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

Five antibody populations selected by immunoaffinity chromatography for their 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 a...

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Bibliographic Details
Published in:Biochemistry (Easton) 1986-10, Vol.25 (21), p.6671-6678
Main Authors: El Ayeb, Mohamed, Bahraoui, El Mostafa, Granier, Claude, Rochat, Herve
Format: Article
Language:English
Subjects:
alpha -toxin
Amino Acid Sequence
ANDROCTONUS AUSTRALIS
Animal poisons toxicology. Antivenoms
Animals
ANTIBODIES
Antibodies - isolation & purification
ANTICORPS
ANTICUERPOS
Antigen-Antibody Complex
Biological and medical sciences
Brain - metabolism
ESCORPION
Ion Channels - metabolism
Kinetics
Medical sciences
Rats
Rats, Inbred Strains
Receptors, Cholinergic - metabolism
SCORPION
Scorpion Venoms - immunology
Scorpion Venoms - metabolism
SCORPIONS
SODIO
SODIUM
Sodium - metabolism
Sodium Channels
Synaptosomes - metabolism
Toxicology
TOXINAS
TOXINE
TOXINS
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Summary:Five antibody populations selected by immunoaffinity chromatography for their 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 125I-labeled toxin to its receptor site. Also, these two antigenic regions are inaccessible to their antibodies when the toxin is bound to its receptor site. In contrast, the two other antigenic sites encompassing the only alpha-helix region (residues 23-32) and a beta-turn structure (residues 32-35) are accessible to their 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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00369a052