp, NspA and lipooligosaccharide sialylation in regulation of the alternative pathway of complement on meningococci

Content Provider	PubMed Central
Author	Lewis, Lisa A. Carter, Matthew Ram, Sanjay
Abstract	Neisseria meningitidis inhibits the alternative pathway (AP) of complement utilizing diverse mechanisms, including expression of capsule (select serogroups), Neisserial surface protein A (NspA), factor H binding protein (fHbp) and lipooligosaccharide (LOS) sialylation. The contribution of the latter three molecules in AP regulation in encapsulated meningococci was studied using isogenic mutants. When LOS was unsialylated, deleting NspA alone from group A strain A2594 (low fHbp/high NspA) significantly increased AP-mediated C3 deposition. C3 deposition further increased ~2-fold in a ΔfHbpΔNspA double mutant, indicating cooperative fHbp function. LOS sialylation of A2594 ΔfHbpΔNspA decreased the rate of C3 deposition, revealing AP inhibition by LOS sialic acid. Maximal C3 deposition on group B strain H44/76 (high fHbp/low NspA) occurred when all three molecules were absent; again, LOS sialylation attenuated the AP in the absence of both fHbp and NspA. When H44/76 LOS was unsialylated, both fHbp and NspA independently inhibited the AP. LOS sialylation enhanced binding of fH C-terminal domains 18–20 to C3 fragments deposited on bacteria. Interaction of meningococci with non-human complement is relevant for animal models and vaccine evaluation studies that employ non-human complement. Consistent with their human-specific fH binding, neither fHbp nor NspA regulated the rat AP. However, LOS sialylation inhibited the rat AP and, as with human serum, enhanced binding of rat fH to surface-bound C3. These data highlight the cooperative roles of meningococcal NspA and fHbp in regulating the human AP and broaden the molecular basis for LOS sialylation in AP regulation on meningococci in more than one animal species.
Related Links	http://dx.doi.org/10.4049/jimmunol.1103748
Ending Page	5072
Page Count	10
Starting Page	5063
File Format	PDF
ISSN	00221767
e-ISSN	15506606
Journal	Journal of Immunology (Baltimore, Md. : 1950)
Issue Number	10
Volume Number	188
Language	English
Publisher Date	2012-05-15
Access Restriction	Open
Subject Keyword	Medicine(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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The relative roles of factor H binding protein, neisserial surface protein A, and lipooligosaccharide sialylation in regulation of the alternative pathway of complement on meningococci.

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