Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein

Aminoacylase 3 (AA3) mediates deacetylation of N-acetyl aromatic amino acids and mercapturic acids. Deacetylation of mercapturic acids of exo- and endobiotics are likely involved in their toxicity. AA3 is predominantly expressed in kidney, and to a lesser extent in liver, brain, and blood. AA3 has been recently reported to interact with the hepatitis C virus core protein (HCVCP) in the yeast two-hybrid system. Here we demonstrate that AA3 directly binds to HCVCP (K-d similar to 10 mu M) that may by implicated in HCV pathogenesis. AA3 also revealed a weak endopeptidase activity towards the N-terminus of HCVCP. Structured summary of protein interactions: AA3 cleaves HCVCP by protease assay (View interaction). AA3 cleaves AA3 by protease assay (View interaction). AA3 binds to HCVCP by surface plasmon resonance (View Interaction: 1, 2, 3, 4, 5) Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.