1. Danger in the Canopy. Comparative Proteomics and Bioactivities of the Venoms of the South American Palm Pit Viper Bothrops bilineatus Subspecies bilineatus and smaragdinus and Antivenomics of B. b. bilineatus (Rondônia) Venom against the Brazilian Pentabothropic Antivenom
- Author
-
Sanz, Libia, Quesada-Bernat, Sarai, Pérez, Alicia, de Morais-Zani, Karen, SantˈAnna, Sávio S., Hatakeyama, Daniela M., Tasima, Lidia J., De Souza, Moisés B., Kayano, Anderson M., Zavaleta, Alfonso, Salas, Maria, Soares, Andreimar M., Calderon, Leonardo A., Tanaka-Azevedo, Anita M., Lomonte, Bruno, Calvete, Juan J., Caldeira, Cleópatra A.S., Ministerio de Ciencia, Innovación y Universidades (España), Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil), Fundação de Amparo à Pesquisa do Estado de São Paulo, Fundação Rondônia de Amparo ao Desenvolvimento das Ações Científicas e Tecnológicas e à Pesquisa do Estado de Rondônia, Calvete, Juan J. [0000-0001-5026-3122], and Calvete, Juan J.
- Subjects
Antivenomics ,South American palm viper ,Brazilian pentabothropic antivenom ,Comparative snake venomics ,Bothrops bilineatus - Abstract
15 páginas, 5 figuras, 1 tabla. Dispone de información suplementaria de libre acceso en: https://pubs.acs.org/doi/10.1021/acs.jproteome.0c00337, We report a structural and functional proteomics characterization of venoms of the two subspecies (Bothrops bilineatus bilineatus and B. b. smaragdinus) of the South American palm pit viper from the Brazilian state of Rondônia and B. b. smaragdinus from Perú. These poorly known arboreal and mostly nocturnal generalist predators are widely distributed in lowland rainforests throughout the entire Amazon region, where they represent an important cause of snakebites. The three B. bilineatus spp. venom samples exhibit overall conserved proteomic profiles comprising components belonging to 11 venom protein classes, with PIII (34-40% of the total venom proteins) and PI (8-18%) SVMPs and their endogenous tripeptide inhibitors (SVMPi, 8-10%); bradykinin-potentiating-like peptides (BBPs, 10.7-15%); snake venom serine proteinases (SVSP, 5.5-14%); C-type lectin-like proteins (CTL, 3-10%); phospholipases A2 (PLA2, 2.8-7.6%); cysteine-rich secretory proteins (CRISP, 0.9-2.8%); l-amino acid oxidases (LAO, 0.9-5%) representing the major components of their common venom proteomes. Comparative analysis of the venom proteomes of the two geographic variants of B. b. smaragdinus with that of B. b. bilineatus revealed that the two Brazilian taxa share identical molecules between themselves but not with Peruvian B. b. smaragdinus, suggesting hybridization between the geographically close, possibly sympatric, Porto Velho (RO, BR) B. b. smaragdinus and B. b. bilineatus parental populations. However, limited sampling does not allow determining the frequency of this event. The toxin arsenal of the South American palm pit vipers may account for the in vitro recorded collagenolytic, caseinolytic, PLA2, l-amino acid oxidase, thrombin-like and factor X-activating activities, and the clinical features of South American palm pit viper envenomings, i.e., local and progressively ascending pain, shock and loss of consciousness, spontaneous bleeding, and profound coagulopathy. The remarkable cross-reactivity of the Brazilian pentabothropic SAB antivenom toward the heterologous B. b. bilineatus venom suggests that the paraspecific antigenic determinants should have been already present in the venom of the last common ancestor of the Bothrops ″jararaca″ and ″taeniatus″ clades, about 8.5 Mya in the mid-late Miocene epoch of the Cenozoic era. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the data set identifiers PXD020043, PXD020026, and PXD020013., This study was partly supported by grant BFU2017-89103-P from the Ministerio de Ciencia, Innovacion y Universidades, ́ Journal of Proteome Research pubs.acs.org/jpr Article https://dx.doi.org/10.1021/acs.jproteome.0c00337 J. Proteome Res. 2020, 19, 3518−3532 3528 Madrid (Spain) to J.J.C. and by Vicerrectori ́ a de Investigacion, ́ Universidad de Costa Rica to B.L. The authors wish to express their gratitude to Conselho Nacional de Desenvolvimento Cienti ́ fico e Tecnologico (CNPq/MCTIC), Coordenac ́ a̧ o de ̃ Aperfeicoamento de Pessoal de Ni ̧ ́ vel Superior (CAPES/ MEC), Fundaca̧ o de Amparo a ̃ ́ Pesquisa do Estado de Saõ Paulo (FAPESP), and Fundaca̧ o Rondo ̃ ̂nia de Amparo ao Desenvolvimento das Aco̧ ̃es Cienti ́ ficas e Tecnologicas de ́ Pesquisa do Estado de Rondônia (FAPERO) for financial support. Authors gratefully thank Dr. Paulo Sergio Bernarde, ́ Universidade Federal do Acre, Campus Floresta, Laboratorió de Herpetologia, Cruzeiro do Sul, Acre, Brazil, for the kind donation of the pictures of B. b. smaragdinus and B. b. bilineatus shown in Figure 1. The venom of Peruvian B. b. smaradignus was used in this study as part of a research agreement signed between the Instituto Nacional de Salud (Peru) and the ́ Universidad Peruana Cayetano Heredia
- Published
- 2020