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Literature summary for 2.7.7.48 extracted from

  • Van Slyke, G.A.; Ciota, A.T.; Willsey, G.G.; Jaeger, J.; Shi, P.Y.; Kramer, L.D.
    Point mutations in the West Nile virus (Flaviviridae; Flavivirus) RNA-dependent RNA polymerase alter viral fitness in a host-dependent manner in vitro and in vivo (2012), Virology, 427, 18-24.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
A365N mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and particularly alters growth and RNA replication kinetics West Nile virus
T363N mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics West Nile virus
T537I mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics West Nile virus

Organism

Organism UniProt Comment Textmining
West Nile virus Q8JU43 viral polyprotein
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West Nile virus 3356 Q8JU43 viral polyprotein
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Synonyms

Synonyms Comment Organism
NS5 RdRp
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West Nile virus