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.
journal_name
J Viroljournal_title
Journal of virologyauthors
Sasaki J,Taniguchi Kdoi
10.1128/JVI.01051-08subject
Has Abstractpub_date
2008-10-01 00:00:00pages
9765-9issue
19eissn
0022-538Xissn
1098-5514pii
JVI.01051-08journal_volume
82pub_type
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journal_title:Journal of virology
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pub_type: 杂志文章
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