〔Abstract〕 Objective To clone and express the 453 bp fragment of P116 ge-ne FP2 ofMycoplasma pneumoniae, and to investigate the adhesion of P116 protein to A549 cells. Methods The immunogenicity and titer of purified P-116 protein fragment were detected by Western blot and ELISA in serum and antibody ofMycoplasma pneumoniaeinfected. Immunofluorescence was used to evaluate the adhesion and adhesion inhibition ofMycoplasma pneumoniaeto A549 cells by P116-FP2 polyclonal antibody.Mycoplasma pneumoniaeadhesion, adhesion inhibition and surface exposure were evaluated using the anti-P116 polycl-onal antibody and A549 cells adhesion assay. Results The results showed that P116-FP2 had immunoreactivity, and the ELISA method established with this protein had high sensitivity and specificity. The P116-FP2 antibody was prepared to block the adhesion ofMycoplasma pneumoniaeto A549 cells. With the increase of titer of polyclonal antibody, the adhesion rate ofMycoplasma pneumoniaeto A549 cells decreased significantly. Conclusion The P116-FP2 protein is proven to be immunoreactive preliminarily. The P116-FP2 polyclonal antibody can inhibit the adhesion ofMycoplasma pneumoniaeto A549 cells.