Binding of the Helicobacter pylori OipA causes apoptosis of host cells via modulation of Bax/Bcl-2 levels.

The H. pylori outer inflammatory protein A (OipA) is an outer membrane protein that contributes to gastric inflammation. OipA is believed to affect intra-cellular signalling and modulate the host signalling pathways. The aim of the current study was to clarify the role of OipA in H. pylori pathogenesis and its effect on host cell signalling pathways. To this end, the oipA gene was isolated and inserted into cloning and expression vectors. The recombinant plasmid was transferred into an expression host to produce OipA, which was subsequently purified by affinity chromatography and used for antibody production. A confluent monolayer of gastric cell lines was treated with various concentrations of OipA and investigated for attachment, toxicity, and apoptosis and alterations in signalling pathways. OipA bound to gastric cell lines confirming its role in the attachment of H. pylori to host cells. The ratio of Bax/Bcl-2 and caspase3, 8, FasL in the host cells were assessed and the results showed that the Bax/Bcl-2 ratio as well as the level of cleaved-caspase 3 was elevated in OipA-treated cells. These findings suggest that OipA can bind and induce toxic events as well as triggering apoptotic cascade in host gastric cells through intrinsic pathway.