Infection par le virus West Nile chez l'homme

作者: Marion C. Lanteri , Philip J. Norris , Michael S. Diamond , Michael P. Busch

DOI: 10.1051/MEDSCI/2011274013

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摘要: Marion C. Lanteri, Michael S. Diamond, Philip J. Norris, P. Busch > Depuis son emergence en 1999, le virus West Nile (WNV) est devenu la principale cause d’encephalite arbovirale aux Etats-Unis. L’infection souvent asymptomatique mais, lorsqu’elle cliniquement apparente, les symptomes vont d’un symptome grippal a des desordres neurologiques plus graves pouvant parfois entrainer mort. Les etudes cours, menees parallele chez l’animal et l’homme, cherchent comprendre dynamique hote-virus mecanismes conduisant au developpement de dans approximativement 1 % cas. La comparaison individus asymptomatiques symptomatiques l’utilisation donnees disponibles pour d’autres Flavivirus ont ameliore nos connaissances laissent esperer solutions therapeutiques actuellement absentes mesures prophylactiques. C’est synthese ces que nous presentons cette seconde partie. < Le recepteur cellulaire utilise par WNV surface cellules cibles n’a pas encore ete caracterise apres s’etre attache cellulaire, internalise cytoplasme un mecanisme qui fait intervenir clathrine une fusion avec endosomes. A pH acide, l’enveloppe virale fusionne membrane l’endosome, liberant nucleocapside materiel genetique viral cellulaire. machinerie traduit l’ARN dont cadre lecture d’environ 10,7 kb code polyproteine virale. Cette derniere clivee cours d’une etape post-traductionnelle produit trois proteines structure (C capside, prM pre-membrane E enveloppe) suivies sept non structurales (NS1, NS2a, 2b, NS3, NS4a, NS4b NS5), lesquelles participent cycle replication du virus. capside associee nucleocapside, sert proteine chaperonne durant maturation virions empeche lors secretion. L’enveloppe permet liaison l’endosome. Parmi roles potentiels structurales, NS1 impliquee l’ARN, l’echappement [2] virulence [3]. NS3 participe virales possede activite helicase ARN nucleoside triphosphatase. NS5 proprietes enzymatiques importantes : c’est polymerase ARN-dependante methyltransferase catalyse methylations N7 and 2’-0 l’extremite 5’ former Cap1 [4]. De plus, antagoniste voie Blood Systems Research Institute, UCSF Department of Laboratory Medicine, 270 Masonic avenue, 94118 San Francisco, mlanteri@bloodsystems.org

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