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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Venom proteomes of South and North American opisthoglyphous (Colubridae and Dipsadidae) snake species: A preliminary approach to understanding their biological roles

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Author(s):
Peichoto, Maria E. [1, 2, 3] ; Tavares, Flavio L. [3, 4] ; Santoro, Marcelo L. [2] ; Mackessy, Stephen P. [3]
Total Authors: 4
Affiliation:
[1] Inst Nacl Med Trop INMeT, RA-3370 Puerto Iguazu - Argentina
[2] Inst Butantan, Lab Fisiopatol, BR-05503900 Sao Paulo - Brazil
[3] Univ No Colorado, Sch Biol Sci, Greeley, CO 80639 - USA
[4] Uniao Dinam Cataratas, BR-85852010 Foz Do Iguacu, PR - Brazil
Total Affiliations: 4
Document type: Journal article
Source: Comparative Biochemistry and Physiology D-Genomics & Proteomics; v. 7, n. 4, p. 361-369, DEC 2012.
Web of Science Citations: 26
Abstract

Opisthoglyphous snake venoms remain under-explored despite being promising sources for ecological, evolutionary and biomedical/biotechnological research. Herein, we compared the protein composition and enzymatic properties of the venoms of Philodryas baroni (PbV), Philodryas olfersii olfersii (PooV) and Philodryas patagoniensis (PpV) from South America, and Hypsiglena torquata texana (HttV) and Trimorphodon biscutatus lambda (TbIV) from North America. All venoms degraded azocasein, and this metalloproteinase activity was significantly inhibited by EDTA. PooV exhibited the highest level of catalytic activity towards synthetic substrates for serine proteinases. All venoms hydrolyzed acetylthiocholine at low levels, and only TbIV showed phospholipase A(2) activity. 1D and 2D SOS-PAGE profile comparisons demonstrated species-specific components as well as several shared components. Size exclusion chromatograms from the three Philodryas venoms and HttV were similar, but TbIV showed a notably different pattern. MALDI-TOF MS of crude venoms revealed as many as 49 distinct protein masses, assigned to six protein families. MALDI-TOF/TOF MS analysis of tryptic peptides confirmed the presence of cysteine-rich secretory proteins in all venoms, as well as a phospholipase A(2) and a three-finger toxin in TbIV. Broad patterns of protein composition appear to follow phylogenetic lines, with finer scale variation likely influenced by ecological factors such as diet and habitat. (C) 2012 Elsevier Inc. All rights reserved. (AU)

FAPESP's process: 10/08162-1 - Contribution of local injury evoked by Bothrops jararaca snake venom to the genesis of systemic hemostatic disturbances
Grantee:Marcelo Larami Santoro
Support Opportunities: Regular Research Grants