Cargando…
In-Depth Glyco-Peptidomics Approach Reveals Unexpected Diversity of Glycosylated Peptides and Atypical Post-Translational Modifications in Dendroaspis angusticeps Snake Venom
Animal venoms represent a valuable source of bioactive peptides that can be derived into useful pharmacological tools, or even innovative drugs. In this way, the venom of Dendroaspis angusticeps (DA), the Eastern Green Mamba, has been intensively studied during recent years. It mainly contains hundr...
Autores principales: | , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5713420/ https://www.ncbi.nlm.nih.gov/pubmed/29156586 http://dx.doi.org/10.3390/ijms18112453 |
_version_ | 1783283421578002432 |
---|---|
author | Degueldre, Michel Echterbille, Julien Smargiasso, Nicolas Damblon, Christian Gouin, Charlotte Mourier, Gilles Gilles, Nicolas De Pauw, Edwin Quinton, Loïc |
author_facet | Degueldre, Michel Echterbille, Julien Smargiasso, Nicolas Damblon, Christian Gouin, Charlotte Mourier, Gilles Gilles, Nicolas De Pauw, Edwin Quinton, Loïc |
author_sort | Degueldre, Michel |
collection | PubMed |
description | Animal venoms represent a valuable source of bioactive peptides that can be derived into useful pharmacological tools, or even innovative drugs. In this way, the venom of Dendroaspis angusticeps (DA), the Eastern Green Mamba, has been intensively studied during recent years. It mainly contains hundreds of large toxins from 6 to 9 kDa, each displaying several disulfide bridges. These toxins are the main target of venom-based studies due to their valuable activities obtained by selectively targeting membrane receptors, such as ion channels or G-protein coupled receptors. This study aims to demonstrate that the knowledge of venom composition is still limited and that animal venoms contain unexpected diversity and surprises. A previous study has shown that Dendroaspis angusticeps venom contains not only a cocktail of classical toxins, but also small glycosylated peptides. Following this work, a deep exploration of DA glycopeptidome by a dual nano liquid chromatography coupled to electrospray ionization mass spectrometry (nanoLC-ESI-MS) and Matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS) analyses was initiated. This study reveals unsuspected structural diversity of compounds such as 221 glycopeptides, displaying different glycan structures. Sequence alignments underline structural similarities with natriuretic peptides already characterized in Elapidae venoms. Finally, the presence of an S-cysteinylation and hydroxylation of proline on four glycopeptides, never described to date in snake venoms, is also revealed by proteomics and affined by nuclear magnetic resonance (NMR) experiments. |
format | Online Article Text |
id | pubmed-5713420 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-57134202017-12-07 In-Depth Glyco-Peptidomics Approach Reveals Unexpected Diversity of Glycosylated Peptides and Atypical Post-Translational Modifications in Dendroaspis angusticeps Snake Venom Degueldre, Michel Echterbille, Julien Smargiasso, Nicolas Damblon, Christian Gouin, Charlotte Mourier, Gilles Gilles, Nicolas De Pauw, Edwin Quinton, Loïc Int J Mol Sci Article Animal venoms represent a valuable source of bioactive peptides that can be derived into useful pharmacological tools, or even innovative drugs. In this way, the venom of Dendroaspis angusticeps (DA), the Eastern Green Mamba, has been intensively studied during recent years. It mainly contains hundreds of large toxins from 6 to 9 kDa, each displaying several disulfide bridges. These toxins are the main target of venom-based studies due to their valuable activities obtained by selectively targeting membrane receptors, such as ion channels or G-protein coupled receptors. This study aims to demonstrate that the knowledge of venom composition is still limited and that animal venoms contain unexpected diversity and surprises. A previous study has shown that Dendroaspis angusticeps venom contains not only a cocktail of classical toxins, but also small glycosylated peptides. Following