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Journal of Virology, October 2008, p. 9765-9769, Vol. 82, No. 19
0022-538X/08/$08.00+0 doi:10.1128/JVI.01051-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Department of Virology and Parasitology, Fujita Health University School of Medicine, Toyoake, Aichi 470-1192, Japan
Received 19 May 2008/ Accepted 11 July 2008
The Aichi virus 2A protein is not a protease, unlike many other picornavirus 2A proteins, and it is related to a cellular protein, H-rev107. Here, we examined the replication properties of two 2A mutants in Vero cells and a cell-free translation/replication system. In one mutant, amino acids 36 to 126 were replaced with an unrelated amino acid sequence. In the other mutant, the NC motif conserved in the H-rev107 family of proteins was changed to alanine residues. The two mutations abolished virus replication in cells. The mutations affected both negative- and positive-strand synthesis, the defect in positive-strand synthesis being more severe than that in negative-strand synthesis.
Published ahead of print on 23 July 2008.
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