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Caractérisation structurale par RMN des interactions entre protéines du complexe polymérase du virus respiratoire syncytial et des protéines partenaires cellulaires

Abstract : Human respiratory syncytial virus (hRSV) is the main pathogen responsible for bronchiolitis. The RNA polymerase complex (RdRp) of hRSV, necessary for the replication of its genome, is composed at least of the catalytic subunit (L), its main cofactor phosphoprotein (P) and nucleoprotein (N), which encapsidates the viral genome. At the heart of my doctoral project was the dynamic and structural study of domains of the proteins N and P of the hRSV as well as of their interactions with several cellular proteins, mainly by nuclear magnetic resonance.Firstly, I studied a potential interaction between 2 domains belonging to the N protein and to the Tax1BP1 cellular protein involved notably in regulation of autophagy. Secondly, I undertook a structural and dynamic study of isolated hRSV-P in order to determine transient contacts within the protein and to obtain the three-dimensional structure of the P oligomerization domain. Last, I participated in the characterization of the interaction between the hRSV-P protein and the hRSV transcription cofactor hRSV-M2-1, and between hRSV P and the cellular phosphatase PP1α to map the contact regions.
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Christophe Cardone. Caractérisation structurale par RMN des interactions entre protéines du complexe polymérase du virus respiratoire syncytial et des protéines partenaires cellulaires. Biologie structurale [q-bio.BM]. Université Paris-Saclay, 2019. Français. ⟨NNT : 2019SACLS586⟩. ⟨tel-02462886⟩

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