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

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Abstract

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 (Kd ∼10 μM) 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) © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Tsirulnikov, K., Abuladze, N., Vahi, R., Hasnain, H., Phillips, M., Ryan, C. M., … Pushkin, A. (2012). Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein. FEBS Letters, 586(21), 3799–3804. https://doi.org/10.1016/j.febslet.2012.09.015

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