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 |
|---|---|
| Pages (from-to) | 9765-9769 |
| Number of pages | 5 |
| Journal | Journal of Virology |
| Volume | 82 |
| Issue number | 19 |
| DOIs | |
| Publication status | Published - 01-10-2008 |
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All Science Journal Classification (ASJC) codes
- Microbiology
- Immunology
- Insect Science
- Virology
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Aichi virus 2A protein is involved in viral RNA replication. / Sasaki, Jun; Taniguchi, Koki.
In: Journal of Virology, Vol. 82, No. 19, 01.10.2008, p. 9765-9769.Research output: Contribution to journal › Article
TY - JOUR
T1 - Aichi virus 2A protein is involved in viral RNA replication
AU - Sasaki, Jun
AU - Taniguchi, Koki
PY - 2008/10/1
Y1 - 2008/10/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=52649140036&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=52649140036&partnerID=8YFLogxK
U2 - 10.1128/JVI.01051-08
DO - 10.1128/JVI.01051-08
M3 - Article
C2 - 18653460
AN - SCOPUS:52649140036
VL - 82
SP - 9765
EP - 9769
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 19
ER -