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

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

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • APOBEC Deaminases
  • Amino Acid Sequence
  • Amino Acid Substitution / genetics
  • Binding Sites / genetics
  • Cell Line
  • Cysteine / genetics*
  • Cytidine Deaminase / genetics
  • Cytidine Deaminase / metabolism*
  • Cytosine Deaminase / genetics
  • Cytosine Deaminase / metabolism*
  • HIV-1 / immunology*
  • Humans
  • Molecular Sequence Data

Substances

  • Cytosine Deaminase
  • APOBEC Deaminases
  • APOBEC3 proteins, human
  • Cytidine Deaminase
  • Cysteine