Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/53980
Type: Artigo de periódico
Title: Ability of rabbit antiserum against crotapotin to neutralize the neurotoxic, myotoxic and phospholipase A(2) activities of crotoxin from Crotalus durissus cascavella snake venom
Author: Beghini, DG
Damico, DCS
da Cruz-Hofling, MA
Rodrigues-Simioni, L
Delatorre, MC
Hyslop, S
Marangoni, S
Abstract: The toxicity of crotoxin, the major toxin of Crotalus durissus terrificus (South American rattlesnake) venom, is mediated by its basic phospholipase A(2) (PLA(2)) subunit. This PLA(2) is non-covalently associated with crotapotin, an acidic, enzymatically inactive subunit of the crotoxin complex. In this work, rabbit antiserum raised against crotapotin purified from Crotalus durissus eascavella venom was tested for its ability to neutralize the neurotoxicity of this venom and its crotoxin in vitro. The ability of this antiserum to inhibit the enzymatic activity of the crotoxin complex and PLA(2) alone was also assessed, and its potency in preventing myotoxicity was compared with that of antisera raised against crotoxin and PLA(2). Antiserum to crotapotin partially neutralized the neuromuscular blockade caused by venom and crotoxin in electrically stimulated mouse phrenic nerve-hemidiaphragm preparations and prevented the venom-induced myotoxicity, but did not inhibit the enzymatic activity of crotoxin and purified PLA(2). In contrast, previous findings showed that antisera against crotoxin and PLA(2) from C. d. cascavella effectively neutralized the neuromuscular blockade and PLA(2) activity of this venom and its crotoxin. The partial neutralization of crotoxin-mediated neurotoxicity by antiserum to crotapotin probably reduced the binding of crotoxin to its receptor following interaction of the antiserum with the crotapotin moiety of the complex. (c) 2007 Elsevier Ltd. All rights reserved.
Subject: antiserum
crotapotin
crotoxin
neuromuscular blockade
neutralization
phospholipase A(2)
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/j.tiv.2007.08.007
Date Issue: 2008
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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