Domains involved in calcineurin phosphatase inhibition and nuclear localisation in the African swine fever virus A238L protein.

摘要: The African swine fever virus A238L protein inhibits calcineurin phosphatase activity and activation of NF-kappaB p300 co-activator. An 82 amino acid domain containing residues 157 to 238 at the C-terminus was expressed in E. coli purified. This purified fragment acted as a potent inhibitor vitro with an IC50 approximately 70 nM. Two putative nuclear localisation signals were identified between 80 86 (NLS-1) 203 207 overlapping N-terminus docking motif (NLS-2). Mutation these motifs independently did not reduce compared wild type protein, whereas mutation both significantly reduced A238L. resulted dramatic increase provided intact NLS present. We propose that binding masks NLS-2 contributing cytoplasmic retention