Monoclonal antibodies to scorpion toxins. Characterization and molecular mechanisms of neutralization.
Two mAb specific for the potent toxin II of the scorpion Androctonus australis Hector have been produced. One of them shows both high affinity binding to the toxin (Kd) = 0.8 nM) and in vivo and in vitro neutralizing properties. The mechanism by which the antibody neutralizes toxin binding to its receptor was shown to be of the competitive type, the epitope overlapping or being close to the receptor-binding region of the toxin. Several residues of the toxin clustered in the C-terminal region were shown likely to be part of the discontinuous epitope recognized by the antibody. The positive charge of the N epsilon-Lys-58 seems to play a pivotal role in the binding of the toxin to both the mAb and the sodium channel receptor.
Bahraoui
E
E
Laboratoire de Biochimie, CNRS UA 1179, Marseille, France.
Pichon
J
J
Muller
J M
JM
Darbon
H
H
Elayeb
M
M
Granier
C
C
Marvaldi
J
J
Rochat
H
H
D000107:Acetylation; D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis / Q000502:physiology; D001666:Binding Sites, Antibody; D001667:Binding, Competitive; D000939:Epitopes / Q000276:immunology; D007158:Immunologic Techniques; D007700:Kinetics; D051379:Mice; D008807:Mice, Inbred BALB C; D008810:Mice, Inbred C57BL; D009500:Neutralization Tests; D010449:Peptide Mapping; D012604:Scorpion Venoms / Q000276:immunology* / Q000378:metabolism / Q000494:pharmacology; D014118:Toxins, Biological / Q000276:immunology* / Q000378:metabolism / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D000939:Epitopes; D012604:Scorpion Venoms; D014118:Toxins, Biological; C044221:scorpion toxin I''