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 Badrane, H.
Right arrow Articles by Tordo, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Badrane, H.
Right arrow Articles by Tordo, N.

 Previous Article  |  Next Article 

Journal of Virology, April 2001, p. 3268-3276, Vol. 75, No. 7
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.7.3268-3276.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Evidence of Two Lyssavirus Phylogroups with Distinct Pathogenicity and Immunogenicity

Hassan Badrane, Chokri Bahloul, Pierre Perrin, and Noël Tordo*

Laboratoire des Lyssavirus, Department of Virology, Institut Pasteur, Paris, France

Received 1 September 2000/Accepted 4 January 2001

The genetic diversity of representative members of the Lyssavirus genus (rabies and rabies-related viruses) was evaluated using the gene encoding the transmembrane glycoprotein involved in the virus-host interaction, immunogenicity, and pathogenicity. Phylogenetic analysis distinguished seven genotypes, which could be divided into two major phylogroups having the highest bootstrap values. Phylogroup I comprises the worldwide genotype 1 (classic Rabies virus), the European bat lyssavirus (EBL) genotypes 5 (EBL1) and 6 (EBL2), the African genotype 4 (Duvenhage virus), and the Australian bat lyssavirus genotype 7. Phylogroup II comprises the divergent African genotypes 2 (Lagos bat virus) and 3 (Mokola virus). We studied immunogenic and pathogenic properties to investigate the biological significance of this phylogenetic grouping. Viruses from phylogroup I (Rabies virus and EBL1) were found to be pathogenic for mice when injected by the intracerebral or the intramuscular route, whereas viruses from phylogroup II (Mokola and Lagos bat viruses) were only pathogenic by the intracerebral route. We showed that the glycoprotein R333 residue essential for virulence was naturally replaced by a D333 in the phylogroup II viruses, likely resulting in their attenuated pathogenicity. Moreover, cross-neutralization distinguished the same phylogroups. Within each phylogroup, the amino acid sequence of the glycoprotein ectodomain was at least 74% identical, and antiglycoprotein virus-neutralizing antibodies displayed cross-neutralization. Between phylogroups, the identity was less than 64.5% and the cross-neutralization was absent, explaining why the classical rabies vaccines (phylogroup I) cannot protect against lyssaviruses from phylogroup II. Our tree-axial analysis divided lyssaviruses into two phylogroups that more closely reflect their biological characteristics than previous serotypes and genotypes.

* Corresponding author. Mailing address: Laboratoire des Lyssavirus, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France. Phone: (33) 1-40613134. Fax: (33) 1-40613256. E-mail: ntordo{at}pasteur.fr.

