Hélène Raux
Université Paris-Saclay
5 Papers
10 Citations
Hélène Raux is an academic researcher from Université Paris-Saclay. The author has contributed to research in topics: Lipid bilayer fusion & Vesicular stomatitis virus. The author has an hindex of 4, co-authored 5 publications. Previous affiliations of Hélène Raux include University of Paris-Sud.
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Papers
Structural basis for the recognition of LDL-receptor family members by VSV glycoprotein.
TL;DR: Crystal structures of G in complex with two distinct CR domains of LDL-R are presented, identifying structural determinants for VSV infectivity in mammalian and insect cells and suggest that VSV G has specifically evolved to interact with receptor CR domains.
Characterization of the Interaction between the Matrix Protein of Vesicular Stomatitis Virus and the Immunoproteasome Subunit LMP2
TL;DR: The association of vesicular stomatitis virus (VSV) matrix protein (M) with LMP2, one of the immunoproteasome-specific catalytic subunits, is suggested to have evolved a mechanism that allows infected cells to escape detection and elimination by the immune system.
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Identification of a pH-Sensitive Switch in VSV-G and a Crystal Structure of the G Pre-fusion State Highlight the VSV-G Structural Transition Pathway.
Frauke Beilstein,Abbas Abou Hamdan,Hélène Raux,Laura Belot,Malika Ouldali,Aurélie A. Albertini,Yves Gaudin +6 more
TL;DR: It is demonstrated that residues H389 and D280, facing each other in the six-helix bundle of the post-fusion state, and more prominently H407, located at the interface between the C-terminal part of the ectodomain and the fusion domain, are crucial for fusion.
Structure of the Low pH Conformation of Chandipura Virus G Reveals Important Features in the Evolution of the Vesiculovirus Glycoprotein
Eduard Baquero,Aurélie A. Albertini,Hélène Raux,Linda Buonocore,John K. Rose,Stéphane Bressanelli,Yves Gaudin +6 more
TL;DR: Local differences indicate that CHAV has evolved alternate structural solutions in hinge regions between PH and fusion domains but also distinct pH sensitive switches, and highlights the remarkable plasticity of G in terms of local structures.
Structural intermediates in the fusion-associated transition of vesiculovirus glycoprotein.
Eduard Baquero,Aurélie A. Albertini,Hélène Raux,Abbas Abou-Hamdan,Elisabetta Boeri-Erba,Malika Ouldali,Linda Buonocore,John K. Rose,Jean Lepault,Stéphane Bressanelli,Yves Gaudin +10 more
TL;DR: The range of G structural changes is revealed and it is suggested that G monomers can re‐associate, through antiparallel interactions between fusion domains, into dimers that play a role at some early stage of the fusion process.