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Background   Helicobacter pylori  is a human pathogen and during the process of infection, antigens from the bacterium elicit strong host humoral immune responses. In our previous report, native  H. pylori  UreG protein showed good reactivity with sera from  H. pylori  patients. This study was aimed at producing the recombinant form of the protein (rUreG) and determining its seroreactivities.    Methods  The coding sequence of  H. pylori  UreG was cloned and the recombinant protein expressed and purified by affinity chromatography using nickel nitrilotriacetic acid (Ni-NTA) resin. The antigenicity of rUreG to detect  H. pylori  specific antibodies was determined by western blot, using HRP-conjugated anti-human IgG and IgA antibodies as probes. A total of 70 sera, comprising 30 positive and 40 control serum samples, were used. The positive sera were from culture-positive  H. pylori -infected patients with duodenal ulcers, gastric ulcers, or gastritis. The control sera comprised three types of samples without detectable  H. pylori  antibodies, i.e. healthy individuals (with no history of gastric disorders) (n = 10); patients who attended an endoscopy clinic (because of gastrointestinal complaints) but were  H. pylori  culture negative (n = 20); and people with other diseases (n = 10). Additionally, hyperimmune mice serum against rUreG was raised and tested with the native and recombinant UreG protein.    Results  The  ureG  gene fragment was successfully cloned and expressed in both soluble and insoluble forms. Western blots on rUreG protein showed 70% (21/30) and 60% (18/30) reactivity with patients’ sera when probed with HRP-conjugated anti-human IgG and IgA antibodies, respectively; and the combination of the IgG and IgA western blots showed reactivity of 83.3% (25/30). By comparison, 97.5% and 92.5% of the control sera showed no reactivity when probed with HRP-conjugated anti-human IgG and IgA antibodies, respectively. Both the  H. pylori  lysate antigen and rUreG protein displayed a distinctive band at the expected molecular weight when probed with the hyperimmune mice serum.    Conclusion  The rUreG protein was successfully cloned and expressed and showed good reactivity with  H. pylori  culture-positive patients’ sera and no reactivity with most control sera. Thus, the diagnostic potential of this recombinant protein merits further investigation.

Helicobacter pylori recombinant UreG protein: cloning, expression, and assessment of its seroreactivity