Journal of Virology, April 2001, p. 3268-3276, Vol. 75, No. 7
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.7.3268-3276.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Castel, G., Chteoui, M., Caignard, G., Prehaud, C., Mehouas, S., Real, E., Jallet, C., Jacob, Y., Ruigrok, R. W. H., Tordo, N. (2009). Peptides That Mimic the Amino-Terminal End of the Rabies Virus Phosphoprotein Have Antiviral Activity. J. Virol. 83: 10808-10820 [Abstract] [Full Text]  
  • Wright, E., Temperton, N. J., Marston, D. A., McElhinney, L. M., Fooks, A. R., Weiss, R. A. (2008). Investigating antibody neutralization of lyssaviruses using lentiviral pseudotypes: a cross-species comparison. J. Gen. Virol. 89: 2204-2213 [Abstract] [Full Text]  
  • Gholami, A., Kassis, R., Real, E., Delmas, O., Guadagnini, S., Larrous, F., Obach, D., Prevost, M.-C., Jacob, Y., Bourhy, H. (2008). Mitochondrial Dysfunction in Lyssavirus-Induced Apoptosis. J. Virol. 82: 4774-4784 [Abstract] [Full Text]  
  • Kuzmin, I. V., Niezgoda, M., Franka, R., Agwanda, B., Markotter, W., Beagley, J. C., Urazova, O. Y., Breiman, R. F., Rupprecht, C. E. (2008). Lagos Bat Virus in Kenya. J. Clin. Microbiol. 46: 1451-1461 [Abstract] [Full Text]  
  • Tuffereau, C., Schmidt, K., Langevin, C., Lafay, F., Dechant, G., Koltzenburg, M. (2007). The Rabies Virus Glycoprotein Receptor p75NTR Is Not Essential for Rabies Virus Infection. J. Virol. 81: 13622-13630 [Abstract] [Full Text]  
  • Marston, D. A., McElhinney, L. M., Johnson, N., Muller, T., Conzelmann, K. K., Tordo, N., Fooks, A. R. (2007). Comparative analysis of the full genome sequence of European bat lyssavirus type 1 and type 2 with other lyssaviruses and evidence for a conserved transcription termination and polyadenylation motif in the G-L 3' non-translated region. J. Gen. Virol. 88: 1302-1314 [Abstract] [Full Text]  
  • Nagarajan, T., Mohanasubramanian, B., Seshagiri, E. V., Nagendrakumar, S. B., Saseendranath, M. R., Satyanarayana, M. L., Thiagarajan, D., Rangarajan, P. N., Srinivasan, V. A. (2006). Molecular epidemiology of rabies virus isolates in India.. J. Clin. Microbiol. 44: 3218-3224 [Abstract] [Full Text]  
  • Johnson, N., McKimmie, C. S., Mansfield, K. L., Wakeley, P. R., Brookes, S. M., Fazakerley, J. K., Fooks, A. R. (2006). Lyssavirus infection activates interferon gene expression in the brain. J. Gen. Virol. 87: 2663-2667 [Abstract] [Full Text]  
  • Johnson, N., Phillpotts, R., Fooks, A. R. (2006). Airborne transmission of lyssaviruses. J Med Microbiol 55: 785-790 [Abstract] [Full Text]  
  • Davis, P. L., Holmes, E. C., Larrous, F., Van der Poel, W. H. M., Tjornehoj, K., Alonso, W. J., Bourhy, H. (2005). Phylogeography, Population Dynamics, and Molecular Evolution of European Bat Lyssaviruses. J. Virol. 79: 10487-10497 [Abstract] [Full Text]  
  • Wakeley, P. R., Johnson, N., McElhinney, L. M., Marston, D., Sawyer, J., Fooks, A. R. (2005). Development of a Real-Time, TaqMan Reverse Transcription-PCR Assay for Detection and Differentiation of Lyssavirus Genotypes 1, 5, and 6. J. Clin. Microbiol. 43: 2786-2792 [Abstract] [Full Text]  
  • Mansfield, K. L., Johnson, N., Fooks, A. R. (2004). Identification of a conserved linear epitope at the N terminus of the rabies virus glycoprotein. J. Gen. Virol. 85: 3279-3283 [Abstract] [Full Text]  
  • Kuzmin, I. V., Botvinkin, A. D., McElhinney, L. M., Smith, J. S., Orciari, L. A., Hughes, G. J., Fooks, A. R., Rupprecht, C. E. (2004). MOLECULAR EPIDEMIOLOGY OF TERRESTRIAL RABIES IN THE FORMER SOVIET UNION. J Wildl Dis 40: 617-631 [Abstract] [Full Text]  
  • Kassis, R., Larrous, F., Estaquier, J., Bourhy, H. (2004). Lyssavirus Matrix Protein Induces Apoptosis by a TRAIL-Dependent Mechanism Involving Caspase-8 Activation. J. Virol. 78: 6543-6555 [Abstract] [Full Text]  
  • Jackson, A. P., Charleston, M. A. (2004). A Cophylogenetic Perspective of RNA-Virus Evolution. Mol Biol Evol 21: 45-57 [Abstract] [Full Text]  
  • Nadin-Davis, S. A., Sheen, M., Wandeler, A. I. (2003). Use of Discriminatory Probes for Strain Typing of Formalin-Fixed, Rabies Virus-Infected Tissues by In Situ Hybridization. J. Clin. Microbiol. 41: 4343-4352 [Abstract] [Full Text]  
  • Guyatt, K. J., Twin, J., Davis, P., Holmes, E. C., Smith, G. A., Smith, I. L., Mackenzie, J. S., Young, P. L. (2003). A molecular epidemiological study of Australian bat lyssavirus. J. Gen. Virol. 84: 485-496 [Abstract] [Full Text]  
  • Johnson, N., Mansfield, K. L., Fooks, A. R. (2002). Canine vaccine recipients recognize an immunodominant region of the rabies virus glycoprotein. J. Gen. Virol. 83: 2663-2669 [Abstract] [Full Text]  
  • Langevin, C., Tuffereau, C. (2002). Mutations Conferring Resistance to Neutralization by a Soluble Form of the Neurotrophin Receptor (p75NTR) Map outside of the Known Antigenic Sites of the Rabies Virus Glycoprotein. J. Virol. 76: 10756-10765 [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]  
  • Jacob, Y., Real, E., Tordo, N. (2001). Functional Interaction Map of Lyssavirus Phosphoprotein: Identification of the Minimal Transcription Domains. J. Virol. 75: 9613-9622 [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]  


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