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Título

Exploring the Venom Proteome of the Western Diamondback Rattlesnake, Crotalus atrox, via Snake Venomics and Combinatorial Peptide Ligand Library Approaches

AutorCalvete, Juan J. ; Fasoli, Elisa; Sanz, Libia ; Boschetti, Egisto; Righetti, Pier Giorgio
Palabras claveCrotalus atrox
Western diamond rattlesnake
Snake venomics
Venom proteome
Viperid toxins
N-terminal sequencing
Mass spectrometry
Low-abundance proteins
Combinatorial peptide ligand library
Peroxiredoxin
Glutaminyl cyclase
Fecha de publicación17-abr-2009
EditorAmerican Chemical Society
CitaciónJournal of Proteome Research 8(6): 3055-3067 (2009)
ResumenWe report the proteomic characterization of the venom of the medically important North American western diamondback rattlesnake, Crotalus atrox, using two complementary approaches: snake venomics (to gain an insight of the overall venom proteome), and two solid-phase combinatorial peptide ligand libraries (CPLL), followed by 2D electrophoresis and mass spectrometric characterization of in-gel digested protein bands (to capture and “amplify“ low-abundance proteins). The venomics approach revealed 24 distinct proteins belonging to 2 major protein families (snake venom metalloproteinases, SVMP, and serine proteinases), which represent 69.5% of the total venom proteins, 4 medium abundance families (medium-size disintegrin, PLA2, cysteine-rich secretory protein, and l-amino acid oxidase) amounting to 25.8% of the venom proteins, and 3 minor protein families (vasoactive peptides, endogenous inhibitor of SVMP, and C-type lectin-like). This toxin profile potentially explains the cytotoxic, myotoxic, hemotoxic, and hemorrhagic effects evoked by C. atrox envenomation. Further, our results showing that C. atrox exhibits a similar level of venom variation as Sistrurus miliarius points to a ”diversity gain” scenario in the lineage leading to the Sistrurus catenatus taxa. On the other hand, the two combinatorial hexapeptide libraries captured distinct sets of proteins. Although the CPLL-treated samples did not retain a representative venom proteome, protein spots barely, or not at all, detectable in the whole venom were enriched in the two CPLL-treated samples. The amplified low copy number C. atrox venom proteins comprised a C-type lectin-like protein, several PLA2 molecules, PIII-SVMP isoforms, glutaminyl cyclase isoforms, and a 2-cys peroxiredoxin highly conserved across the animal kingdom. Peroxiredoxin and glutaminyl cyclase may participate, respectively, in redox processes leading to the structural/functional diversification of toxins, and in the N-terminal pyrrolidone carboxylic acid formation required in the maturation of bioactive peptides such as bradykinin-potentiating peptides and endogenous inhibitors of metalloproteases. Our findings underscore the usefulness of combinatorial peptide libraries as powerful tools for mining below the tip of the iceberg, complementing thereby the data gained using the snake venomics protocol toward a complete visualization of the venom proteome.
Descripción13 pages, 5 figures, 3 tables.-- PMID: 19371136 [PubMed].-- Printed version published Jun 5, 2009.
Versión del editorhttp://dx.doi.org/10.1021/pr900249q
URIhttp://hdl.handle.net/10261/13848
DOI10.1021/pr900249q
ISSN1535-3893
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