Dimerization and interactions of Brucella suis VirB8 with VirB4 and VirB10 are required for its biological activity.

ABSTRACT: VirB8-like proteins are essential components of type IV secretion systems, bacterial virulence factors that mediate the translocation of effector molecules from many bacterial pathogens into eukaryotic cells. Based on cell biological, genetic, and x-ray crystallographic data, VirB8 was proposed to undergo multiple protein-protein interactions to mediate assembly of the translocation machinery. Here we report the results of a structure-function analysis of the periplasmic domain of VirB8 from the mammalian pathogen Brucella suis, which identifies amino acid residues required for three protein-protein interactions. VirB8 variants changed at residues proposed to be involved in dimerization, and protein-protein interactions were purified and characterized in vitro and in vivo. Changes at M102,

SUBMITTER: Paschos A 

PROVIDER: S-EPMC1464329 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature