Abstract
HIV-1 Vif counteracts restrictive APOBEC3 proteins by targeting them for proteasomal degradation. To determine the regions mediating sensitivity to Vif, we compared human APOBEC3F, which is HIV-1 Vif sensitive, with rhesus APOBEC3F, which is HIV-1 Vif resistant. Rhesus-human APOBEC3F chimeras and amino acid substitution mutants were tested for sensitivity to HIV-1 Vif. This approach identified the α3 and α4 helices of human APOBEC3F as important determinants of the interaction with HIV-1 Vif.
Copyright © 2014, American Society for Microbiology. All Rights Reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Substitution
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Animals
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Cytosine Deaminase / genetics
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Cytosine Deaminase / metabolism*
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DNA Mutational Analysis
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HIV-1 / immunology*
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Humans
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Macaca mulatta
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Mutant Proteins / genetics
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Mutant Proteins / metabolism
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Protein Interaction Mapping
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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vif Gene Products, Human Immunodeficiency Virus / metabolism*
Substances
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Mutant Proteins
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Recombinant Proteins
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vif Gene Products, Human Immunodeficiency Virus
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vif protein, Human immunodeficiency virus 1
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APOBEC3F protein, human
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Cytosine Deaminase