Interaction between protein subunits of the type IV secretion system of Bartonella henselae

Abstract

In this study we used the yeast two-hybrid system to identify interactions between protein subunits of the virB type IV secretion system of Bartonella henselae. We report interactions between inner membrane and periplasmic proteins, the pilus polypeptide, and the core complex and a novel interaction between VirB3 and VirB5.

FIG. 1.

Genetic organization of the TFSS of B. henselae.

FIG. 2.

His-VirB3 copurifies with MBP-VirB5. MBP-VirB5 or MBP alone was immobilized on amylose columns and used to capture His-VirB3 from a crude lysate subsequently washed through the column. Fractions (1 ml) eluted from the column were analyzed by Western blotting for the presence of copurified His-VirB3 using anti-His antisera (A) or for MBP-VirB5 or MBP using anti-MBP antisera (B).

FIG. 3.

Model depicting the location of the VirB proteins in the structure of the B. henselae TFSS apparatus.