Multiple lysines combined in HIV-1 Vif determines the responsiveness to CBF-β
Copyright policy )Multiple lysines combined in HIV-1 Vif determines the responsiveness to CBF-β
The Vif (viral infectivity factor) protein of human immunodeficiency virus type-1 (HIV-1) is critical for HIV-1 infectivity. CBF-β is required for HIV-1 Vif function, as it increases the steady-state level of the HIV-1 Vif protein to promote host restriction factor APOBEC3 degradation. However, the precise mechanism by which CBF-β promotes HIV-1 Vif levels remains unclear. In the present study, we provided evidences that CBF-β promoted steady-state levels of HIV-1 Vif by inhibiting the degradation of HIV-1 Vif through the proteasome pathway. Our results reveal a new mechanism by which a cellular protein supports viral infectivity by inhibiting viral protein degradation.
- Northeast Forestry University China (People's Republic of)
Proteasome Endopeptidase Complex, Virulence, Lysine, HIV Infections, Core Binding Factor beta Subunit, Recombinant Proteins, HEK293 Cells, Amino Acid Substitution, Host-Pathogen Interactions, Proteolysis, HIV-1, Mutagenesis, Site-Directed, vif Gene Products, Human Immunodeficiency Virus, Humans
Proteasome Endopeptidase Complex, Virulence, Lysine, HIV Infections, Core Binding Factor beta Subunit, Recombinant Proteins, HEK293 Cells, Amino Acid Substitution, Host-Pathogen Interactions, Proteolysis, HIV-1, Mutagenesis, Site-Directed, vif Gene Products, Human Immunodeficiency Virus, Humans
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