Objective    To study the function of CagL protein of recombinant Helicobacter pylori (Hp) through preparing rabbit anti-CagL specific polyclonal antibody and blocking the adhesion of Hp with host cells.     Methods    CagL gene was amplified by PCR

then constructed into prokaryotic expression vector pET-22b. Expressed protein of CagL was purified by affinity chromatography

and then used to immunize rabbits to prepare anti-CagL polyclonal antibody serum

so as to detect whether CagL polyclonal antibody serum can block the adhesion of Hp with host cells and analyze the activity of IL-8.      Results    Recombinant CagL protein was successfully constructed and purified. CagL polyclonal antibody serum played a stronger role in blocking the adhesion of Hp with host cells

and can induce host cells to secrete IL-8.      Conclusion    Our study suggests that CagL plays a role in Hp pathogenicity and colonization

and secretion of IL-8.