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Dynamique d'assemblage de la capside des norovirus

Abstract : Noroviruses are the leading cause of acute viral gastroenteritis in humans and animas. Each year, they are responsible for 220 000 deaths and cost close to 65 billion euros.It’s a small single-stranded positive sense RNA virus. The capsid is composed of 90 dimers of a single structural protein (VP1) which consists of two main domains: the protruding domain (P) exposed to the biological environment, and the shell domain (S) which is the assembly module of the capsid .Using computational approaches such as homology modelling, simulated annealing, molecular dynamic simulations in all atoms and coarse grains systems, we are looking to determine the molecular basis of norovirus capsid assembly.Our results on the capsid assembly brick (dimer of VP1) indicate the presence of an asymmetry that can have a role in the first stages of self-assembly, which we confirm experimentally by SAXS.Our results on larger VP1 assemblages (pentamer and hexamer of dimers) also reveal a disruption of symmetry in the pentamer of dimer, leaving a preferred position for the insertion of an additional dimer and promoting anisotropic growth.We complete and specify the assembly model originally published by our team in 2013.
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Submitted on : Monday, April 23, 2018 - 11:40:22 AM
Last modification on : Saturday, September 12, 2020 - 3:14:54 AM
Long-term archiving on: : Tuesday, September 18, 2018 - 10:16:07 PM


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  • HAL Id : tel-01773889, version 1


Thibault Tubiana. Dynamique d'assemblage de la capside des norovirus. Biologie structurale [q-bio.BM]. Université Paris-Saclay, 2017. Français. ⟨NNT : 2017SACLS307⟩. ⟨tel-01773889⟩



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