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Toxins (Basel). 2015 Dec 25;8(1). pii: E9. doi: 10.3390/toxins8010009.

Snake Venomics and Antivenomics of Bothrops diporus, a Medically Important Pitviper in Northeastern Argentina.

Author information

1
Facultad de Ciencias Exactas y Naturales y Agrimensura, Universidad Nacional del Nordeste, Avenida Libertad 5470, 3400 Corrientes, Argentina. claudiacarolinagay@yahoo.com.ar.
2
Instituto de Biomedicina de Valencia, CSIC, Jaime Roig 11, 46010 Valencia, Spain. libia.sanz@ibv.csic.es.
3
Instituto de Biomedicina de Valencia, CSIC, Jaime Roig 11, 46010 Valencia, Spain. jcalvete@ibv.csic.es.
4
Instituto de Biomedicina de Valencia, CSIC, Jaime Roig 11, 46010 Valencia, Spain. dpla@ibv.csic.es.

Abstract

Snake species within genus Bothrops are responsible for more than 80% of the snakebites occurring in South America. The species that cause most envenomings in Argentina, B. diporus, is widely distributed throughout the country, but principally found in the Northeast, the region with the highest rates of snakebites. The venom proteome of this medically relevant snake was unveiled using a venomic approach. It comprises toxins belonging to fourteen protein families, being dominated by PI- and PIII-SVMPs, PLA₂ molecules, BPP-like peptides, L-amino acid oxidase and serine proteinases. This toxin profile largely explains the characteristic pathophysiological effects of bothropic snakebites observed in patients envenomed by B. diporus. Antivenomic analysis of the SAB antivenom (Instituto Vital Brazil) against the venom of B. diporus showed that this pentabothropic antivenom efficiently recognized all the venom proteins and exhibited poor affinity towards the small peptide (BPPs and tripeptide inhibitors of PIII-SVMPs) components of the venom.

KEYWORDS:

Bothrops diporus venom; antivenomics; mass spectrometry; snake venom proteome; venomics

PMID:
26712790
PMCID:
PMC4728531
DOI:
10.3390/toxins8010009
[Indexed for MEDLINE]
Free PMC Article

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