Author | Rocha, Surza L. G. | |
Author | Ferreira, Ana G. C. Neves | |
Author | Trugilho, Monique R. O. | |
Author | Angulo, Yamileth | |
Author | Lomonte, Bruno | |
Author | Valente, Richard H. | |
Author | Domont, Gilberto B. | |
Author | Perales, Jonas | |
Access date | 2017-11-28T14:26:25Z | |
Available date | 2017-11-28T14:26:25Z | |
Document date | 2017 | |
Citation | ROCHA, Surza L. G. et al. Screening for target toxins of the antiophidic protein DM64 through a gel-based interactomics approach. Journal of Proteomics, v.151, p.204-213, 2017. | pt_BR |
ISSN | 1874-3919 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/23422 | |
Language | eng | pt_BR |
Publisher | Elsevier | pt_BR |
Rights | restricted access | |
Subject in Portuguese | Venenos de Serpentes | pt_BR |
Subject in Portuguese | Proteômica | pt_BR |
Subject in Portuguese | Miotoxina | pt_BR |
Subject in Portuguese | Inibidor de miotoxina | pt_BR |
Subject in Portuguese | Didelphis aurita | pt_BR |
Title | Screening for target toxins of the antiophidic protein DM64 through a gel-based interactomics approach | pt_BR |
Type | Article | |
DOI | 10.1016/j.jprot.2016.05.020 | |
Abstract | DM64 is a glycosylated protein with antivenom activity isolated from the serum of the opossum Didelphis aurita. It binds non-covalently to myotoxins I (Asp49) and II (Lys49) from Bothrops asper venom and inhibits their myotoxic effect. In this study, an affinity column with immobilized DM64 as bait was used to fish potential target toxins. All ten isolated myotoxins tested were able to effectively bind to the DM64 column. To better access the specificity of the inhibitor, crude venoms from Bothrops (8 species), Crotalus (2 species) and Naja naja atra were submitted to the affinity purification. Venom fractions bound and nonbound to the DM64 column were analyzed by two-dimensional gel electrophoresis and MALDI-TOF/TOF MS. Although venom fractions bound to the column were mainly composed of basic PLA2, a few spots corresponding to acidic PLA2 were also observed. Some unexpected protein spots were also identified: C-type lectins and CRISP may represent putative new targets for DM64, whereas the presence of serine peptidases in the venom bound fraction is likely a consequence of nonspecific binding to the column matrix. The present results contribute to better delineate the inhibitory potential of DM64, providing a framework for the development of more specific antivenom therapies. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil. | pt_BR |
Affilliation | Universidad de Costa Rica. Facultad de Microbiologia. Instituto Clodomiro Picado. San José, Costa Rica. | pt_BR |
Affilliation | Universidad de Costa Rica. Facultad de Microbiologia. Instituto Clodomiro Picado. San José, Costa Rica. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro, Instituto de Química. Departamento de Bioquímica. Laboratório de Química de Proteínas/ Unidade Proteômica. Rio de Janeiro, RJ, Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil. | pt_BR |
Subject | Snake venoms | pt_BR |
Subject | Myotoxin | pt_BR |
Subject | Myotoxin inhibitor | pt_BR |
Subject | Didelphis aurita | pt_BR |
Subject | Proteomics | pt_BR |
Subject | Interactomics | pt_BR |
e-ISSN | 1876-7737 | |
Embargo date | 2030-01-01 | |