OBJECTIVETo confirm the activity of non structural protein 1 (NSP1) of Rotavirus (RV) as E3 ubiquitin ligase by experiments and to provide some clues for NSP1 on the pathogenic mechanisms and replication of RV.

METHODSThe whole gene and RING deleted mutation gene of NSP1 were coloned into pEGFPC1 expression plasmid, and transfected into human embryonic kidney (HEK) 293 FT cells with pBlue-Script-HA-Ubiquitin. The expression of proteins were proved by using con-focal microscope and western blotting. The ubiquination of proteins were detected by co-immunoprecite.

RESULTSThe cellular proteins of HEK293FT are ubiquinated by NSP1 protein and NSP1 protein was self-ubiquinated also.

CONCLUSIONSIt revealed that RV NSP1 had the activity of E3 ubiquitin ligase and it may play a role on the modulate mechanisms of ubiquination.