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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.


Journal article


J Virol

Publication Date





5017 - 5020


Amino Acid Substitution, Animals, Cell Line, DNA-Directed RNA Polymerases, Defective Viruses, Humans, Influenza A virus, RNA Interference, RNA Replicase, RNA, Viral, Viral Plaque Assay, Viral Proteins, Virulence