Protein profiling of infected human gastric epithelial cells with an Iranian Helicobacter pylori clinical isolate

The main objective of this study was to use high throughput approach to characterize the response of human gastric epithelial cells to Helicobacter pylori (H. pylori) infection at protein level.

Alteration of host cell protein profiles occurs due to H.pylori infection. This alteration seems to be strain specific. High throughput approaches, such as proteomics, can describe changes that occurs at the protein levelin the infected cells in response to H.pylori infection. In accordance with this point of view, we used two dimensional electrophoresis (2-DE)/MS to determine changes in proteome profile of gastric epithelial cells infected with a clinical isolate of H. pylori from an Iranian patient.

Human gastric epithelial cells (AGS) were infected by an Iranian H.pylori isolate (complete cagPAI, vacA s2m2, babA2, iceA1, sabA). The altered protein patterns separated by 2-DE were identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF MS) analysis.

The results showed 40 spots with significantly different intensities between the 2-DE gels. Protein SETSIP and Endoplasmic reticulum resident protein 29 were identified by MALD-TOF and Mascot search. Proteomic analysis for functional roles of these proteins showed that mechanisms to deal with stress conditions and transcriptional activator related to cell reprogramming are involved in H. pylori infection.

Using high throughput approaches, such as proteomics, we can provide further molecular details about interaction of H. pylori strains with the infected cells at protein level.