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

Ying Dang, Aierken Abudu, SungMo Son, Elena Harjes, Paul Spearman, Hiroshi Matsuo, Yong Hui Zheng

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)5691-5695
Number of pages5
JournalJournal of virology
Volume85
Issue number11
DOIs
StatePublished - Jun 2011

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