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Science 20 August 1982:
Vol. 217. no. 4561, pp. 732 - 733
DOI: 10.1126/science.7100919
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Articles

Science, Vol 217, Issue 4561, 732-733
Copyright © 1982 by American Association for the Advancement of Science

articles

Neurotoxin-specific immunoglobulins accelerate dissociation of the neurotoxin-acetylcholine receptor complex

JC Boulain and A Menez

Toxin isolated from cobra venom and labeled with tritium was incubated with membranes rich in acetylcholine receptors. The amount of toxin bound to the receptors was determined and the kinetics of dissociation of the receptor-toxin complex was followed. Addition of an excess of horse antiserum to the venom resulted in a significant acceleration of the dissociation reaction. Similarly, a monoclonal antibody against the toxin accelerated dissociation of the receptor-toxin complex. The results indicate that specific antibody binding destabilizes the toxin-receptor complex.


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How Do Short Neurotoxins Bind to a Muscular-type Nicotinic Acetylcholine Receptor?.
F. Teixeira-Clerc, A. Menez, and P. Kessler (2002)
J. Biol. Chem. 277, 25741-25747
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Do Structural Deviations between Toxins Adopting the Same Fold Reflect Functional Differences?.
A. Ricciardi, M.-H. le Du, M. Khayati, F. Dajas, J.-C. Boulain, A. Menez, and F. Ducancel (2000)
J. Biol. Chem. 275, 18302-18310
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Presentation of Antigen in Immune Complexes Is Boosted by Soluble Bacterial Immunoglobulin Binding Proteins.
M. Leonetti, J. Galon, R. Thai, C. Sautes-Fridman, G. Moine, and A. Menez (1999)
J. Exp. Med. 189, 1217-1228
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Mimicry between Receptors and Antibodies. IDENTIFICATION OF SNAKE TOXIN DETERMINANTS RECOGNIZED BY THE ACETYLCHOLINE RECEPTOR AND AN ACETYLCHOLINE RECEPTOR-MIMICKING MONOCLONAL ANTIBODY.
F. Ducancel, K. Merienne, C. Fromen-Romano, O. Tremeau, L. Pillet, P. Drevet, S. Zinn-Justin, J.-C. Boulain, and A. Menez (1996)
J. Biol. Chem. 271, 31345-31353
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