Snake Venomics of the Lesser Antillean Pit Vipers Bothrops caribbaeus and Bothrops lanceolatus: Correlation with Toxicological Activities and Immunoreactivity of a Heterologous Antivenom
Fecha
2008-10
Tipo
artículo original
Autores
Gutiérrez, José María
Sanz, Libia
Escolano, José
Fernández Ulate, Julián
Lomonte, Bruno
Angulo Ugalde, Yamileth
Rucavado Romero, Alexandra
Warrell, David A.
Calvete Chornet, Juan José
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Resumen
The venom proteomes of the snakes Bothrops caribbaeus and Bothrops lanceolatus, endemic to the
Lesser Antillean islands of Saint Lucia and Martinique, respectively, were characterized by reversephase
HPLC fractionation, followed by analysis of each chromatographic fraction by SDS-PAGE,
N-terminal sequencing, MALDI-TOF mass fingerprinting, and collision-induced dissociation tandem mass
spectrometry of tryptic peptides. The venoms contain proteins belonging to seven (B. caribbaeus) and
five (B. lanceolatus) types of toxins. B. caribbaeus and B. lanceolatus venoms contain phospholipases
A2, serine proteinases, L-amino acid oxidases and zinc-dependent metalloproteinases, whereas a long
disintegrin, DC-fragments and a CRISP molecule were present only in the venom of B. caribbaeus, and
a C-type lectin-like molecule was characterized in the venom of B. lanceolatus. Compositional differences
between venoms among closely related species from different geographic regions may be due to
evolutionary environmental pressure acting on isolated populations. The venoms of these two species
differed in the composition and the relative abundance of their component toxins, but they exhibited
similar toxicological and enzymatic profiles in mice, characterized by lethal, hemorrhagic, edemaforming,
phospholipase A2 and proteolytic activities. The venoms of B. caribbaeus and B. lanceolatus
are devoid of coagulant and defibrinogenating effects and induce only mild local myotoxicity in mice.
The characteristic thrombotic effect described in human envenomings by these species was not
reproduced in the mouse model. The toxicological profile observed is consistent with the abundance
of metalloproteinases, PLA2s and serine proteinases in the venoms. A polyvalent (Crotalinae) antivenom
produced in Costa Rica was able to immunodeplete ∼80% of the proteins from both B. caribbaeus and
B. lanceolatus venoms, and was effective in neutralizing the lethal, hemorrhagic, phospholipase A2
and proteolytic activities of these venoms
Descripción
Palabras clave
Bothrops Caribbaeus, Bothrops lanceolatus, Saint Lucia lancehead viper, Fer-de-lance pitviper, Immunodepletion, Mass spectrometry, N-terminal Sequencing, Polyvalent (Crotalinae) Antivenom, Proteomics, Snake venom protein families, Snake venomics, viperid toxins, Snake venom