J Proteomics. 2014 Jun 13;105:323-39. doi: 10.1016/j.jprot.2014.02.020. Epub 2014 Feb 24.
Abstract
In spite of its small territory of ~50,000km(2), Costa Rica harbors a remarkably rich biodiversity. Its herpetofauna includes 138 species of snakes, of which sixteen pit vipers (family Viperidae, subfamily Crotalinae), five coral snakes
(family Elapidae, subfamily Elapinae), and one sea snake (Family
Elapidae, subfamily Hydrophiinae) pose potential hazards to human and
animal health. In recent years, knowledge on the composition of snake
venoms has expanded dramatically thanks to the development of
increasingly fast and sensitive analytical techniques in mass
spectrometry and separation science applied to protein characterization.
Among several analytical strategies to determine the overall
protein/peptide composition of snake venoms, the methodology known as
'snake venomics' has proven particularly well suited and informative, by
providing not only a catalog of protein types/families present in a
venom, but also a semi-quantitative estimation of their relative
abundances. Through a collaborative research initiative between
Instituto de Biomedicina de Valencia (IBV) and Instituto Clodomiro
Picado (ICP), this strategy has been applied to the study of venoms of Costa Rican snakes,
aiming to obtain a deeper knowledge on their composition, geographic
and ontogenic variations, relationships to taxonomy, correlation with
toxic activities, and discovery of novel components. The proteomic
profiles of venoms from sixteen out of the 22 species within the
Viperidae and Elapidae families found in Costa Rica
have been reported so far, and an integrative view of these studies is
hereby presented. In line with other venomic projects by research groups
focusing on a wide variety of snakes
around the world, these studies contribute to a deeper understanding of
the biochemical basis for the diverse toxic profiles evolved by venomous snakes.
In addition, these studies provide opportunities to identify novel
molecules of potential pharmacological interest. Furthermore, the
establishment of venom proteomic profiles offers a fundamental platform
to assess the detailed immunorecognition of individual proteins/peptides
by therapeutic or experimental antivenoms, an evolving methodology for
which the term 'antivenomics' was coined (as described in an
accompanying paper in this special issue).
BIOLOGICAL SIGNIFICANCE:
Venoms
represent an adaptive trait and an example of both divergent and
convergent evolution. A deep understanding of the composition of venoms
and of the principles governing the evolution of venomous
systems is of applied importance for exploring the enormous potential
of venoms as sources of chemical and pharmacological novelty but also to
fight the consequences of snakebite envenomings. Key to this is the
identification of evolutionary and ecological trends at different
taxonomical levels. However, the evolution of venomous
species and their venoms do not always follow the same course, and the
identification of structural and functional convergences and divergences
among venoms is often unpredictable by a phylogenetic hypothesis. Snake
venomics is a proteomic-centered strategy to deconstruct the complex
molecular phenotypes the venom proteomes. The proteomic profiles of
venoms from sixteen out of the 22 venomous species within the Viperidae and Elapidae families found in Costa Rica
have been completed so far. An integrative view of their venom
composition, including the identification of geographic and ontogenic
variations, is hereby presented. Venom proteomic profiles offer a
fundamental platform to assess the detailed immunorecognition of
individual venom components by therapeutic or experimental antivenoms.
This aspect is reviewed in the companion paper. This article is part of a
Special Issue entitled: Proteomics of non-model organisms.
Copyright © 2014 Elsevier B.V. All rights reserved.
KEYWORDS:
Costa Rica; Elapidae; Proteomics; Snake venom; Venomics; Viperidae
