Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.jprot.2017.09.006 http://hdl.handle.net/11449/175179 |
Resumo: | Many scorpion accidents occur in the Brazilian Amazonian region and are frequently caused by Tityus obscurus. Approximately 5% of the crude venom of this species is composed of short linear, non-disulfide-bridged peptides, which have not been intensively investigated. As a consequence, only a few of these peptides have been structurally and functionally characterized to date. In the present paper, the peptide fraction of the venom was subjected to peptide profiling using an LCMS-IT-TOF/MS and MSn system. The analysis detected 320 non-disulfide bond-containing peptides (NDBPs), of which twenty-seven had their sequences assigned; among them, thirteen peptides were characterized, constituting novel toxins in T. obscurus venom. Some of the novel peptides showed similarities to hypotensin-like toxins, while other peptides appear to be natural fragments of neurotoxins. The novel peptides were submitted to a series of bioassays, revealing that many are multifunctional toxins that cause, for example, pain, edema formation and hemolysis to potentiate strong inflammatory processes and alterations in the locomotion and lifting activities in the victims of stinging. Knowledge of the complex matrix of peptides composing the venom of T. obscurus will contribute to better understanding of the complex mechanism of envenoming caused by stinging accidents. Significance The scorpion Tityus obscurus causes many envenoming accidents of medical importance in Brazilian Amazon region; despite to this, very few is known about the toxinology of this animal. The knowledge about the venom composition and mechanisms of action is very important to understand the physiopathology processes related to the envenoming caused by this animal. The proteopeptidomic investigations of scorpion venoms in general have focused mainly the neurotoxins (which are disulfide bonds containing peptides) and large proteins. The short, linear, non-disulfide bonds containing peptides (NDBPs) represent up to 5% of scorpion venom compositions; however, they have been few investigated in comparison with the neurotoxins. The present study used a mass spectrometric approach to detect 320 NDBPs and to sequence 27 of them; pharmacological assays permitted to characterize 13 NDBPs as novel toxins involved with inflammation, pain and edema formation. |
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Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurusESI-IT-TOF/MSLCMSPeptide toxinPeptidomicsScorpionTityus obscurusVenomicsMany scorpion accidents occur in the Brazilian Amazonian region and are frequently caused by Tityus obscurus. Approximately 5% of the crude venom of this species is composed of short linear, non-disulfide-bridged peptides, which have not been intensively investigated. As a consequence, only a few of these peptides have been structurally and functionally characterized to date. In the present paper, the peptide fraction of the venom was subjected to peptide profiling using an LCMS-IT-TOF/MS and MSn system. The analysis detected 320 non-disulfide bond-containing peptides (NDBPs), of which twenty-seven had their sequences assigned; among them, thirteen peptides were characterized, constituting novel toxins in T. obscurus venom. Some of the novel peptides showed similarities to hypotensin-like toxins, while other peptides appear to be natural fragments of neurotoxins. The novel peptides were submitted to a series of bioassays, revealing that many are multifunctional toxins that cause, for example, pain, edema formation and hemolysis to potentiate strong inflammatory processes and alterations in the locomotion and lifting activities in the victims of stinging. Knowledge of the complex matrix of peptides composing the venom of T. obscurus will contribute to better understanding of the complex mechanism of envenoming caused by stinging accidents. Significance The scorpion Tityus obscurus causes many envenoming accidents of medical importance in Brazilian Amazon region; despite to this, very few is known about the toxinology of this animal. The knowledge about the venom composition and mechanisms of action is very important to understand the physiopathology processes related to the envenoming caused by this animal. The proteopeptidomic investigations of scorpion venoms in general have focused mainly the neurotoxins (which are disulfide bonds containing peptides) and large proteins. The short, linear, non-disulfide bonds containing peptides (NDBPs) represent up to 5% of scorpion venom compositions; however, they have been few investigated in comparison with the neurotoxins. The present study used a mass spectrometric approach to detect 320 NDBPs and to sequence 27 of them; pharmacological assays permitted to characterize 13 NDBPs as novel toxins involved with inflammation, pain and edema formation.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Dept. Biology/CEIS Institute of Biosciences of Rio Claro University of São Paulo State (UNESP)Laboratory of Biological Research Amazon College/Amazon University UNAMALaboratory of Pharmacology Butantan InstituteDept. Biology/CEIS Institute of Biosciences of Rio Claro University of São Paulo State (UNESP)FAPESP: 2011/51684-1Universidade Estadual Paulista (Unesp)Amazon College/Amazon University UNAMAButantan InstituteDias, Nathalia Baptista [UNESP]de Souza, Bibiana Monson [UNESP]Cocchi, Fernando Kamimura [UNESP]Chalkidis, Hipócrates M.Dorce, Valquíria Abrão CoronadoPalma, Mario Sergio [UNESP]2018-12-11T17:14:43Z2018-12-11T17:14:43Z2018-01-06info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article70-79application/pdfhttp://dx.doi.org/10.1016/j.jprot.2017.09.006Journal of Proteomics, v. 170, p. 70-79.1876-77371874-3919http://hdl.handle.net/11449/17517910.1016/j.jprot.2017.09.0062-s2.0-850295650442-s2.0-85029565044.pdf2901888624506535Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Proteomics1,430info:eu-repo/semantics/openAccess2023-12-19T06:24:35Zoai:repositorio.unesp.br:11449/175179Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-12-19T06:24:35Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus |
