Abstract: The present invention provides methods for diagnosing and treating Helicobacter pylori infection by using a monoclonal antibody to detect Helicobacter pylori neutrophil-activating protein (HP-NAP) and inhibit the activity thereof. The monoclonal antibody is an ANTI-FLAG antibody that binds to a specific epitope on HP-NAP for the detection of HP-NAP in its native form or denatured form. Furthermore, the present invention uses the ANTI-FLAG antibody to block HP-NAP-induced production of reactive oxygen species by human neutrophils. Thus, the present invention can be applied in clinical diagnosis of Helicobacter pylori infection as well as treatment of the infection via inhibiting Helicobacter pylori-induced inflammation.

Abstract: The present invention provides methods for diagnosing and treating Helicobacter pylori infection by using a monoclonal antibody to detect Helicobacter pylori neutrophil-activating protein (HP-NAP) and inhibit the activity thereof. The monoclonal antibody is an anti-FLAG antibody that binds to a specific epitope on HP-NAP for the detection of HP-NAP in its native form or denatured form. Furthermore, the present invention uses the anti-FLAG antibody to block HP-NAP-induced production of reactive oxygen species by human neutrophils. Thus, the present invention can be applied in clinical diagnosis of Helicobacter pylori infection as well as treatment of the infection via inhibiting Helicobacter pylori-induced inflammation.

Abstract: Helicobacter pylori is closely associated with chronic gastritis, peptic ulcer disease, and gastric adenocarcinoma. Helicobacter pylori neutrophil-activating protein (HP-NAP), a virulence factor of Helicobacter pylori, plays an important role in pathogenesis of Helicobacter pylori infection. Since HP-NAP has been proposed as a candidate vaccine against Helicobacter pylori infection, an efficient way to obtain pure HP-NAP needs to be developed. In the present invention, recombinant HP-NAP expressed in Bacillus subtilis and Escherichia coli was purified through a single step of DEAE SEPHADEX ion-exchange chromatography with high purity. Also, purified recombinant HP-NAP was able to stimulate neutrophils to produce reactive oxygen species. Thus, recombinant HP-NAP obtained from our Bacillus subtilis expression system and Escherichia coli expression system is functionally active.

Abstract: Helicobacter pylori is closely associated with chronic gastritis, peptic ulcer disease, and gastric adenocarcinoma. Helicobacter pylori neutrophil-activating protein (HP-NAP), a virulence factor of Helicobacter pylori, plays an important role in pathogenesis of Helicobacter pylori infection. Since HP-NAP has been proposed as a candidate vaccine against Helicobacter pylori infection, an efficient way to obtain pure HP-NAP needs to be developed. In the present invention, recombinant HP-NAP expressed in Bacillus subtilis and Escherichia coli was purified through a single step of DEAE Sephadex ion-exchange chromatography with high purity. Also, purified recombinant HP-NAP was able to stimulate neutrophils to produce reactive oxygen species. Thus, recombinant HP-NAP obtained from our Bacillus subtilis expression system and Escherichia coli expression system is functionally active.