this work, a deep exploration of DA glycopeptidome by a dual nano liquid chromatography coupled to electrospray ionization mass spectrometry (nanoLC-ESI-MS) and Matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS) analyses was initiated. This study reveals unsuspected structural diversity of compounds such as 221 glycopeptides, displaying different glycan structures. Sequence alignments underline structural similarities with natriuretic peptides already characterized in Elapidae venoms. Finally, the presence of an S-cysteinylation and hydroxylation of proline on four glycopeptides, never described to date in snake venoms, is also revealed by proteomics and affined by nuclear magnetic resonance (NMR) experiments. MDPI 2017-11-18 /pmc/articles/PMC5713420/ /pubmed/29156586 http://dx.doi.org/10.3390/ijms18112453 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Degueldre, Michel Echterbille, Julien Smargiasso, Nicolas Damblon, Christian Gouin, Charlotte Mourier, Gilles Gilles, Nicolas De Pauw, Edwin Quinton, Loïc In-Depth Glyco-Peptidomics Approach Reveals Unexpected Diversity of Glycosylated Peptides and Atypical Post-Translational Modifications in Dendroaspis angusticeps Snake Venom |
title | In-Depth Glyco-Peptidomics Approach Reveals Unexpected Diversity of Glycosylated Peptides and Atypical Post-Translational Modifications in Dendroaspis angusticeps Snake Venom |
title_full | In-Depth Glyco-Peptidomics Approach Reveals Unexpected Diversity of Glycosylated Peptides and Atypical Post-Translational Modifications in Dendroaspis angusticeps Snake Venom |
title_fullStr | In-Depth Glyco-Peptidomics Approach Reveals Unexpected Diversity of Glycosylated Peptides and Atypical Post-Translational Modifications in Dendroaspis angusticeps Snake Venom |
title_full_unstemmed | In-Depth Glyco-Peptidomics Approach Reveals Unexpected Diversity of Glycosylated Peptides and Atypical Post-Translational Modifications in Dendroaspis angusticeps Snake Venom |
title_short | In-Depth Glyco-Peptidomics Approach Reveals Unexpected Diversity of Glycosylated Peptides and Atypical Post-Translational Modifications in Dendroaspis angusticeps Snake Venom |
title_sort | in-depth glyco-peptidomics approach reveals unexpected diversity of glycosylated peptides and atypical post-translational modifications in dendroaspis angusticeps snake venom |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5713420/ https://www.ncbi.nlm.nih.gov/pubmed/29156586 http://dx.doi.org/10.3390/ijms18112453 |
work_keys_str_mv | AT degueldremichel indepthglycopeptidomicsapproachrevealsunexpecteddiversityofglycosylatedpeptidesandatypicalposttranslationalmodificationsindendroaspisangusticepssnakevenom AT echterbillejulien indepthglycopeptidomicsapproachrevealsunexpecteddiversityofglycosylatedpeptidesandatypicalposttranslationalmodificationsindendroaspisangusticepssnakevenom AT smargiassonicolas indepthglycopeptidomicsapproachrevealsunexpecteddiversityofglycosylatedpeptidesandatypicalposttranslationalmodificationsindendroaspisangusticepssnakevenom AT damblonchristian indepthglycopeptidomicsapproachrevealsunexpecteddiversityofglycosylatedpeptidesandatypicalposttranslationalmodificationsindendroaspisangusticepssnakevenom AT gouincharlotte indepthglycopeptidomicsapproachrevealsunexpecteddiversityofglycosylatedpeptidesandatypicalposttranslationalmodificationsindendroaspisangusticepssnakevenom AT mouriergilles indepthglycopeptidomicsapproachrevealsunexpecteddiversityofglycosylatedpeptidesandatypicalposttranslationalmodificationsindendroaspisangusticepssnakevenom AT gillesnicolas indepthglycopeptidomicsapproachrevealsunexpecteddiversityofglycosylatedpeptidesandatypicalposttranslationalmodificationsindendroaspisangusticepssnakevenom AT depauwedwin indepthglycopeptidomicsapproachrevealsunexpecteddiversityofglycosylatedpeptidesandatypicalposttranslationalmodificationsindendroaspisangusticepssnakevenom AT quintonloic indepthglycopeptidomicsapproachrevealsunexpecteddiversityofglycosylatedpeptidesandatypicalposttranslationalmodificationsindendroaspisangusticepssnakevenom |