In this study, the primers was designed according to MMP （Myristylated membrane protein）gene sequence of FV3, and then cloned the MMP gene using genome of RGV as the template. Computer-assisted analysis revealed the putative open reading frame encoded a protein of 323 amino acids with a predicted molecular weight of 35kDa. Amino acid alignment of MMP with other proteins of viruses in the same genus showed that they were mostly homologious, with identity of 91-99%, of which a transmembrane domain was predicted.
MMP fusion protein was deleted the transmembrane domain when prokaryotic expressing, and the antibodies against it was prepared. The intracellular distribution and western blot analysis indicated that the MMP gene coded a membrane protein.