Isolation, functional, and partial biochemical characterization of galatrox, an acidic lectin from Bothrops atrox snake venom

Author(s):Show less -

Mendonca-Franqueiro, Elaine de Paula ^[1] ; Alves-Paiva, Raquel de Melo ^[1] ; Sartim, Marco Aurelio ^[1] ; Callejon, Daniel Roberto ^[1] ; Paiva, Helder Henrique ^[1] ; Antonucci, Gilmara Ausech ^[1] ; Rosa, Jose Cesar ^{[2, 3]} ; Oliveira Cintra, Adelia Cristina ^[1] ; Franco, Joao Jose ^[1] ; Arantes, Eliane Candiani ^[4] ; Dias-Baruffi, Marcelo ^[1] ; Sampaio, Suely Vilela ^[1]

Affiliation

^[1] Univ Sao Paulo, Fac Ciencias Farmaceut Ribeirao Preto, Dept Anal Clin Toxicol & Bromatol, BR-14040903 Ribeirao Preto, SP - Brazil

^[2] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Biol Celular & Mol & Bioagentes Patogen, BR-14040903 Ribeirao Preto, SP - Brazil

^[3] Univ Sao Paulo, Fac Med Ribeirao Preto, Ctr Quim Proteinas, BR-14040903 Ribeirao Preto, SP - Brazil

^[4] Univ Sao Paulo, Fac Ciencias Farmaceut Ribeirao Preto, Dept Quim & Fis, BR-14040903 Ribeirao Preto, SP - Brazil

• Document type: Journal article
• Source: ACTA BIOCHIMICA ET BIOPHYSICA SINICA; v. 43, n. 3, p. 181-192, 2011.
• Web of Science Citations: 10

Abstract

Snake venom lectins have been studied in regard to their chemical structure and biological functions. However, little is known about lectins isolated from Bothrops atrox snake venom. We report here the isolation and partial functional and biochemical characterization of an acidic glycan-binding protein called galatrox from this venom. This lectin was purified by affinity chromatography using a lactosyl-sepharose column, and its homogeneity and molecular mass were evaluated by high-performance liquid chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry. The purified galatrox was homogeneous and characterized as an acidic protein (pI 5.2) with a monomeric and dimeric molecular mass of 16.2 and 32.5 kDa, respectively. Alignment of N-terminal and internal amino acid sequences of galatrox indicated that this protein exhibits high homology to other C-type snake venom lectins. Galatrox showed optimal hemagglutinating activity at a concentration of 100 mu g/ml and this effect was drastically inhibited by lactose, ethylenediaminetetraacetic acid, and heating, which confirmed galatrox's lectin activity. While galatrox failed to induce the same level of paw edema or mast cell degranulation as B. atrox crude venom, galatrox did alter cellular viability, which suggested that galatrox might contribute to venom toxicity by directly inducing cell death. (AU)

• FAPESP's process: 05/54855-0 - Animal toxins: structure, function and biotechnological applications
• Grantee: Suely Vilela
• Support Opportunities: Research Projects - Thematic Grants