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Neisseria gonorrhoeae PilC1 is a member of the PilC family of type IV pilus-associated adhesins found inNeisseria species and other type IV pilus-producing genera. Previously, a calcium-binding domain was described in the C-terminal domains of PilY1 ofPseudomonas aeruginosa and in PilC1 and PilC2 ofKingella kingae . Genetic analysis ofN. gonorrhoeae revealed a similar calcium-binding motif in PilC1. To evaluate the potential significance of this calcium-binding region inN. gonorrhoeae , we produced recombinant full-length PilC1 and a PilC1 C-terminal domain fragment. We show that, while alterations of the calcium-binding motif disrupted the ability of PilC1 to bind calcium, they did not grossly affect the secondary structure of the protein. Furthermore, we demonstrate that both full-length wild-type PilC1 and full-length calcium-binding-deficient PilC1 inhibited gonococcal adherence to cultured human cervical epithelial cells, unlike the truncated PilC1 C-terminal domain. Similar to PilC1 inK. kingae , but in contrast to the calcium-binding mutant ofP. aeruginosa PilY1, an equivalent mutation inN. gonorrhoeae PilC1 produced normal amounts of pili. However, theN. gonorrhoeae PilC1 calcium-binding mutant still had partial defects in gonococcal adhesion to ME180 cells and genetic transformation, which are both essential virulence factors in this human pathogen. Thus, we conclude that calcium binding to PilC1 plays a critical role in pilus function inN. gonorrhoeae .

Mutation of the Conserved Calcium-Binding Motif in Neisseria gonorrhoeae PilC1 Impacts Adhesion but Not Piliation