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Title: Use of antibodies specific to defined regions of scorpion. cap alpha. -toxin to study its interaction with its receptor site on the sodium channel

Abstract

Five antibody populations selected by immunoaffinity chromatography for the specificity toward various regions of toxin II of the scorpion Androctonus australis Hector were used to probe the interaction of this protein with its receptor site on the sodium channel. These studies indicate that two antigenic sites, one located around the disulfide bridge 12-63 and one encompassing residues 50-59, are involved in the molecular mechanisms of toxicity neutralization. Fab fragments specific to the region around disulfide bridge 12-63 inhibit binding of the /sup 125/I-labeled toxin to its receptor site. Also, these two antigenic regions are inaccessible to the antibodies when the toxin is bound to its receptor site. In contrast, the two other antigenic sites encompassing the only ..cap alpha..-helix region (residues 23-32) and a ..beta..-turn structure (residues 32-35) are accessible to the respective antibodies when the toxin is bound to its receptor. Together, these data support the recent proposal that a region made of residues that are conserved in the scorpion toxin family is involved in the binding of the toxin to the receptor.

Authors:
; ; ;
Publication Date:
Research Org.:
INSERM U172, Marseille, France
OSTI Identifier:
6523631
Resource Type:
Journal Article
Journal Name:
Biochemistry; (United States)
Additional Journal Information:
Journal Volume: 25:21
Country of Publication:
United States
Language:
English
Subject:
62 RADIOLOGY AND NUCLEAR MEDICINE; TOXINS; MOLECULAR STRUCTURE; RADIORECEPTOR ASSAY; ANTIBODIES; ANTIGEN-ANTIBODY REACTIONS; CATIONS; IMMUNOGLOBULINS; IODINE 125; ION EXCHANGE CHROMATOGRAPHY; SCORPIONS; SODIUM COMPOUNDS; SODIUM IODIDES; ALKALI METAL COMPOUNDS; ANIMALS; ANTIGENS; ARACHNIDS; ARTHROPODS; BETA DECAY RADIOISOTOPES; CHARGED PARTICLES; CHROMATOGRAPHY; DAYS LIVING RADIOISOTOPES; ELECTRON CAPTURE RADIOISOTOPES; GLOBULINS; HALIDES; HALOGEN COMPOUNDS; INORGANIC PHOSPHORS; INTERMEDIATE MASS NUCLEI; INVERTEBRATES; IODIDES; IODINE COMPOUNDS; IODINE ISOTOPES; IONS; ISOTOPE APPLICATIONS; ISOTOPES; MATERIALS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; PHOSPHORS; PROTEINS; RADIOISOTOPES; SEPARATION PROCESSES; TOXIC MATERIALS; TRACER TECHNIQUES; 550601* - Medicine- Unsealed Radionuclides in Diagnostics

Citation Formats

Ayeb, M E, Bahraoui, E M, Granier, C, and Rochat, H. Use of antibodies specific to defined regions of scorpion. cap alpha. -toxin to study its interaction with its receptor site on the sodium channel. United States: N. p., 1986. Web.
Ayeb, M E, Bahraoui, E M, Granier, C, & Rochat, H. Use of antibodies specific to defined regions of scorpion. cap alpha. -toxin to study its interaction with its receptor site on the sodium channel. United States.
Ayeb, M E, Bahraoui, E M, Granier, C, and Rochat, H. 1986. "Use of antibodies specific to defined regions of scorpion. cap alpha. -toxin to study its interaction with its receptor site on the sodium channel". United States.
@article{osti_6523631,
title = {Use of antibodies specific to defined regions of scorpion. cap alpha. -toxin to study its interaction with its receptor site on the sodium channel},
author = {Ayeb, M E and Bahraoui, E M and Granier, C and Rochat, H},
abstractNote = {Five antibody populations selected by immunoaffinity chromatography for the specificity toward various regions of toxin II of the scorpion Androctonus australis Hector were used to probe the interaction of this protein with its receptor site on the sodium channel. These studies indicate that two antigenic sites, one located around the disulfide bridge 12-63 and one encompassing residues 50-59, are involved in the molecular mechanisms of toxicity neutralization. Fab fragments specific to the region around disulfide bridge 12-63 inhibit binding of the /sup 125/I-labeled toxin to its receptor site. Also, these two antigenic regions are inaccessible to the antibodies when the toxin is bound to its receptor site. In contrast, the two other antigenic sites encompassing the only ..cap alpha..-helix region (residues 23-32) and a ..beta..-turn structure (residues 32-35) are accessible to the respective antibodies when the toxin is bound to its receptor. Together, these data support the recent proposal that a region made of residues that are conserved in the scorpion toxin family is involved in the binding of the toxin to the receptor.},
doi = {},
url = {https://www.osti.gov/biblio/6523631}, journal = {Biochemistry; (United States)},
number = ,
volume = 25:21,
place = {United States},
year = {1986},
month = {10}
}