Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

J Virol

Publication Date

04/2003

Volume

77

Pages

5017 - 5020

Keywords

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