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Originally published In Press as doi:10.1074/jbc.M201374200 on August 5, 2002

J. Biol. Chem., Vol. 277, Issue 40, 37655-37662, October 4, 2002
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Rabies Virus Glycoprotein (RVG) Is a Trimeric Ligand for the N-terminal Cysteine-rich Domain of the Mammalian p75 Neurotrophin Receptor*

Christelle LangevinDagger §, Hanna Jaaro, Stéphane BressanelliDagger , Mike Fainzilber||, and Christine TuffereauDagger **

From the Dagger  Laboratoire de Virologie Moléculaire et Structurale, Centre National de la Recherche Scientifique-Institut National de la Recherche Agronomique, 91198 Gif-sur-Yvette, France and the  Laboratory of Molecular Neurobiology, Deptartment of Biological Chemistry, Weizmann Institute, 76100 Rehovot, Israel

Rabies virus glycoprotein (RVG) is a trimeric and surface-exposed viral coat protein that has been shown to interact with the murine p75 neurotrophin receptor. We have investigated binding of RVG to p75 and describe several features that distinguish the p75-RVG interaction from conventional neurotrophin binding to p75. RVG binds mammalian but not avian p75 and does not bind to any of the Trk neurotrophin receptors. The mammalian p75 specificity of RVG binding may partly explain the phyletic specificity of rabies infection. Radioiodinated nerve growth factor (NGF) and RVG both bind to rat p75 but do not compete with each other's binding site. Although neurotrophins bind to the second and third cysteine-rich domains (CRD) of p75, RVG specifically interacts with high affinity (Kd 30-35 pM) with the first CRD (CRD1). Substitution of Gln33 in p75-CRD1 by Glu completely abolishes RVG binding. Our data therefore firmly establish RVG as a trimeric high affinity ligand for a non-neurotrophin binding site on p75. Interestingly, the CRD1 in another TNF/NGF family receptor was recently shown to be involved in the binding of the herpes virus glycoprotein gD, suggesting that the CRD1 of TNF/NGF family members may be a widely used binding domain for viral glycoproteins.

* This work was supported by CNRS funding from the Ministère de l'Education Nationale de la Recherche et de la Technologie and by research Grant QLRT-1999-00573 from the 5th Framework Program of the European Union and the Israel Science Foundation Grant 647/01.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Recipient of a doctoral fellowship from the Ministère de l'Education Nationale et de l'Enseignement Supérieur.

|| The incumbent of the Daniel Koshland Sr. Career Development Chair at the Weizmann Institute.

** To whom correspondence should be addressed: Laboratoire de Virologie Moléculaire et Structurale, UMR 2472 CNRS-INRA, 91198 Gif-sur-Yvette, France. Tel.: 33-1-69-82-38-41; Fax: 33-1-69-82-43-08; E-mail: christine.tuffereau@gv.cnrs-gif.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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