The Cag Type IV secretion apparatus proteins in Helicobacter pylori can mediate the injection of effector CagA protein into eukaryotic target cells. Although this apparatus forms an important pathway for bacterium-host interaction, its assembly process in vivo is poorly understood, and the proteins which contribute to break the bacterial cell walls in Cag-PAI have not yet been identified. The cagγ gene in Cag-PAI is a unique member that contains a conserved SLT catalysis domain, which makes it an attracting question whether cagy gene has the capacity to digest the bacterial cell wall. In the current study, therefore, the cagγ gene was cloned from the H. pylori NCTC 11637 and expressed in Escherichia coli, and its lytic effect on cell walls in vitro was observed. Results indicated that Cagγ protein has a lytic activity against bacterial cell walls. An allelic-exchange mutant (Δcagγ) was further constructed to investigate the relationship between Cagγ and effector CagA translocation. These results suggested that Cagγ contributed to the assembly of Cag Type IV secretion apparatus by digesting the peptidoglycan meshwork of bacterial cell walls.

Helicobacter pylori (H. pylori) is a highly successful human-specific gastric pathogen, infecting over half the world's population. Virulent H. pylori isolates harbour the cytotoxin-associated genes pathogenicity island (cag-PAI), the majority of which have no known function. In this study, we used cell infection assay and reverse transcriptase PCR, identified that CagL recombinant protein, one of the cag-PAI proteins, induced GES-1 cells to express cytokine IL-8. Then we performed western blot and translocation assay. Our result showed CagL polyclonal antibody counteracted translocation of CagA. This will provide a foundation for the further studies on its biological function.