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J Virol. 2011 Jun;85(11):5691-5. doi: 10.1128/JVI.00243-11. Epub 2011 Mar 23.

Identification of a single amino acid required for APOBEC3 antiretroviral cytidine deaminase activity.

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  • 1Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan, USA.


During studies of APOBEC3 (A3) anti-human immunodeficiency virus type 1 (anti-HIV-1) mechanisms, we identified a single cysteine at position 320 (C320) that disrupts A3DE activity. This residue is located in the recently identified DNA binding domain in A3G. Replacing C320 with a corresponding tyrosine from A3F (Y307) increased A3DE antiviral activity more than 20-fold. Conversely, replacing A3F Y307 with a cysteine or inserting a similar cysteine into A3B or A3G disrupted the anti-HIV activity of A3. Further investigation uncovered that C320 significantly reduces A3DE catalytic activity.

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