NEUTRALIZING CAPACITY OF ANTIBODIES ELICITED BY A NONTOXIC PROTEIN PURIFIED FROM THE VENOM OF THE SCORPION TITYUS-SERRULATUS

Polyclonal rabbit antibodies raised against a non-toxic protein (TsNTx P) purified from the toxic fraction of the crude venom of Tityus serru latus can neutralize the effects of the venom. The antigenic specifici ties of anti-TsNTxP were compared by an indirect enzyme-linked immunos orbent assay using TsNTxP, TstFG50 (toxic fraction of venom that repre sents most of the toxicity of the crude venom), and crude venoms from T. serrulatus, T. bahiensis, T. cambridgei, T. stigmurus, Androctonus australis Hector and Centruroides sculpturatus to coat microtitration plates. The anti-TsNTxP antibodies had a comparable high cross-reactiv ity with the toxic fraction and crude venom of T. serrulatus, moderate binding capacity for T. bahiensis, T. cambridgei, T. stigmurus and we re unable to recognize the venoms of A. australis Hector and C. sculpt uratus. Quantities of venom equivalent to 20 LD(50) were effectively n eutralized by 1 ml of the anti-TsNTxP serum. This result shows that th is protein may be of interest in the production of antivenoms for clin ical use. (C) 1997 Elsevier Science Ltd.