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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.)

The distinct N-terminomes of Bothrops jararaca newborn and adult venoms

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Author(s):
Andrade-Silva, Debora [1] ; Nishiyama Jr, Milton Y. ; Stuginski, Daniel R. [2] ; Zelanis, Andre [3] ; Serrano, Solange M. T. [4]
Total Authors: 5
Affiliation:
[1] Inst Butantan, Ctr Toxins Immune Response & Cell Signaling CeTIC, Lab Toxinol Aplicada, Av Vital Brasil 1500, BR-05503000 Sao Paulo, SP - Brazil
[2] Inst Butantan, Lab Herpetol, Sao Paulo, SP - Brazil
[3] Univ Fed Sao Paulo, Dept Sci & Technol, Funct Prote Lab, ICT UNIFESP, Sao Jose Dos Campos, SP - Brazil
[4] Nishiyama Jr, Jr., Milton Y., Inst Butantan, Ctr Toxins Immune Response & Cell Signaling CeTIC, Lab Toxinol Aplicada, Av Vital Brasil 1500, BR-05503000 Sao Paulo, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS; v. 1869, n. 7 JUL 2021.
Web of Science Citations: 0
Abstract

Using approaches of transcriptomics and proteomics we have shown that the phenotype of Bothrops jararaca venom undergoes a significant rearrangement upon neonate to adult transition. Most regulatory processes in biology are intrinsically related to modifications of protein structure, function, and abundance. However, it is unclear to which extent intrinsic proteolysis affects toxins and snake venom phenotypes upon ontogenesis. Here we assessed the natural N-terminome of Bothrops jararaca newborn and adult venoms and explored the degree of N-terminal protein truncation in ontogenetic-based proteome variation. To this end we applied the Terminal Amine Isotopic Labeling of Substrates (TAILS) technology to characterize venom collected in the presence of proteinase inhibitors. We identified natural N-terminal sequences in the newborn (71) and adult (84) venoms, from which only 37 were common to both. However, truncated toxins were found in higher number in the newborn (212) than in the adult (140) venom. Moreover, sequences N-terminally blocked by pyroglutamic acid were identified in the newborn (55) and adult (49) venoms. Most toxin classes identified by their natural N-terminal sequences showed a similar number of unique peptides in the newborn and adult venoms, however, those of serine proteinases and C-type lectins were more abundant in the adult venom. Truncated sequences from at least ten toxin classes were detected, however the catalytic and cysteine-rich domains of metalloproteinases were the most prone to proteolysis, mainly in the newborn venom. Our results underscore the pervasiveness of truncations in most toxin classes and highlight variable post-translational events in newborn and adult venoms. (AU)

FAPESP's process: 16/16935-7 - A post-translational modification perspective of Bothrops venom toxins: site-specific proteomic characterization of N-glycans and Cys residues.
Grantee:Débora Andrade Silva
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 13/14651-3 - Experimental approaches in proteomics and glycomics applied to the characterization of Bothrops alcatraz
Grantee:Débora Andrade Silva
Support Opportunities: Scholarships in Brazil - Master