Abstract
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.
Original language | English |
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Pages (from-to) | 9765-9769 |
Number of pages | 5 |
Journal | Journal of Virology |
Volume | 82 |
Issue number | 19 |
DOIs | |
Publication status | Published - 10-2008 |
All Science Journal Classification (ASJC) codes
- Microbiology
- Immunology
- Insect Science
- Virology