Identification of a single amino acid required for APOBEC3 antiretroviral cytidine deaminase activity |
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| Authors: | Dang Ying Abudu Aierken Son Sungmo Harjes Elena Spearman Paul Matsuo Hiroshi Zheng Yong-Hui |
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| Affiliation: | 1Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan;2Department of Biochemistry, Molecular Biology & Biophysics, and Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota;3Departments of Pediatrics & Microbiology & Immunology, Emory University School of Medicine, Atlanta, Georgia |
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| 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. |
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