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American Society for Microbiology, Journal of Virology, 11(85), p. 5691-5695, 2011

DOI: 10.1128/jvi.00243-11

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Identification of a Single Amino Acid Required for APOBEC3 Antiretroviral Cytidine Deaminase Activity

Journal article published in 2011 by Ying Dang, Aierken Abudu, SungMo Son, Elena Harjes ORCID, Paul Spearman, Hiroshi Matsuo, Yong-Hui Zheng
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.