Viral entry into the host is the earliest stage of infection in the viral life cycle in which attachment proteins play a key role. VP31(WSV340/WSSV396), an envelope protein of white spot syndrome virus(WSSV), contains an Arg-Gly-Asp(RGD) peptide domain known as a cellular attachment site. At present, the process of VP31 interacting with shrimp host cells has not been explored. Therefore, the VP31 gene was cloned into p ET30a(+), expressed in Escherichia coli strain BL21 and purifi ed with immobilized metal ion affi nity chromatography. Four gill cellular proteins of shrimp( Fenneropenaeus c hinensis) were pulled down by an affi nity column coupled with recombinant VP31(r VP31), and the amino acid sequences were identifi ed with MALDI-TOF/TOF mass spectrometry. Hemocyanin, beta-actin, arginine kinase(AK), and an unknown protein were suggested as the putative VP31 receptor proteins. SDS-PAGE showed that AK is the predominant binding protein of VP31. An i n vitro binding activity experiment indicated that recombinant AK’s(r AK) binding activity with r VP31 is comparable to that with the same amount of WSSV. These results suggested that AK, as a member of the phosphagen kinase family, plays a role in WSSV infection. This is the fi rst evidence showing that AK is a binding protein of VP31. Further studies on this topic will elucidate WSSV infection mechanism in the future. Viral entry into the host is the earliest stage of infection in the viral life cycle in which attachment proteins play a key role. VP31 (WSV340 / WSSV396), an envelope protein of white spot syndrome virus (WSSV), contains an Arg-Gly- At present, the VP31 gene was cloned into p ET30a (+), expressed in Escherichia coli strain BL21 and purifi ed with immobilized metal ion affinity chromatography. Four gill cellular proteins of shrimp (Fenneropenaeus c hinensis) were pulled down by an affi nity column coupled with recombinant VP31 (r VP31), and the amino acid sequences were identif ed with MALDI- TOF / TOF mass spectrometry. Hemocyanin, beta-actin, arginine kinase (AK), and an unknown protein were suggested as the putative VP31 receptor proteins. SDS-PAGE showed that AK is the predominant binding protein of VP31. experime nt indicated that recombinant AK’s (r AK) binding activity with r VP31 is comparable to that with the same amount of WSSV. These results suggest that AK, as a member of the phosphagen kinase family, plays a role in WSSV infection. This is the fi rst evidence showing that AK is a binding protein of VP31. Further studies on this topic will elucidate WSSV infection mechanism in the future.