Biological and proteomic characterization of the venom from Peruvian Andes rattlesnake Crotalus durissus. (February 2022)

• Record Type: Journal Article
• Authors: Rodrigues, Carolina Rego; Molina Molina, Denis A.; de Souza, Dayane L. Naves; Cardenas, Javier; Costal-Oliveira, Fernanda; Guerra-Duarte, Clara; Chávez-Olórtegui, Carlos
• Is Part Of: Toxicon. Volume 207(2022)
• Page Start: 31
• Page End: 42
• Publication Date: 2022-02
• Subjects: Crotalus durissus -- Venom proteomics -- Peruvian snake -- Venom characterization; Toxins -- Periodicals; Venom -- Periodicals; 615.9
• DOI: 10.1016/j.toxicon.2021.12.008
• Languages: English
• ISSNs: 0041-0101

Abstract

Abstract: The Peruvian rattlesnake Crotalus durissus is a venomous species that is restricted to the Peruvian Departments of Puno and Madre de Dios. Although clinically meaningful in this region, Crotalus durissus venom composition remains largely elusive. In this sense, this work aimed to provide a primary description of Peruvian C. durissus venom (P Cd V). The enzymatic activities (SVMP, SVSP, LAAO, Hyaluronidase and PLA2 ) of P Cd V were analyzed and compared to Brazilian Crotalus durissus terrificus venom (B Cdt V). P Cd V showed higher PLA2 activity when compared to the Brazilian venom. P Cd V also showed cytotoxicity in VERO cells. For proteomic analysis, P Cd V proteins were separated by HPLC, followed by SDS-PAGE. Gel bands were excised and tryptic digested for MALDI-TOF/TOF identification. Approximately 21 proteins were identified, belonging to 7 families. Phospholipases A2 (PLA2, 66.63%) were the most abundant proteins of the venom, followed by snake venom serine proteinases (SVSPs, 13.37%), C-type lectins (Snaclec, 8.98%) and snake venom metalloproteinases (SVMPs, 7.13%), crotamine (2.98%) and phosphodiesterase (PDE, 0.87%). Moreover, antivenom recognition assays indicated that both Brazilian and Peruvian antivenoms recognize P Cd V, indicating the presence of antigenically related proteins in crotalic venoms. The results reported here, may impact in the venom selection for the production of effective Pan-American crotalic antivenom. Graphical abstract: Image 1 Highlights: P Cd V and B Cdt V show a very diverse pattern of toxic activities. P Cd V presents high phospholipase in vitro activity. P Cd V and B Cdt V have antigenically related proteins. Proteomic analysis showed that PLA2, SVSPs, CTLs and SVMPs are the main components of P Cd V.