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© Valérie Choumet
Mosquitoes were orally infected with the chikungunya virus. Midguts were dissected at day 5 post-infection, fixed and permeabilised. Virus is shown in red (anti-E2 protein, cyanine 3), the actin network in green (phalloidin 548) and nuclei in blue (DAPI).
Publication : The Journal of biological chemistry

A structural basis for the inhibition of the NS5 dengue virus mRNA 2′-O-methyltransferase domain by ribavirin 5′-triphosphate

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 19 May 2004

Benarroch D, Egloff MP, Mulard L, Guerreiro C, Romette JL, Canard B

Link to Pubmed [PMID] – 15152003

J. Biol. Chem. 2004 Aug;279(34):35638-43

Ribavirin is one of the few nucleoside analogues currently used in the clinic to treat RNA virus infections, but its mechanism of action remains poorly understood at the molecular level. Here, we show that ribavirin 5′-triphosphate inhibits the activity of the dengue virus 2′-O-methyltransferase NS5 domain (NS5MTase(DV)). Along with several other guanosine 5′-triphosphate analogues such as acyclovir, 5-ethynyl-1-beta-d-ribofuranosylimidazole-4-carboxamide (EICAR), and a series of ribose-modified ribavirin analogues, ribavirin 5′-triphosphate competes with GTP to bind to NS5MTase(DV). A structural view of the binding of ribavirin 5′-triphosphate to this enzyme was obtained by determining the crystal structure of a ternary complex consisting of NS5MTase(DV), ribavirin 5′-triphosphate, and S-adenosyl-l-homocysteine at a resolution of 2.6 A. These detailed atomic interactions provide the first structural insights into the inhibition of a viral enzyme by ribavirin 5′-triphosphate, as well as the basis for rational drug design of antiviral agents with improved specificity against the emerging flaviviruses.

http://www.ncbi.nlm.nih.gov/pubmed/15152003