Structural Determinants of HIV-1 Vif Susceptibility and DNA Binding in APOBEC3F

Siu KK, et al., 4, 2593, Nat Commun, 2013

This important study reports the crystal structure of the HIV-1 viral infectivity factor (Vif) binding domain in A3F-CD2, a critical obstructer to retroviral replication. The author performed site-directed mutagenesis to map out the ssDNA-binding site, and developed a novel BLI-based HIV-1 Vif-APOBEC3 binding assay. The BLItz system first was used to determine the equilibrium dissociation constant for A3Fc-CD2/ssDNA binding using biotinylated ssDNA loaded onto Streptavidin biosensors. Second, ssDNA alanine-mutants were generated for each position and characterized similarly. Next, the authors used their BLI-based Vif-binding assay to map the HIV-1 Vif-binding interface at single-residue resolution.

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