Truncated BabA binding domain (C51) promotes the binding of Helicobacter pylori to AGS cells

  Objective   To obtain a truncated binding domain of BabA capable of binding to Lewis b and to evaluate its effect on adhesion of H. pylori to AGS cells.

  Methods   The binding domain of BabA was truncated and the Swiss model was used to analyze structural changes. The truncated binding domain, named C51, was expressed and identified by Western blot. Native-PAGE electrophoresis was used to identify whether it is a multimer. Flow cytometry was used to detect its effect on adhesion of H. pylori J99 and M523 to AGS cells. The effect of C51 protein on H. pylori aggregation was observed by Gram staining.

  Results   The protein C51 was expressed and purified as a multimer. It increased the aggregation of J99 and M523 strains and their binding to AGS by 12% (t=8.211, P=0.001) and 22% (t=4.402, P=0.012), respectively.

  Conclusion   The protein C51 maintained the spatial structure related to adhesion and promoted the adhesion of H. pylori to AGS cells.