Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone.

Abstract : Nipah virus (NiV) is a highly pathogenic emergent paramyxovirus causing deadly encephalitis in humans. Its replication requires a constant supply of unassembled nucleoprotein (N(0)) in complex with its viral chaperone, the phosphoprotein (P). To elucidate the chaperone function of P, we reconstituted NiV the N(0)-P core complex and determined its crystal structure. The binding of the N-terminal region of P blocks the polymerization of N by interfering with subdomain exchange between N protomers and keeps N(0) in an open conformation, ready to grasp an RNA molecule. We found that a peptide derived from the N-binding region of P protects cells against viral infection and demonstrated by structure-based mutagenesis that this peptide acts by inhibiting N(0)-P formation. These results provide new insights about the assembly of N along genomic RNA and validate the N(0)-P complex as a target for drug development.
Type de document :
Article dans une revue
Nature Structural and Molecular Biology, Nature Publishing Group, 2014, pp.754-9
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http://hal.univ-grenoble-alpes.fr/hal-01101596
Contributeur : Frank Thomas <>
Soumis le : vendredi 9 janvier 2015 - 10:10:41
Dernière modification le : lundi 25 juin 2018 - 11:58:03

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  • HAL Id : hal-01101596, version 1
  • PUBMED : 25108352

Citation

Filip Yabukarski, Philip Lawrence, Nicolas Tarbouriech, Jean-Marie Bourhis, Elise Delaforge, et al.. Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone.. Nature Structural and Molecular Biology, Nature Publishing Group, 2014, pp.754-9. 〈hal-01101596〉

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