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Science 16 November 1984:
Vol. 226. no. 4676, pp. 847 - 848
DOI: 10.1126/science.6494916
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Articles

Science, Vol 226, Issue 4676, 847-848
Copyright © 1984 by American Association for the Advancement of Science

articles

Amino acid sequence similarity between rabies virus glycoprotein and snake venom curaremimetic neurotoxins

TL Lentz, PT Wilson, E Hawrot, and DW Speicher

Evidence was presented earlier that a host-cell receptor for the highly neurotropic rabies virus might be the acetylcholine receptor. The amino acid sequence of the glycoprotein of rabies virus was compared by computer analysis with that of snake venom curaremimetic neurotoxins, potent ligands of the acetylcholine receptor. A statistically significant sequence relation was found between a segment of the rabies glycoprotein and the entire sequence of long neurotoxins. The greatest identity occurs with residues considered most important in neurotoxicity, including those interacting with the acetylcholine binding site of the acetylcholine receptor. Because of the similarity between the glycoprotein and the receptor-binding region of the neurotoxins, this region of the viral glycoprotein may function as a recognition site for the acetylcholine receptor. Direct binding of the rabies virus glycoprotein to the acetylcholine receptor could contribute to the neurotropism of this virus.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
MOLECULAR EPIDEMIOLOGY OF TERRESTRIAL RABIES IN THE FORMER SOVIET UNION.
I. V. Kuzmin, A. D. Botvinkin, L. M. McElhinney, J. S. Smith, L. A. Orciari, G. J. Hughes, A. R. Fooks, and C. E. Rupprecht (2004)
J. Wildl. Dis. 40, 617-631
   Abstract »    Full Text »    PDF »
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.
C. Langevin and C. Tuffereau (2002)
J. Virol. 76, 10756-10765
   Abstract »    Full Text »    PDF »
Rabies Virus Glycoprotein (RVG) Is a Trimeric Ligand for the N-terminal Cysteine-rich Domain of the Mammalian p75 Neurotrophin Receptor.
C. Langevin, H. Jaaro, S. Bressanelli, M. Fainzilber, and C. Tuffereau (2002)
J. Biol. Chem. 277, 37655-37662
   Abstract »    Full Text »    PDF »
Interaction of lyssaviruses with the low-affinity nerve-growth factor receptor p75NTR.
C. Tuffereau, E. Desmezieres, J. Benejean, C. Jallet, A. Flamand, N. Tordo, and P. Perrin (2001)
J. Gen. Virol. 82, 2861-2867
   Abstract »    Full Text »    PDF »
Rescue of Rabies Virus from Cloned cDNA and Identification of the Pathogenicity-Related Gene: Glycoprotein Gene Is Associated with Virulence for Adult Mice.
N. Ito, M. Takayama, K. Yamada, M. Sugiyama, and N. Minamoto (2001)
J. Virol. 75, 9121-9128
   Abstract »    Full Text »    PDF »
Host Switching in Lyssavirus History from the Chiroptera to the Carnivora Orders.
H. Badrane and N. Tordo (2001)
J. Virol. 75, 8096-8104
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Evidence of Two Lyssavirus Phylogroups with Distinct Pathogenicity and Immunogenicity.
H. Badrane, C. Bahloul, P. Perrin, and N. Tordo (2001)
J. Virol. 75, 3268-3276
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De Novo Design of Peptides Targeted to the EF Hands of Calmodulin.
M. Villain, P. L. Jackson, M. K. Manion, W.-J. Dong, Z. Su, G. Fassina, T. M. Johnson, T. T. Sakai, N. R. Krishna, and J. E. Blalock (2000)
J. Biol. Chem. 275, 2676-2685
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Neuronal Cell Surface Molecules Mediate Specific Binding to Rabies Virus Glycoprotein Expressed by a Recombinant Baculovirus on the Surfaces of Lepidopteran Cells.
C. Tuffereau, J. Benejean, A.-M. R. Alfonso, A. Flamand, and M. C. Fishman (1998)
J. Virol. 72, 1085-1091
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Molecular Mimicry Between the Rabies Virus Glycoprotein and Human Immunodeficiency Virus-1 GP120: Cross-Reacting Antibodies Induced by Rabies Vaccination.
L. Bracci, S. K. Ballas, A. Spreafico, and P. Neri (1997)
Blood 90, 3623-3628
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Amino acid homology between the encephalitogenic site of myelin basic protein and virus: mechanism for autoimmunity.
R. Fujinami and M. Oldstone (1985)
Science 230, 1043-1045
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