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Scientific Fields
Diseases
Organisms
Applications
Technique
Date
21
Mar 2017
Time
14:00:00
28 Rue du Dr Roux, Paris, France
Address
Building: Bâtiment Lwoff Room: Salle 014-015 - RDC
Location
2017-03-21 14:00:00 2017-03-21 15:30:00 Europe/London Aurélie Albertini seminar Séminaire du Département de Biologie Structurale & Chimie Mardi 21 mars 2017 à 14h00 Salle 014-015 – RDC bâtiment Lwoff Aurélie ALBERTINI Département de Virologie, Institut de Biologie Intégrative de la Cellule (I2BC), Université […] 28 Rue du Dr Roux, Paris, France Célia Caillet-Saguy celia.caillet-saguy@pasteur.fr

About

Séminaire du Département de Biologie Structurale & Chimie

Mardi 21 mars 2017 à 14h00

Salle 014-015 – RDC bâtiment Lwoff

Aurélie ALBERTINI

Département de Virologie, Institut de Biologie Intégrative de la Cellule (I2BC),

Université Paris-Saclay, CEA, CNRS, Université Paris-Sud

Structural basis of low density lipoprotein receptor recognition by VSV glycoprotein.

 Jovan Nikolic, Laura Belot, Pierre Legrand, Yves Gaudin & Aurélie Albertini Vesicular stomatitis virus (VSV) is an oncolytic rhabdovirus and its glycoprotein G is widely used to pseudotype other viruses for gene therapy. G mediates both virus attachment to its receptor and the fusion of the viral envelope with the endosomal membrane. Recently, it has been shown that VSV engages the low density lipoprotein receptor (LDL-R) to gain entry into host cells. To elucidate the complex interplay between the virus and its receptor, we combined several techniques to understand molecular basis of the interaction between G and the LDL-R. In vitro, we found that both VSV viral particles and G ectodomain can bind two separate cysteine rich domains (CR2 and CR3) of the LDL-R and only when G is in its pre-fusion conformation (i.e. at high pH). We reported also two crystalline structures of VSV G in complex with two distinct cysteinerich domains (CR2 and CR3) of the LDL-R, which reveal that the binding sites of CR2 and CR3 on G are identical. Furthermore, although VSV can use alternative receptors,  the mutations of basic residues, which are keys for interaction with LDL-R CR domains, abolish VSV infectivity. Our data indicate that the only receptors of VSV in mammalian cells are members of the LDL-R family and that VSV G has specifically evolved to interact with their CR domains. This provides structural insights on the interaction between VSV G and host cell receptors and basis for design of recombinant viruses with an altered tropism.

Contacts : Célia Caillet-Saguy

Unité de RMN des Biomolécules

celia.caillet-saguy@pasteur.fr

Location

Building: Bâtiment Lwoff
Room: Salle 014-015 - RDC
Address: 28 Rue du Dr Roux, Paris, France