Abstract: To study the phosphorylation catalyze effect of wsv083, wsv083, VP19 and VP28 were sub-cloned into a pET28a vector and expressed in the prokaryotic expression system. The obtained protein wsv083, supernatant of wsv083 expression strain lysate and dephosphorylation wsv083 were used to interact with VP19 and VP28. Plasmids of wsv083, VP19 and VP28 were transformed into the same host strain. The results showed that phosphorlation of VP19 and VP28 were not found, while wsv083 itself displayed threonine and tyrosine phosphorylation. The author changed expression plasmid of wsv083, but wsv083 still presented the same phosphorylation. Furthermore, when the sequence of wsv083 was mutated to make its kinase activity lost, the expressed wsv083 did not have any phosphorylation. In conclusion, the results presented that phosphorylation of VP19 and VP28 were not catalyzed by wsv083, but wsv083 was able to make self-phosphorylation.