A novel inhibitory domain of Helicobacter pylori protein CagA reduces CagA effects on host cell biology.

ABSTRACT: The Helicobacter pylori protein CagA (cytotoxin-associated gene A) is associated with an increased risk for gastric cancer formation. After attachment to epithelial cells, the bacteria inject CagA via a type IV secretion apparatus into host cells, where it exerts its biological activity. Host cell responses to intracellular CagA have been linked exclusively to signaling motifs in the C terminus of the CagA protein. Little is known about the functional role of the remaining CagA protein. Using transgenic expression of CagA mutants in epithelial cells, we were able to identify a novel CagA inhibitory domain at the N terminus consisting of the first 200 amino acids. This domain localizes to cell-cell contacts and increases the rate and strength of cell-cell adhesion in epithelial cells. Thus,

SUBMITTER: Pelz C 

PROVIDER: S-EPMC3059056 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature