A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase promotes the generation of defective interfering RNAs.
An R638A mutation of the polymerase acidic protein (PA) subunit of the RNA polymerase of influenza A/WSN/33 virus results in severe attenuation of viral growth in cell culture by promoting the synthesis of defective interfering RNAs. We propose that R638A is an "elongation" mutant that destabilizes PA-RNA template interactions during elongation. A C453R mutation in PA can compensate for this defect, suggesting that amino acids C453 and R638 form part of the same domain.
Fodor
Ervin
E
Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
Mingay
Louise J
LJ
Crow
Mandy
M
Deng
Tao
T
Brownlee
George G
GG
D019943:Amino Acid Substitution; D000818:Animals; D002460:Cell Line; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D003673:Defective Viruses / Q000378:metabolism*; D006801:Humans; D009980:Influenza A virus / Q000235:genetics / Q000472:pathogenicity*; D034622:RNA Interference; D012367:RNA, Viral / Q000235:genetics / Q000378:metabolism; D012324:RNA-Dependent RNA Polymerase / Q000235:genetics* / Q000378:metabolism; D010948:Viral Plaque Assay; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism; D014774:Virulence
C061290:PA protein, influenza viruses; D012367:RNA, Viral; D014764:Viral Proteins; D012324:RNA-Dependent RNA Polymerase; D012321:DNA-Directed RNA Polymerases