Research on APOBEC3C / 中国免疫学杂志

ABSTRACT

APOBEC3 C is special as it has only weak antiviral functions and weakly restricts retroelements compared to other APOBEC3 s. APOBEC3 has only one cytidine deaminase domain which coordinates a zinc ion, and then is classified to A3 Z2 according to the amino acid specificity. APOBEC3 C induces less cytidine deamination in HIV-1 DNA than APOBEC3 G and has reduced ability to inhibit HIV-1 reverse transcription and integration compared to APOBEC3 G. APOBEC3 C induces G-to-A mutation that cannot block viral replications but contribute more to viral diversity. A single nucleotide polymorphism in human APOBEC3 C, a change from serine to isoleucine at position 188, results in increased enzymatic activity and potent antiviral activity against HIV-1. Dimerization of human APOBEC3 C increases the ability of continuous synthesis of single-stranded DNA, resulting in higher levels of mutation during reverse transcription in vitro and in cells. APOBEC3 C has evolved under positive selection in primates, and it is an important barrier that must be countered by the virus during natural infections. Therefore, research on APOBEC3 C may provide some ideas for anti-retroviral and anti-cancer therapeutic design.