You are in the accessibility menu

Please use this identifier to cite or link to this item:
Modulation of the pharmacological effects of enzymatically-active PLA 2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga
  • Universidade Estadual de Campinas (UNICAMP)
  • University of Mackenzie
  • Biological Institute
  • IBV
  • Federal University of Ceará
  • Universidade Estadual Paulista (UNESP)
Background. An interaction between lectins from marine algae and PLA 2 from rattlesnake was suggested some years ago. We, herein, studied the effects elicited by a small isolectin (BTL-2), isolated from Bryothamnion triquetrum, on the pharmacological and biological activities of a PLA 2 isolated from rattlesnake venom (Crotalus durissus cascavella), to better understand the enzymatic and pharmacological mechanisms of the PLA 2 and its complex. Results. This PLA2 consisted of 122 amino acids (approximate molecular mass of 14 kDa), its pI was estimated to be 8.3, and its amino acid sequence shared a high degree of similarity with that of other neurotoxic and enzymatically-active PLA2s. BTL-2 had a molecular mass estimated in approximately 9 kDa and was characterized as a basic protein. In addition, BTL-2 did not exhibit any enzymatic activity. The PLA2 and BTL-2 formed a stable heterodimer with a molecular mass of approximately 24-26 kDa, estimated by molecular exclusion HPLC. In the presence of BTL-2, we observed a significant increase in PLA2 activity, 23% higher than that of PLA2 alone. BTL-2 demonstrated an inhibition of 98% in the growth of the Gram-positive bacterial strain, Clavibacter michiganensis michiganensis (Cmm), but only 9.8% inhibition of the Gram-negative bacterial strain, Xanthomonas axonopodis pv passiflorae (Xap). PLA2 decreased bacterial growth by 27.3% and 98.5% for Xap and Cmm, respectively, while incubating these two proteins with PLA2-BTL-2 inhibited their growths by 36.2% for Xap and 98.5% for Cmm. PLA2 significantly induced platelet aggregation in washed platelets, whereas BTL-2 did not induce significant platelet aggregation in any assay. However, BTL-2 significantly inhibited platelet aggregation induced by PLA2. In addition, PLA 2 exhibited strong oedematogenic activity, which was decreased in the presence of BTL-2. BTL-2 alone did not induce oedema and did not decrease or abolish the oedema induced by the 48/80 compound. Conclusion. The unexpected results observed for the PLA2-BTL-2 complex strongly suggest that the pharmacological activity of this PLA2 is not solely dependent on the presence of enzymatic activity, and that other pharmacological regions may also be involved. In addition, we describe for the first time an interaction between two different molecules, which form a stable complex with significant changes in their original biological action. This opens new possibilities for understanding the function and action of crude venom, an extremely complex mixture of different molecules. © 2008 Oliveira et al; licensee BioMed Central Ltd.
Issue Date: 
BMC Biochemistry, v. 9, n. 1, 2008.
  • bryothamnion triquerum lectin 2
  • heterodimer
  • lectin
  • phospholipase A2
  • snake venom
  • algal protein
  • amino acid sequence
  • bacterial growth
  • bacterial strain
  • controlled study
  • edema
  • enzyme activity
  • Gram positive bacterium
  • growth inhibition
  • high performance liquid chromatography
  • methodology
  • molecular weight
  • nonhuman
  • protein analysis
  • protein isolation
  • red alga
  • thrombocyte aggregation
  • Xanthomonas axonopodis
  • animal
  • chemistry
  • enzymology
  • isolation and purification
  • metabolism
  • molecular genetics
  • algae
  • Bacteria (microorganisms)
  • Bryothamnion triquetrum
  • Clavibacter michiganensis subsp. michiganensis
  • Crotalus durissus cascavella
  • Negibacteria
  • Posibacteria
  • Rhodophyta
  • Algae, Red
  • Algal Proteins
  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Crotalid Venoms
  • Lectins
  • Molecular Sequence Data
  • Phospholipases A2
Access Rights: 
Acesso aberto
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.