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INRA
24, chemin de Borde Rouge –Auzeville – CS52627
31326 Castanet Tolosan CEDEX - France

Dernière mise à jour : Mai 2018

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Unité de Virologie et Immunologie Moléculaires

Specific projects

RSV RNA replication and transcription

The group specializes in structural and functional analysis of some of the key RSV proteins required for replication. One of the main projects focuses on viral RNA replication and transcription, specifically the structural and functional analysis of Ribonucleoprotein (RNP) complex. Our team has built all the necessary tools to track the viral proteins within infected cells and on replicon system. We have set up a reverse genetics system allowing targeted modifications the viral genome and engineered fluorescent and luminescent RSV. We have also developed protocols to produce recombinant proteins for studying their structure and function in vitro, especially the different components of the RNP complex (M2-1, Phospho and Nucleo proteins). In collaboration with crystallography lab in Pasteur Institute, we were able to purify the N-P complex and to resolve the atomic structure of the N protein assembled as rings contain either 10 or 11 N protomers and RNA. Our current focus is on the Large polymerase (L) structure, M2-1–P and N–P interactions and RNA encapsidation by N.

RSV-host interactions

We have previously used different protein-protein interaction screens to identify host factors binding to the RSV M and N protein. Our current goal is to characterize virus-cell interactions at the molecular level and to define molecular targets for the development of new antivirals. Host factors interacting with the N protein were identified using IP and Mass Spectrometry. Specific host factors interacting with M were identified using a protein microfluidics screen. We are now focusing on host factors interacting with M during assembly and budding. Other targets include nuclear host proteins and their possible link to cellular transcription regulation during RSV infection.

RSV assembly and budding

Other project focuses on RSV assembly and budding, combining biochemical, functional and structural analysis of viral and cellular protein-protein interactions. Our interest is on host factors as well as on specific viral protein-protein interactions required during RSV assembly. The virus assembles and buds through the plasma membrane, forming elongated membrane filaments, but details of how this happens remain obscure.  The minimal RSV viral protein requirement for filament formation and budding of virus-like particles (VLPs) are F, N, P, and M protein. M, a key structural protein, directs assembly and budding on the plasma membrane, presumably by interacting with the cytoplasmic tails of the glycoproteins and with the RNP complex in the cytoplasm. We have previously shown that M is biologically active as a dimer and that the switch from M dimers to higher oligomers triggers viral filament assembly and virus production. Our main current focus is on host factors interacting with M during assembly and on M-N viral interaction.