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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Unraveling the structure and function of CdcPDE: A novel phosphodiesterase from Crotalus durissus collilineatus snake venom

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de Oliveira, Isadora Sousa [1] ; Pucca, Manuela Berto [2] ; Wiezel, Gisele Adriano [1] ; Cardoso, Iara Aime [1] ; Figueiredo Bordon, Karla de Castro [1] ; Sartim, Marco Aurelio [3, 4] ; Kalogeropoulos, Konstantinos [5] ; Ahmadi, Shirin [5] ; Baiwir, Dominique [6, 7] ; Nonato, Maria Cristina [1] ; Sampaio, Suely Vilela [8] ; Laustsen, Andreas Hougaard [5] ; dem Keller, Ulrich auf [5] ; Quinton, Loic [6] ; Arantes, Eliane Candiani [1]
Total Authors: 15
[1] Univ Sao Paulo, Dept Biomol Sci, Sch Pharmaceut Sci Ribeirao Preto, Ribeirao Preto, SP - Brazil
[2] Univ Fed Roraima, Med Sch, Boa Vista, Parana - Brazil
[3] Univ Fed Amazonas, Inst Biol Sci, Manaus, Amazonas - Brazil
[4] Dr Heitor Vieira Dourado Trop Med Fdn, Dept Teaching & Res, Manaus, Amazonas - Brazil
[5] Tech Univ Denmark, Dept Biotechnol & Biomed, Lyngby - Denmark
[6] Univ Liege, Dept Chem, MotSys Res Unit, Mass Spectrometry Lab, Liege - Belgium
[7] Univ Liege, GIGA Prote Facil, Liege - Belgium
[8] Univ Sao Paulo, Sch Pharmaceut Sci Ribeirao Preto, Dept Clin Anal Toxicol & Food Sci, Ribeirao Preto, SP - Brazil
Total Affiliations: 8
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 178, p. 180-192, MAY 1 2021.
Web of Science Citations: 0

This study reports the isolation, structural, biochemical, and functional characterization of a novel phosphodiesterase from Crotalus durissus collilineatus venom (CdcPDE). CdcPDE was successfully isolated from whole venom using three chromatographic steps and represented 0.7% of total protein content. CdcPDE was inhibited by EDTA and reducing agents, demonstrating that metal ions and disulfide bonds are necessary for its enzymatic activity. The highest enzymatic activity was observed at pH 8-8.5 and 37 degrees C. Kinetic parameters indicated a higher affinity for the substrate bis(p-nitrophenyl) phosphate compared to others snake venom PDEs. Its structural characterization was done by the determination of the protein primary sequence by Edman degradation and mass spectrometry, and completed by the building of molecular and docking-based models. Functional in vitro assays showed that CdcPDE is capable of inhibiting platelet aggregation induced by adenosine diphosphate in a dose-dependent manner and demonstrated that CdcPDE is cytotoxic to human keratinocytes. CdcPDE was recognized by the crotalid antivenom produced by the Instituto Butantan. These findings demonstrate that the study of snake venom toxins can reveal new molecules that may be relevant in cases of snakebite envenoming, and that can be used as molecular tools to study pathophysiological processes due to their specific biological activities. (C) 2021 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 17/00586-6 - Characterization of a phospholipase A2 inhibitor from the Crotalus durissus terrificus venom gland: a possible adjuvant in the antivenom therapy
Grantee:Gisele Adriano Wiezel
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 17/03580-9 - Biochemical, structural and functional evaluation of a phosphodiesterase from Crotalus durissus collilineatus venom
Grantee:Isadora Sousa de Oliveira
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 19/10173-6 - Production, modification and characterization of animal toxins with potential biotechnological application
Grantee:Eliane Candiani Arantes Braga
Support Opportunities: Regular Research Grants
FAPESP's process: 11/23236-4 - Native and recombinant animal toxins: functional, structural and molecular analysis
Grantee:Suely Vilela
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 18/21233-7 - Mass spectrometry analysis of a new phosphodiesterase from Crotalus durissus collilineatus venom
Grantee:Isadora Sousa de Oliveira
Support Opportunities: Scholarships abroad - Research Internship - Doctorate