Purification, amino-acid sequence and partial characterization of two toxins with anti-insect activity from the venom of the South American scorpion Tityus bahiensis (Buthidae)

被引:40
作者
Pimenta, AMC [1 ]
Martin-Eauclaire, MF
Rochat, H
Figueiredo, SG
Kalapothakis, E
Afonso, LCC
De Lima, ME
机构
[1] Univ Fed Minas Gerais, ICB, Dept Fisiol & Biofis, BR-31270901 Belo Horizonte, MG, Brazil
[2] Univ Fed Minas Gerais, ICB, Dept Farmacol, BR-31270901 Belo Horizonte, MG, Brazil
[3] Univ Fed Minas Gerais, ICB, Dept Bioquim & Imunol, BR-31270901 Belo Horizonte, MG, Brazil
[4] IFR Jean Roche, Lab Biochim Ingn Prot, UMR6560, F-13916 Marseille, France
[5] Univ Fed Espirito Santo, CBM, Dept Ciencias Fisiol, BR-29040090 Vitoria, ES, Brazil
[6] Univ Fed Ouro Preto, ICEB, NUPEB, DECBI,Lab Imunoparasitol, BR-35400000 Ouro Preto, MG, Brazil
关键词
Tityus bahiensis; toxin; anti-insect activity; three-dimensional models;
D O I
10.1016/S0041-0101(00)00240-3
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
We report here the isolation by a two-step chromatographic procedure of two new toxins from the South American scorpion Tityus bahiensis. Their amino-acid sequences and some of their biological features were established. The two toxins have different biological properties. Toxin TbIT-I had almost no activity or pharmacological effects in vertebrate tissues whereas it was lethal to house flies (LD50 80.0 ng/house fly). In contrast, Tb2-II was active against both mammals (intracerebroventricular injection of 100 ng/mouse was lethal) and insects (LD50 40.0 ng/house fly). The amino-acid sequences of these toxins were established and found to be similar (60-95%) to previously described beta -toxins from the Tityus, genus. Based on the available comparative information, this study attempts identify possible structure-function relationships that may be responsible for the differences in bioactivity displayed by these toxins. (C) 2001 Published by Elsevier Science Ltd.
引用
收藏
页码:1009 / 1019
页数:11
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