TABLE 1.

Surface plasmon resonance analysis of the gonococcal pilin-CR3 interaction^a

Strain	Glycan	KD (nM)
		rI-domain		Human CR3
		Mouse	Human
MS11 wild type	Gal(α1-3) diNAcBac	NCDI	349 ± 45	907 ± 43.8
MS11 pglA	diNAcBac	NCDI	NCDI	NCDI

^aThe interaction between N. gonorrhoeae MS11 pilin modified with either a disaccharide or a monosaccharide and mouse rI-domain, human rI-domain, and human rCR3 was characterized by SPR analysis. Results listed are the means ± standard errors from three replicate experiments. No concentration-dependent interaction (NCDI; no binding of ≤2 μM glycan to immobilized protein) was observed with either of the gonococcal pilins and the mouse rI-domain. The human rI-domain and rCR3 showed NCDI with MS11 pglA pilin. A high-affinity interaction (nanomolar range) was only observed between the disaccharide modified pilin and both the human rI-domain and rCR3.