Biochemical Analysis Of CBF-β Promote SIVagm Vif Function

APOBEC3 family of proteins is an important of immune lentiviral replication limiting factor. Lentivirus encoding the accessory proteins Vif recruit Cullin5-ElonginB-ElonginC E3 ubiquitin ligase complex,make the APOBEC3G (A3G) poly-ubiquitination and degradation, thereby inhibiting A3G restrictions on the virus.CBF-3 is RUNX family transcription cofactors may be adjusted A3G Vif-mediated degradation. To explore the CBF-P on African green Qauqaut immunodeficiency virus Vif protein (SIVagm Vif) regulatory mechanism and its impact on the degradation of A3G, this study biochemical and virological methods SIVagm and HIV-1 Vif protein encoded CBF-β action carried out comparative studies.The results show, SIVagm encoded Vif degradation of the corresponding species A3Gagm also need CBF-β auxiliary. Among the biochemical function test, CBF-β auxiliary SIVagm Vif-mediated degradation mechanism A3Gagm with HIV-1 Vif protein has a certain similarity, also promote stability SIVagm Vif protein in the cell and break SIVagm Vif by CBF-β in the oligomerization state of protein aggregation within the cell, to make more effective SIVagm Vif degradation A3Gagm corresponding species. These results suggest that CBF-β Auxiliary Vif-mediated degradation of A3G conserved in primate lentiviruses.When Vif (HIV-1/SIVagm) deletion of the N-terminal 12 amino acids, CBF- β auxiliary Vif protein modulator significantly reduce the ability of A3G degradation. Experimental results of the study biochemical function of the protein Vif deletion mutants show, Vif deletion mutants lost their interaction with the CBF-β, CBF-β Vif deletion does not promote stability in the body cells, Vif in cells is still mainly in the high-mer form. It is suggested that, Vif protein N-terminal lentivirus encoding amino acids 12 to interact with the CBF-β plays an important role.