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...

Descripción completa

Detalles Bibliográficos
Autores principales: Degueldre, Michel, Echterbille, Julien, Smargiasso, Nicolas, Damblon, Christian, Gouin, Charlotte, Mourier, Gilles, Gilles, Nicolas, De Pauw, Edwin, Quinton, Loïc
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