C-type lectins (CTL) are a family of carbohydrate-binding proteins which it not only recognize and bind to potentially pathogenic microbes but also activate the complement pathway in the innate immunity of invertebrates. In this study, LvCTL3 protein was bonded by cloning the LvCTL3, which was isolated from Litopenaeus vannamei shrimp into the pET200/D-TOPO vector to construct a recombinant pET200/LvCTL3 plasmid. The plasmid was then transferred into competent E. coli BL21 (DE3) cells to express the protein. The expression of LvCTL3 protein was confirmed by SDS-PAGE. Pathogen binding assays confirmed recombinant LvCTL3 protein had strong agglutination with the pathogenic Vibrio parahaemolyticus, which caused acute hepatopancreas necrosis (AHPND) in white-leg shrimp. This preliminary study showed LvCTL3 protein acted as a PRR that inhibited AHPND-causing bacteria and could be used for