PARTIAL CHARACTERIZATION OF THE VENOM OF THE SPIDER Oligoctenus ornatus (CTENIDAE)

OLIVEIRA C. F. B. (1); ASSIS I. S. (1); REZENDE F. F. (1); GONÇALVES J. M. (1); SANTOS D. M. (2); BORGES M. H. (1,2); DE LIMA M. E. (2); RICHARDSON M. (1); CORDEIRO M. N. (1)

(1) Lab. de Bioquímica e Química de Proteínas, Diretoria de Pesquisa e Desenvolvimento, FUNED; (2) Lab. de Venenos e Toxinas Animais, Dep. de Bioquímica e Imunologia, UFMG

The objective of this work was to characterize the venoms of the male and female spiders of Oligoctenus ornatus. The venoms examined by SDS-PAGE and in reverse phase chromatography contained high complexity. The LD50 values for the female venom injected in mice (ic) were about 3.5 times more toxic than the venom of male. For flies were injected about 55ng both male and female venom and not possible to determine the LD50 value. Toxicity tests in mice showed effects such as excitability, salivation, spastic and flaccid paralysis, tail elevation and sometimes death. In flies the effects were excitability, salivation, trembling of the legs and body, lost of ability to walk or to fly and death. The crude venom of female was partially purified using reverse phase chromatography on an analytical column of Vydac C4. Preliminary bioassays with the fractions 8, 13, 17 and 40 showed toxicity towards insects. The fractions 13, 17, 22-26, 28, 29, 33, 38-41, 43 and 51 showed toxic effects in mice. SDS-PAGE zymogram experiments using hyaluronic acid, glycol chitin and gelatin as substrates showed the presence of hyaluronidase, chitinase and proteolytic enzymes, respectively in this venom. In addition, the alpha chain of fibrinogen was degraded when it was incubated with the venoms during 30 min at 37ºC. The amino acid sequences of various peptides purified from these venoms were determined by automated Edman degradation and show high similarity with peptides from Phoneutria nigriventer but these are other sequences that show no significant similarity.

KEY WORDS: Oligoctenus ornatus, spider venoms, neurotoxins, enzymes, proteolytic activity.

FINANCIAL SUPPORT: CNPq, FAPEMIG, PUC-Minas, FUNED

CORRESPONDENCE TO: CAMILA FRANCO, Lab. de Bioquímica e Química de Proteínas, Diretoria de Pesquisa e Desenvolvimento, FUNED. Belo Horizonte, MG, Brasil. Tel.: (31) 8811-1495 Email: camilafrancobo@gmail.com