Biochemical characterization of a phospholipase A2 homologue from the venom of the social wasp Polybia occidentalis

Abstract Background: Wasp venoms constitute a molecular reservoir of new pharmacological substances such as peptides and proteins, biological property holders, many of which are yet to be identified. Exploring these sources may lead to the discovery of molecules hitherto unknown. This study describe...

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Bibliographic Details
Published in:Journal of Venomous Animals and Toxins including Tropical Diseases
Main Authors: Rafaela Diniz-Sousa, Anderson M. Kayano, Cleópatra A. Caldeira, Rodrigo Simões-Silva, Marta C. Monteiro, Leandro S. Moreira-Dill, Fernando P. Grabner, Leonardo A. Calderon, Juliana P. Zuliani, Rodrigo G. Stábeli, Andreimar M. Soares
Format: Article in Journal/Newspaper
Language:English
Published: SciELO 2018
Subjects:
Wasp
Polybia occidentalis
PocTX
PLA2 homologue
Arctic medicine. Tropical medicine
RC955-962
Toxicology. Poisons
RA1190-1270
Zoology
QL1-991
Arctic
Online Access:https://doi.org/10.1186/s40409-018-0143-1
https://doaj.org/article/426dcbb15370457d818b3af54a870f26
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Summary:Abstract Background: Wasp venoms constitute a molecular reservoir of new pharmacological substances such as peptides and proteins, biological property holders, many of which are yet to be identified. Exploring these sources may lead to the discovery of molecules hitherto unknown. This study describes, for the first time in hymenopteran venoms, the identification of an enzymatically inactive phospholipase A2 (PLA2) from the venom of the social wasp Polybia occidentalis. Methods: P. occidentalis venom was fractioned by molecular exclusion and reverse phase chromatography. For the biochemical characterization of the protein, 1D and 2D SDS-PAGE were performed, along with phospholipase activity assays on synthetic substrates, MALDI-TOF mass spectrometry and sequencing by Edman degradation. Results: The protein, called PocTX, was isolated using two chromatographic steps. Based on the phospholipase activity assay, electrophoresis and mass spectrometry, the protein presented a high degree of purity, with a mass of 13,896. 47 Da and a basic pI. After sequencing by the Edman degradation method, it was found that the protein showed a high identity with snake venom PLA2 homologues. Conclusion: This is the first report of an enzymatically inactive PLA2 isolated from wasp venom, similar to snake PLA2 homologues.

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