Abstract: Objective To prepare the polyclonal antibody against methyl-accepting chemotaxis signal transduction protein
(MCP) of Helicobacter hepaticus (H.hepaticus). Methods The recombinant plasmid pET22b +/MCP was transformed into E.coli
BL2l(DE3) to express the fusion protein His-rhMCP under the induction of IPTG. The fusion protein was purified and the
antibody was obtained by immunizing rabbits. The titer of the polyclonal antibody was tested by indirect ELISA, and the
specificity of the antibody was identified based on Western blotting using the prepared cell surface proteins (CSPs) of the
bacteria. Results The fusion protein was successfully expressed, and the titer of the antibody reached 1∶32 000. Western
blotting indicated that the antibody could specifically bind to CSPs and His-rhMCP. Conclusion The antibody with a high titer
and specificity was prepared to facilitate further study of the pathogenicity and epidemiology of H.hepaticus in human.