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Basic Characteristics of Mutations
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Mutation Site
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G143R |
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Mutation Site Sentence
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Conversely, NL4-3 Vif containing the mutations W11R or G143R displayed activity close to that of unmutated NL4-3 Vif. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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Vif |
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Standardized Encoding Gene
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Vif
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Genotype/Subtype
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HIV-1 |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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HIV Infections
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Immune
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- |
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Target Gene
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-
|
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
|
- |
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Location
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- |
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Literature Information
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PMID
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16201018
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Title
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Natural variation in Vif: differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification
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Author
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Simon V,Zennou V,Murray D,Huang Y,Ho DD,Bieniasz PD
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Journal
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PLoS pathogens
|
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Journal Info
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2005 Sep;1(1):e6
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Abstract
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The HIV-1 Vif protein counteracts the antiviral activity exhibited by the host cytidine deaminases APOBEC3G and APOBEC3F. Here, we show that defective vif alleles can readily be found in HIV-1 isolates and infected patients. Single residue changes in the Vif protein sequence are sufficient to cause the loss of Vif-induced APOBEC3 neutralization. Interestingly, not all the detected defects lead to a complete inactivation of Vif function since some mutants retained selective neutralizing activity against APOBEC3F but not APOBEC3G or vice versa. Concordantly, independently hypermutated proviruses with distinguishable patterns of G-to-A substitution attributable to cytidine deamination induced by APOBEC3G, APOBEC3F, or both enzymes were present in individuals carrying proviruses with completely or partly defective Vif variants. Natural variation in Vif function may result in selective and partial neutralization of cytidine deaminases and thereby promote viral sequence diversification within HIV-1 infected individuals.
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Sequence Data
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DQ097739-DQ097768
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