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. Author manuscript; available in PMC: 2008 Feb 20.
Published in final edited form as: J Immunol. 2006 Jul 1;177(1):501–510. doi: 10.4049/jimmunol.177.1.501

FIGURE 2.

FIGURE 2

PorA and PorB3 on N. meningitidis strain H44/76 are not the ligands for fH. A, Binding of fH by flow cytometry to an unencapsulated mutant of H44/76 that lacked the ability to sialylate LOS (H44/76 siaD lst; broken line) and its two mutant derivatives that lacked either PorA (H44/76 siaD lst ΔporA; solid line) or PorB3 (H44/76 siaD lst ΔporB3; gray shaded histogram). B, fH binding to a mutant derivative of strain Y2220 siaD lst (fH nonbinder) whereby its PorB2 molecule was replaced with PorB3 of strain H44/76 (Y2220 siaD lst H44/76PorB3+; gray shaded histogram). fH binding to Y2220 siaD lst (negative control) is shown with the broken line, and the positive control strain, H44/76 siaD lst, by the solid line. Axes are as described for Fig. 1.