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Modulation of the pharmacological effects of enzymatically-active PLA2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga

Authors
  • Oliveira, Simone CB1
  • Fonseca, Fabiana V1
  • Antunes, Edson2
  • Camargo, Enilton A2
  • Morganti, Rafael P2
  • Aparício, Ricardo3
  • Toyama, Daniela O4
  • Beriam, Luís OS5
  • Nunes, Eudismar V6
  • Cavada, Benildo S6
  • Nagano, Celso S7
  • Sampaio, Alexandre H7
  • Nascimento, Kyria S7
  • Toyama, Marcos H8
  • 1 UNICAMP, Biochemistry Department, Biology Institute, Campinas, São Paulo, Brazil , Campinas
  • 2 University of Medical Science, UNICAMP, Pharmacology Department, Campinas, São Paulo, Brazil , Campinas
  • 3 UNICAMP, Chemistry Institute, Campinas, São Paulo, Brazil , Campinas
  • 4 University of Biological and EXaperimental Sciences, University of Mackenzie, São Paulo, São Paulo, Brazil , São Paulo
  • 5 Experimental Center of the Biological Institute, Laboratory of Vegetal Bacteriology, Campinas, São Paulo, Brazil , Campinas
  • 6 IBV, Institute of Biomedicine of Valencia, Valencia, Spain , Valencia
  • 7 Federal University of Ceará, Lab. of marine biochemistry -BioMar-Lab, Fishing Engeneer Department, Fortaleza, Ceará, Brazil , Fortaleza
  • 8 UNESP, Litoral Paulista Campus, São Vicente, São Paulo, Brazil , São Vicente
Type
Published Article
Journal
BMC Biochemistry
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Jun 06, 2008
Volume
9
Issue
1
Identifiers
DOI: 10.1186/1471-2091-9-16
Source
Springer Nature
Keywords
License
Green

Abstract

BackgroundAn interaction between lectins from marine algae and PLA2 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 PLA2 isolated from rattlesnake venom (Crotalus durissus cascavella), to better understand the enzymatic and pharmacological mechanisms of the PLA2 and its complex.ResultsThis 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, PLA2 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.ConclusionThe 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.

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