Mapping of a domain required for protein-protein interactions and inhibitory activity of a Helicobacter pylori dominant-negative VacA mutant protein.

ABSTRACT: The Helicobacter pylori VacA toxin is an 88-kDa secreted protein that causes multiple alterations in mammalian cells and is considered an important virulence factor in the pathogenesis of peptic ulcer disease and gastric cancer. We have shown previously that a VacA mutant protein lacking amino acids 6 to 27 (Delta6-27p88 VacA) is able to inhibit many activities of wild-type VacA in a dominant-negative manner. Analysis of a panel of C-terminally truncated Delta6-27p88 VacA proteins indicated that a fragment containing amino acids 1 to 478 (Delta6-27p48) exhibited a dominant-negative phenotype similar to that of the full-length Delta6-27p88 VacA protein. In contrast, a shorter VacA fragment lacking amino acids 6 to 27 (Delta6-27p33) did not exhibit detectable inhibitory activity. The Delta6-

SUBMITTER: Torres VJ 

PROVIDER: S-EPMC1418911 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature