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

ABSTRACT: 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.

SUBMITTER: Dang Y

PROVIDER: S-EPMC3094948 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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

Dang Ying Y Abudu Aierken A Son Sungmo S Harjes Elena E Spearman Paul P Matsuo Hiroshi H Zheng Yong-Hui YH

Journal of virology 20110323 11

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 ...[more]

PMID: 21430060

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