Biochemical characterization of a phospholipase A 2 homologue from the venom of the social wasp Polybia occidentalis .

Autor: Diniz-Sousa R; Center for the Study of Biomolecules Applicable to Health (CEBio), Oswaldo Cruz Foundation - Rondônia (Fiocruz - Rondônia), Porto Velho, RO Brazil.; 2Department of Medicine, Federal University of Rondônia (UNIR), Porto Velho, RO Brazil.; 3Postgraduate Program in Experimental Biology (PGBIOEXP), Federal University of Rondônia (UNIR), Porto Velho, RO Brazil.; São Lucas University Center (UniSL), Porto Velho, RO Brazil., Kayano AM; Center for the Study of Biomolecules Applicable to Health (CEBio), Oswaldo Cruz Foundation - Rondônia (Fiocruz - Rondônia), Porto Velho, RO Brazil.; 2Department of Medicine, Federal University of Rondônia (UNIR), Porto Velho, RO Brazil., Caldeira CA; Center for the Study of Biomolecules Applicable to Health (CEBio), Oswaldo Cruz Foundation - Rondônia (Fiocruz - Rondônia), Porto Velho, RO Brazil.; 2Department of Medicine, Federal University of Rondônia (UNIR), Porto Velho, RO Brazil.; 5Postgraduate Program in Biodiversity and Biotechnology, Bionorte Network, Federal University of Rondônia (UNIR), Porto Velho, RO Brazil., Simões-Silva R; Center for the Study of Biomolecules Applicable to Health (CEBio), Oswaldo Cruz Foundation - Rondônia (Fiocruz - Rondônia), Porto Velho, RO Brazil.; 2Department of Medicine, Federal University of Rondônia (UNIR), Porto Velho, RO Brazil., Monteiro MC; 6School of Pharmacy, Federal University of Pará (UFPA), Belém, PA Brazil., Moreira-Dill LS; Center for the Study of Biomolecules Applicable to Health (CEBio), Oswaldo Cruz Foundation - Rondônia (Fiocruz - Rondônia), Porto Velho, RO Brazil.; 2Department of Medicine, Federal University of Rondônia (UNIR), Porto Velho, RO Brazil., Grabner FP; Center for the Study of Biomolecules Applicable to Health (CEBio), Oswaldo Cruz Foundation - Rondônia (Fiocruz - Rondônia), Porto Velho, RO Brazil.; São Lucas University Center (UniSL), Porto Velho, RO Brazil., Calderon LA; Center for the Study of Biomolecules Applicable to Health (CEBio), Oswaldo Cruz Foundation - Rondônia (Fiocruz - Rondônia), Porto Velho, RO Brazil.; 2Department of Medicine, Federal University of Rondônia (UNIR), Porto Velho, RO Brazil., Zuliani JP; Center for the Study of Biomolecules Applicable to Health (CEBio), Oswaldo Cruz Foundation - Rondônia (Fiocruz - Rondônia), Porto Velho, RO Brazil.; 2Department of Medicine, Federal University of Rondônia (UNIR), Porto Velho, RO Brazil., Stábeli RG; Center for the Study of Biomolecules Applicable to Health (CEBio), Oswaldo Cruz Foundation - Rondônia (Fiocruz - Rondônia), Porto Velho, RO Brazil.; 7Department of Medicine, UFSCar, São Carlos, Center of Translational Medicine, Fiocruz - SP, and School of Medicine of Ribeirão Preto, University of São Paulo (USP), São Paulo, Brazil., Soares AM; Center for the Study of Biomolecules Applicable to Health (CEBio), Oswaldo Cruz Foundation - Rondônia (Fiocruz - Rondônia), Porto Velho, RO Brazil.; 2Department of Medicine, Federal University of Rondônia (UNIR), Porto Velho, RO Brazil.; São Lucas University Center (UniSL), Porto Velho, RO Brazil.
Jazyk: angličtina
Zdroj: The journal of venomous animals and toxins including tropical diseases [J Venom Anim Toxins Incl Trop Dis] 2018 Feb 15; Vol. 24, pp. 5. Date of Electronic Publication: 2018 Feb 15 (Print Publication: 2018).
DOI: 10.1186/s40409-018-0143-1
Abstrakt: 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 A 2 (PLA 2 ) 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 PLA 2 homologues.
Conclusion: This is the first report of an enzymatically inactive PLA 2 isolated from wasp venom, similar to snake PLA 2 homologues.
Competing Interests: The present study was approved by the Ethics Committee on Animal Use (protocol no. 2012/1), the Ethics Committee of FCFRP-USP (protocol no. 102/2009) and received the Certificate of Presentation for Ethical Appreciation (CAAE: 14204413.5.0000.0011). Moreover, the research was also approved by the Brazilian Institute of Environment and Renewable Natural Resources (IBAMA – license number 27131-1).Not applicable.The authors declare that they have no competing interests.Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Databáze: MEDLINE
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