Aichi virus 2A protein is involved in viral RNA replication.
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.
Sasaki
Jun
J
Department of Virology and Parasitology, Fujita Health University School of Medicine, Toyoake, Aichi 470-1192, Japan. jsasaki@fujita-hu.ac.jp
Taniguchi
Koki
K
D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D002474:Cell-Free System; D002522:Chlorocebus aethiops; D018076:DNA, Complementary / Q000378:metabolism; D015967:Gene Expression Regulation, Viral; D052699:Kobuvirus / Q000235:genetics*; D008954:Models, Biological; D008957:Models, Genetic; D009154:Mutation; D014176:Protein Biosynthesis; D012367:RNA, Viral / Q000235:genetics*; D014709:Vero Cells; D014779:Virus Replication
D000596:Amino Acids; D018076:DNA, Complementary; D012367:RNA, Viral