This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tuffereau, C.
Right arrow Articles by Fishman, M. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tuffereau, C.
Right arrow Articles by Fishman, M. C.

 Previous Article  |  Next Article 

J Virol, February 1998, p. 1085-1091, Vol. 72, No. 2
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Neuronal Cell Surface Molecules Mediate Specific Binding to Rabies Virus Glycoprotein Expressed by a Recombinant Baculovirus on the Surfaces of Lepidopteran Cells

Christine Tuffereau,1,* Jacqueline Benejean,1 Anne-Marie Roque Alfonso,1 Anne Flamand,1 and Mark C. Fishman2

Laboratoire de Génétique des Virus, CNRS, 91198 Gif sur Yvette Cédex, France,1 and Developmental Biology Laboratory, CVRC, Massachusetts General Hospital, Charlestown, Massachusetts 021292

Received 21 August 1997/Accepted 21 October 1997

The existence of specific rabies virus (RV) glycoprotein (G) binding sites on the surfaces of neuroblastoma cells is demonstrated. Spodoptera frugiperda (Sf21) cells expressing G of the RV strain CVS (Gcvs-Sf21 cells) bind specifically to neuroblastoma cells of different species but not to any other cell type (fibroblast, myoblast, epithelial, or glioma). Attachment to mouse neuroblastoma NG108-15 cells is abolished by previous treatment of Gcvs-Sf21 cells with anti-G antibody. Substitutions for lysine at position 330 and for arginine at position 333 in RV G greatly reduce interaction between Gcvs-Sf21 cells and NG108-15 cells. These data are consistent with in vivo results: an avirulent RV mutant bearing the same double mutation is not able to infect sensory neurons or motoneurons (P. Coulon, J.-P. Ternaux, A. Flamand, and C. Tuffereau, J. Virol. 72:273-278, 1998) after intramuscular inoculation into a mouse. Furthermore, infection of NG108-15 cells by RV but not by vesicular stomatitis virus leads to a reduction of the number of binding sites at the neuronal-cell surface. Our data strongly suggest that these specific attachment sites on neuroblastoma cells represent a neuronal receptor(s) used by RV to infect certain types of neurons in vivo.

* Corresponding author. Mailing address: Laboratoire de Génétique des Virus, Bat 14C, Centre National de la Recherche Scientifique, 91198 Gif sur Yvette Cédex, France. Phone: 33 1 69 82 38 41. Fax: 33 1 69 82 43 08. E-mail: ctuffer{at}gv.cnrs-gif.fr.




This article has been cited by other articles:

  • Sissoeff, L., Mousli, M., England, P., Tuffereau, C. (2005). Stable trimerization of recombinant rabies virus glycoprotein ectodomain is required for interaction with the p75NTR receptor. J. Gen. Virol. 86: 2543-2552 [Abstract] [Full Text]  
  • Langevin, C., Jaaro, H., Bressanelli, S., Fainzilber, M., Tuffereau, C. (2002). Rabies Virus Glycoprotein (RVG) Is a Trimeric Ligand for the N-terminal Cysteine-rich Domain of the Mammalian p75 Neurotrophin Receptor. J. Biol. Chem. 277: 37655-37662 [Abstract] [Full Text]  
  • Tuffereau, C., Desmezieres, E., Benejean, J., Jallet, C., Flamand, A., Tordo, N., Perrin, P. (2001). Interaction of lyssaviruses with the low-affinity nerve-growth factor receptor p75NTR. J. Gen. Virol. 82: 2861-2867 [Abstract] [Full Text]  
  • Mebatsion, T. (2001). Extensive Attenuation of Rabies Virus by Simultaneously Modifying the Dynein Light Chain Binding Site in the P Protein and Replacing Arg333 in the G Protein. J. Virol. 75: 11496-11502 [Abstract] [Full Text]  
  • Badrane, H., Tordo, N. (2001). Host Switching in Lyssavirus History from the Chiroptera to the Carnivora Orders. J. Virol. 75: 8096-8104 [Abstract] [Full Text]  
  • Badrane, H., Bahloul, C., Perrin, P., Tordo, N. (2001). Evidence of Two Lyssavirus Phylogroups with Distinct Pathogenicity and Immunogenicity. J. Virol. 75: 3268-3276 [Abstract] [Full Text]  
  • Jacob, Y., Badrane, H., Ceccaldi, P.-E., Tordo, N. (2000). Cytoplasmic Dynein LC8 Interacts with Lyssavirus Phosphoprotein. J. Virol. 74: 10217-10222 [Abstract] [Full Text]  
  • Bourhy, H., Kissi, B., Audry, L., Smreczak, M., Sadkowska-Todys, M., Kulonen, K., Tordo, N., Zmudzinski, J. F., Holmes, E. C. (1999). Ecology and evolution of rabies virus in Europe. J. Gen. Virol. 80: 2545-2557 [Abstract] [Full Text]  
  • Bearzotti, M., Delmas, B., Lamoureux, A., Loustau, A.-M., Chilmonczyk, S., Bremont, M. (1999). Fish Rhabdovirus Cell Entry Is Mediated by Fibronectin. J. Virol. 73: 7703-7709 [Abstract] [Full Text]  
  • Kissi, B., Badrane, H., Audry, L., Lavenu, A., Tordo, N., Brahimi, M., Bourhy, H. (1999). Dynamics of rabies virus quasispecies during serial passages in heterologous hosts. J. Gen. Virol. 80: 2041-2050 [Abstract] [Full Text]  
  • Jallet, C., Jacob, Y., Bahloul, C., Drings, A., Desmezieres, E., Tordo, N., Perrin, P. (1999). Chimeric Lyssavirus Glycoproteins with Increased Immunological Potential. J. Virol. 73: 225-233 [Abstract] [Full Text]  
  • Morimoto, K., Hooper, D. C., Spitsin, S., Koprowski, H., Dietzschold, B. (1999). Pathogenicity of Different Rabies Virus Variants Inversely Correlates with Apoptosis and Rabies Virus Glycoprotein Expression in Infected Primary Neuron Cultures. J. Virol. 73: 510-518 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»