Synthetic peptides corresponding to sequences of snake venom neurotoxins and rabies virus glycoprotein bind to the nicotinic acetylcholine receptor

1987 ◽  
Vol 2 (4) ◽  
pp. 298-307 ◽  
Author(s):  
Thomas L. Lentz ◽  
Edward Hawrot ◽  
Paul T. Wilson
Keyword(s):  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Rabies Virus ◽  
Snake Venom ◽  
Synthetic Peptides ◽  
Nicotinic Acetylcholine ◽  
Rabies Virus Glycoprotein ◽  
Virus Glycoprotein

scholarly journals Molecular Determinants by Which a Long Chain Toxin from Snake Venom Interacts with the Neuronal α7-Nicotinic Acetylcholine Receptor

2000 ◽  
Vol 275 (38) ◽  
pp. 29594-29601 ◽  
Author(s):  
Stéphanie Antil-Delbeke ◽  
Carole Gaillard ◽  
Toru Tamiya ◽  
Pierre-Jean Corringer ◽  
Jean-Pierre Changeux ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Snake Venom ◽  
Α7 Nicotinic Acetylcholine Receptor ◽  
Nicotinic Acetylcholine ◽  
Molecular Determinants ◽  
Long Chain

Sequence homology between HIV gp120, rabies virus glycoprotein, and snake venom neurotoxins

1990 ◽  
Vol 114 (3-4) ◽  
pp. 265-269 ◽  
Author(s):  
P. Neri ◽  
Luisa Bracci ◽  
M. Rustici ◽  
Annalisa Santucci
Keyword(s):  
Rabies Virus ◽  
Snake Venom ◽  
Sequence Homology ◽  
Rabies Virus Glycoprotein ◽  
Virus Glycoprotein ◽  
Hiv Gp120

Effect of nicotinic acetylcholine receptor alpha 1 (nAChRα1) peptides on rabies virus infection in neuronal cells

Neuropeptides ◽  
2016 ◽  
Vol 57 ◽  
pp. 59-64 ◽  
Author(s):  
Basavaraj Sajjanar ◽  
Shikha Saxena ◽  
Deepika Bisht ◽  
Arvind Kumar Singh ◽  
G.B. Manjunatha Reddy ◽  
...  
Keyword(s):  
Virus Infection ◽  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Rabies Virus ◽  
Neuronal Cells ◽  
Nicotinic Acetylcholine ◽  
Receptor Alpha ◽  
Rabies Virus Infection

scholarly journals Identification of regions involved in the binding of alpha-bungarotoxin to the human alpha7 neuronal nicotinic acetylcholine receptor using synthetic peptides

2003 ◽  
Vol 372 (2) ◽  
pp. 543-554 ◽  
Author(s):  
Martha MARINOU ◽  
Socrates J. TZARTOS
Keyword(s):  
Binding Site ◽  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Binding Sites ◽  
Synthetic Peptides ◽  
Extracellular Domain ◽  
Muscle Type ◽  
Nicotinic Acetylcholine ◽  
Toxin Binding ◽  
Α1 Subunit

The neuronal α7 nicotinic acetylcholine receptor (AChR) binds the neurotoxin α-bungarotoxin (α-Bgt). Fine mapping of the α-Bgt-binding site on the human α7 AChR was performed using synthetic peptides covering the entire extracellular domain of the human α7 subunit (residues 1–206). Screening of these peptides for 125I-α-Bgt binding resulted in the identification of at least two toxin-binding sites, one at residues 186–197, which exhibited the best 125I-α-Bgt binding, and one at residues 159–165, with weak toxin-binding capacity; these correspond, respectively, to loops C and IV of the agonist-binding site. Toxin binding to the α7(186–197) peptide was almost completely inhibited by unlabelled α-Bgt or d-tubocurarine. Alanine substitutions within the sequence 186–198 revealed a predominant contribution of aromatic and negatively charged residues to the binding site. This sequence is homologous to the α-Bgt binding site of the α1 subunit (residues 188–200 in Torpedo AChR). In competition experiments, the soluble peptides α7(186–197) and Torpedo α1(184–200) inhibited the binding of 125I-α-Bgt to the immobilized α7(186–197) peptide, to native Torpedo AChR, and to the extracellular domain of the human α1 subunit. These results suggest that the toxin-binding sites of the neuronal α7 and muscle-type AChRs bind to identical or overlapping sites on the α-Bgt molecule. In support of this, when synthetic α-Bgt peptides were tested for binding to the recombinant extracellular domains of the human α7 and α1 subunits, and to native Torpedo and α7 AChR, the results indicated that α-Bgt interacts with both neuronal and muscle-type AChRs through its central loop II and C-terminal tail.

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