Open AccessStructure/Function Analysis of Neisseria meningitidis PilW, a Conserved Protein That Plays Multiple Roles in Type IV Pilus Biology
Author(s) -
Tim H. Szeto,
Andréa Dessen,
Vladimir Pelicic
Publication year - 2011
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.05313-11
Subject(s) - biology , pilus , neisseria meningitidis , biogenesis , mutagenesis , neisseria , function (biology) , organelle , genetics , microbiology and biotechnology , computational biology , gene , bacteria , mutant , escherichia coli
Type IV pili (Tfp) are widespread filamentous bacterial organelles that mediate multiple functions and play a key role in pathogenesis in several important human pathogens, includingNeisseria meningitidis . Tfp biology remains poorly understood at a molecular level because the roles of the numerous proteins that are involved remain mostly obscure. Guided by the high-resolution crystal structure we recently reported forN. meningitidis PilW, a widely conserved protein essential for Tfp biogenesis, we have performed a structure/function analysis by targeting a series of key residues through site-directed mutagenesis and analyzing the corresponding variants using an array of phenotypic assays. Here we show that PilW's involvement in the functionality of Tfp can be genetically uncoupled from its concurrent role in the assembly/stabilization of the secretin channels through which Tfp emerge on the bacterial surface. These findings suggest that PilW is a multifunctional protein.