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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.)

Comparative analysis of the high molecular mass subproteomes of eight Bothrops snake venoms

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Author(s):
Gren, Eric C. K. [1, 2, 3, 4] ; Kitano, Eduardo S. [1] ; Andrade-Silva, Debora [1] ; Iwai, Leo Kei [1] ; Reis, Marcelo S. [5] ; Menezes, Milene C. [1] ; Serrano, Solange M. T. [1]
Total Authors: 7
Affiliation:
[1] Inst Butantan, Ctr Toxins Immune Response & Cell Signaling CeTIC, Lab Especial Toxinol Aplicada, Sao Paulo - Brazil
[2] Loma Linda Univ, Ctr Environm Studies & Stewardship, Loma Linda, CA 92350 - USA
[3] Bitterroot Community Sci Ctr, Hamilton, MT - USA
[4] Asclepius Snakebite Fdn, Seattle, WA - USA
[5] Inst Butantan, Ctr Toxins Immune Response & Cell Signaling CeTIC, Lab Especial Ciclo Celular, Sao Paulo - Brazil
Total Affiliations: 5
Document type: Journal article
Source: Comparative Biochemistry and Physiology D-Genomics & Proteomics; v. 30, p. 113-121, JUN 2019.
Web of Science Citations: 0
Abstract

Snake venoms are extremely active biological secretions composed primarily of various classes of enzymes. The genus Bothrops comprises various pit viper species that represent the most medically significant taxa in Central and South America, accounting for more human envenomations and fatalities than any other snakes in the region. Venom proteomes of many Bothrops species have been well-characterized but investigations have focused almost exclusively on proteins smaller than 100 kDa despite expression of larger components being documented in several Bothrops venoms. This study sought to achieve detailed identification of major components in the high molecular mass subproteome of venoms from eight Bothrops species (B. brazili, B. cotiara, B. insularis, B. jararaca, B. jararacussu, B. leucurus, B. moojeni and B. neuwiedi). Enzymes such as metalloproteinases and L-amino acid oxidases were the most prominent components identified in the first size-exclusion chromatography fractions of these venoms. Minor components also identified in the first peaks included 5'-nucleotidase, aminopeptidase, phosphodiesterase, and phospholipases A(2) and B. Most of these components disappeared in electrophoretic profiles under reducing conditions, suggesting that they may be composed of more than one polypeptide chain. A significant shift in the molecular masses of these protein bands was observed following enzymatic N-deglycosylation, indicating that they may contain N-glycans. Furthermore, none of the identified high molecular mass proteins were shared by all eight species, revealing a high level of interspecific variability among these venom components. (AU)

FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 15/01234-0 - Proteolytic enzymes from snake venoms trigger cascades of yet unknown molecular events
Grantee:Eric Conrad Kyle Gren
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 13/13548-4 - Proteomic/Glycoproteomic characterization of the venoms of the Bothrops jararaca complex with emphasis on the N-terminome and N-glycome of toxins
Grantee:Solange Maria de Toledo Serrano
Support type: Regular Research Grants