title |
Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus |
spellingShingle |
Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus Dias, Nathalia Baptista [UNESP] ESI-IT-TOF/MS LCMS Peptide toxin Peptidomics Scorpion Tityus obscurus Venomics |
title_short |
Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus |
title_full |
Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus |
title_fullStr |
Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus |
title_full_unstemmed |
Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus |
title_sort |
Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus |
author |
Dias, Nathalia Baptista [UNESP] |
author_facet |
Dias, Nathalia Baptista [UNESP] de Souza, Bibiana Monson [UNESP] Cocchi, Fernando Kamimura [UNESP] Chalkidis, Hipócrates M. Dorce, Valquíria Abrão Coronado Palma, Mario Sergio [UNESP] |
author_role |
author |
author2 |
de Souza, Bibiana Monson [UNESP] Cocchi, Fernando Kamimura [UNESP] Chalkidis, Hipócrates M. Dorce, Valquíria Abrão Coronado Palma, Mario Sergio [UNESP] |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Amazon College/Amazon University UNAMA Butantan Institute |
dc.contributor.author.fl_str_mv |
Dias, Nathalia Baptista [UNESP] de Souza, Bibiana Monson [UNESP] Cocchi, Fernando Kamimura [UNESP] Chalkidis, Hipócrates M. Dorce, Valquíria Abrão Coronado Palma, Mario Sergio [UNESP] |
dc.subject.por.fl_str_mv |
ESI-IT-TOF/MS LCMS Peptide toxin Peptidomics Scorpion Tityus obscurus Venomics |
topic |
ESI-IT-TOF/MS LCMS Peptide toxin Peptidomics Scorpion Tityus obscurus Venomics |
description |
Many scorpion accidents occur in the Brazilian Amazonian region and are frequently caused by Tityus obscurus. Approximately 5% of the crude venom of this species is composed of short linear, non-disulfide-bridged peptides, which have not been intensively investigated. As a consequence, only a few of these peptides have been structurally and functionally characterized to date. In the present paper, the peptide fraction of the venom was subjected to peptide profiling using an LCMS-IT-TOF/MS and MSn system. The analysis detected 320 non-disulfide bond-containing peptides (NDBPs), of which twenty-seven had their sequences assigned; among them, thirteen peptides were characterized, constituting novel toxins in T. obscurus venom. Some of the novel peptides showed similarities to hypotensin-like toxins, while other peptides appear to be natural fragments of neurotoxins. The novel peptides were submitted to a series of bioassays, revealing that many are multifunctional toxins that cause, for example, pain, edema formation and hemolysis to potentiate strong inflammatory processes and alterations in the locomotion and lifting activities in the victims of stinging. Knowledge of the complex matrix of peptides composing the venom of T. obscurus will contribute to better understanding of the complex mechanism of envenoming caused by stinging accidents. Significance The scorpion Tityus obscurus causes many envenoming accidents of medical importance in Brazilian Amazon region; despite to this, very few is known about the toxinology of this animal. The knowledge about the venom composition and mechanisms of action is very important to understand the physiopathology processes related to the envenoming caused by this animal. The proteopeptidomic investigations of scorpion venoms in general have focused mainly the neurotoxins (which are disulfide bonds containing peptides) and large proteins. The short, linear, non-disulfide bonds containing peptides (NDBPs) represent up to 5% of scorpion venom compositions; however, they have been few investigated in comparison with the neurotoxins. The present study used a mass spectrometric approach to detect 320 NDBPs and to sequence 27 of them; pharmacological assays permitted to characterize 13 NDBPs as novel toxins involved with inflammation, pain and edema formation. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-12-11T17:14:43Z 2018-12-11T17:14:43Z 2018-01-06 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.jprot.2017.09.006 Journal of Proteomics, v. 170, p. 70-79. 1876-7737 1874-3919 http://hdl.handle.net/11449/175179 10.1016/j.jprot.2017.09.006 2-s2.0-85029565044 2-s2.0-85029565044.pdf 2901888624506535 |
url |
http://dx.doi.org/10.1016/j.jprot.2017.09.006 http://hdl.handle.net/11449/175179 |
identifier_str_mv |
Journal of Proteomics, v. 170, p. 70-79. 1876-7737 1874-3919 10.1016/j.jprot.2017.09.006 2-s2.0-85029565044 2-s2.0-85029565044.pdf 2901888624506535 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Proteomics 1,430 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
70-79 application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1803047021617086464 |