title: [Study on the ubiquitin ligase activity of rotavirus NSP1 protein].
abstract: OBJECTIVE
  To 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.
  
  
  METHODS
  The 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.
  
  
  RESULTS
  The cellular proteins of HEK293FT are ubiquinated by NSP1 protein and NSP1 protein was self-ubiquinated also.
  
  
  CONCLUSIONS
  It revealed that RV NSP1 had the activity of E3 ubiquitin ligase and it may play a role on the modulate mechanisms of ubiquination.
authors: State Key Laboratory of Molecular Virology and Genetic Engineering, Institute of Pathogen Biology, Peking Union Medical College & Chinese Academy of Medical Sciences, Beijing 100730.
authors: Lan
authors: L
authors: Qin
authors: Xiao-Bo
authors: XB
authors: Lei
authors: Li-Li
authors: LL
authors: Ren
authors: Jian-Wei
authors: JW
authors: Wang
authors: Tao
authors: T
authors: Hong