Key result
The human parechovirus 1 2C protein exhibits Mg2+-dependent ATP diphosphohydrolase activity, AMP kinase activity, and undergoes autophosphorylation in vitro.
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Suggests 2C as antiviral target for human parechovirus 1; leaves open in vivo functional validation.
The highly conserved picornavirus 2C proteins, thought to be involved in genome replication, contain three motifs found in NTPases/helicases of superfamily III. We report that human parechovirus 1 2C displays Mg2+-dependent ATP diphosphohydrolase activity in vitro, whereas other nucleoside triphosphates are not substrates for the hydrolysis. We also found that the 2C protein has an enzymatic activity that converts AMP to a corresponding diphosphate using ADP or ATP as a phosphate donor. In addition, we observed that ATP hydrolysis results in 2C autophosphorylation. These findings indicate that the parechovirus 2C protein has enzymatic activities, which may contribute to several functions in the viral replication cycle.
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Samuilova et al. (2005) studied Human parechovirus 1. HPEV1 2C protein vs. Mutant GST-2CK146A or GST alone was evaluated on Enzymatic activities (ATP hydrolysis, AMP kinase, autophosphorylation). The human parechovirus 1 2C protein exhibits Mg2+-dependent ATP diphosphohydrolase activity, AMP kinase activity, and undergoes autophosphorylation in vitro.
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