Interactions between the lipoprotein PilP and the secretin PilQ in Neisseria meningitidis.

ABSTRACT: Neisseria meningitidis can be the causative agent of meningitis or septicemia. This bacterium expresses type IV pili, which mediate a variety of functions, including autoagglutination, twitching motility, biofilm formation, adherence, and DNA uptake during transformation. The secretin PilQ supports type IV pilus extrusion and retraction, but it also requires auxiliary proteins for its assembly and localization in the outer membrane. Here we have studied the physical properties of the lipoprotein PilP and examined its interaction with PilQ. We found that PilP was an inner membrane protein required for pilus expression and transformation, since pilP mutants were nonpiliated and noncompetent. These mutant phenotypes were restored by the expression of PilP in trans. The pilP gene is located up

SUBMITTER: Balasingham SV 

PROVIDER: S-EPMC1951802 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature