Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif |
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Authors: | Doehle Brian P Schäfer Alexandra Cullen Bryan R |
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Affiliation: | Center for Virology, Duke University Medical Center, Durham, NC 27710, USA. |
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Abstract: | While the human antiretroviral defense factors APOBEC3F and APOBEC3G are potent inhibitors of the replication of HIV-1 mutants lacking a functional vif gene, the Vif protein expressed by wild-type HIV-1 blocks the function of both host cell proteins. Here, we report that a third human protein, APOBEC3B, is able to suppress the infectivity of both Vif-deficient and wild-type HIV-1 with equal efficiency. APOBEC3B, which shows approximately 58% sequence identity to both APOBEC3F and APOBEC3G, shares the ability of these other human proteins to bind the nucleocapsid domain of HIV-1 Gag specifically and to thereby package into progeny virion particles. However, APOBEC3B differs from APOBEC3F and APOBEC3G in that it is unable to bind to HIV-1 Vif in co-expressing cells and is therefore efficiently packaged into HIV-1 virions regardless of Vif expression. Unfortunately, APOBEC3B also differs from APOBEC3F and APOBEC3G in that it is not normally expressed in the lymphoid cells that serve as targets for HIV-1 infection. These studies therefore raise the possibility that activation of the endogenous APOBEC3B gene in primary human lymphoid cells could form a novel and effective strategy for inhibition of HIV-1 replication in vivo. |
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Keywords: | APOBEC, apolipoprotein B mRNA editing enzyme catalytic polypeptide AGM, African green monkey HA, influenza virus hemagglutinin HIV, human immunodeficiency virus MLV, murine leukemia virus NC, nucleocapsid PBMC, peripheral blood mononuclear cells SIV, simian immunodeficiency virus |
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