Bothrops jararaca venom proteome rearrangement upon neonate to adult transition

Proteomics - Tập 11 Số 21 - Trang 4218-4228 - 2011
André Zelanis1,2, Alexandre K. Tashima3,2, Antônio F. M. Pinto4, Adriana Franco Paes Leme5, Daniel Rodrigues Stuginski6, Maria F. Furtado6, Nicholas E. Sherman7, Paulo Lee Ho8,1, Jay W. Fox7, Solange M.T. Serrano1,2
1Instituto de Química, Departamento de Bioquímica, Universidade de São Paulo, Brazil
2Laboratório Especial de Toxinologia Aplicada-CAT/cepid, Instituto Butantan, Brazil
3Departamento de Ciências Exatas e da Terra, Universidade Federal de São Paulo, Brazil
4Laboratório de Bioquímica Farmacológica, Centro de Biotecnologia (UFRGS), Porto Alegre, Brazil
5Laboratório Nacional de Biociências (LNBio), Campinas, Brazil
6Laboratório de Herpetologia, Instituto Butantan, Brazil
7Department of Microbiology, University of Virginia, Charlottesville, USA
8Centro de Biotecnologia, Instituto Butantan, Brazil

Tóm tắt

AbstractThe pharmacological activities displayed by Bothrops jararaca venom undergo a significant ontogenetic shift. Similarly, the diet of this species changes from ectothermic prey in early life to endothermic prey in adulthood. In this study we used large and representative newborn and adult venom samples consisting of pools from 694 and 110 specimens, respectively, and demonstrate a significant ontogenetic shift in the venom proteome complexity of B. jararaca. 2‐DE coupled to MS protein identification showed a clear rearrangement of the toxin arsenal both in terms of the total proteome, as of the glycoproteome. N‐glycosylation seems to play a key role in venom protein variability between newborn and adult specimens. Upon the snake development, the subproteome of metalloproteinases undergoes a shift from a P‐III‐rich to a P‐I‐rich profile while the serine proteinase profile does not vary significantly. We also used isobaric tag labeling (iTRAQ) of venom tryptic peptides for the first time to examine the quantitative changes in the venom toxins of B. jararaca upon neonate to adult transition. The iTRAQ analysis showed changes in various toxin classes, especially the proteinases. Our study expands the in‐depth understanding of venom complexity variation particularly with regard to toxin families that have been associated with envenomation pathogenesis.

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Proteomics

Tập 11 Số 21

4218-4228

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