As the outermost structure of microsporidia, the spore wall is the bridge for microsporidia to communicate with the external environment. Therefore, studying the spore wall composition may play a key role in elucidating the mechanism of host parasite interaction. In this study, the spore wall protein (SWP7) of Enterocytozoon hepatopenaei (EHP) was studied. Firstly, the basic characteristics of the SWP7 sequence were analyzed by bioinformatics. Then the gene sequence was synthesized, the prokaryotic expression vector was constructed, and the induced recombinant protein was purified. Finally, the anti SWP7 rabbit polyclonal antibody was prepared. After the specificity verification of the antibody by western blotting, the localization of the SWP7 protein on mature spores was observed and analyzed by indirect immunofluorescence. The results showed that there was a signal peptide sequence in the N terminal of SWP7, and there was none of transmembrane domain and GPI anchor site, which indicated that SWP7 may display the function as a secretory protein. Meanwhile, it was predicted that SWP7 had multiple phosphorylation sites, which may paticipate in the signal transduction, immune response, receptor activation and other functions. The results of indirect immunofluorescence showed that SWP7 was uniformly expressed in the spore wall of mature EHP, which might participate in the germination process. The results lay a foundation for further study on the function and mechanism of SWP7 in the EHP invasion. [Chinese Fishery Quality and Standards, 2022, 12(6): 01-08]