An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant <i>Paraponera clavata</i>

A critical hurdle in ant venom proteomic investigations is the lack of databases to comprehensively and specifically identify the sequence and function of venom proteins and peptides. To resolve this, we used venom gland transcriptomics to generate a sequence database that was used to assign the tan...

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Main Authors: Samira R. Aili, Axel Touchard, Regan Hayward, Samuel D. Robinson, Sandy S. Pineda, Hadrien Lalagüe, Mrinalini Mrinalinie.undheim@uq.edu.au, Irina Vetter, Eivind A. B. Undheim, R. Manjunatha Kini, Pierre Escoubas, Matthew P. Padula, Garry S. A. Myers, Graham M. Nicholson
Format: Article
Language:English
Published: MDPI AG 2020-05-01
Series:Toxins
Subjects:
Online Access:https://www.mdpi.com/2072-6651/12/5/324
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spelling doaj-55d7d69d39f74058b7a192f9f196b6962020-11-25T03:23:39ZengMDPI AGToxins2072-66512020-05-011232432410.3390/toxins12050324An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant <i>Paraponera clavata</i>Samira R. Aili0Axel Touchard1Regan Hayward2Samuel D. Robinson3Sandy S. Pineda4Hadrien Lalagüe5Mrinalini Mrinalinie.undheim@uq.edu.au6Irina Vetter7Eivind A. B. Undheim8R. Manjunatha Kini9Pierre Escoubas10Matthew P. Padula11Garry S. A. Myers12Graham M. Nicholson13School of Life Sciences, University of Technology Sydney, Broadway, NSW 2007, AustraliaCNRS, UMR Ecologie des Forêts de Guyane, AgroParisTech, CIRAD, INRA, Université de Guyane, Université des Antilles, Campus Agronomique, BP316, CEDEX, 97379 Kourou, FranceSchool of Life Sciences, University of Technology Sydney, Broadway, NSW 2007, AustraliaInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072, AustraliaBrain and Mind Centre, University of Sydney, Camperdown, Sydney, NSW 2050, AustraliaCNRS, UMR Ecologie des Forêts de Guyane, AgroParisTech, CIRAD, INRA, Université de Guyane, Université des Antilles, Campus Agronomique, BP316, CEDEX, 97379 Kourou, FranceProtein Science Laboratory, Department of Biological Science, Faculty of Science, National University of Singapore, Singapore 117543, SingaporeInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072, AustraliaCentre for Advanced Imaging, The University of Queensland, St. Lucia, QLD 4072, AustraliaProtein Science Laboratory, Department of Biological Science, Faculty of Science, National University of Singapore, Singapore 117543, SingaporeFaculty of Science, University of Nice, 06000 Nice, FranceSchool of Life Sciences, University of Technology Sydney, Broadway, NSW 2007, AustraliaSchool of Life Sciences, University of Technology Sydney, Broadway, NSW 2007, AustraliaSchool of Life Sciences, University of Technology Sydney, Broadway, NSW 2007, AustraliaA critical hurdle in ant venom proteomic investigations is the lack of databases to comprehensively and specifically identify the sequence and function of venom proteins and peptides. To resolve this, we used venom gland transcriptomics to generate a sequence database that was used to assign the tandem mass spectrometry (MS) fragmentation spectra of venom peptides and proteins to specific transcripts. This was performed alongside a shotgun liquid chromatography–mass spectrometry (LC-MS/MS) analysis of the venom to confirm that these assigned transcripts were expressed as proteins. Through the combined transcriptomic and proteomic investigation of <i>Paraponera clavata </i>venom, we identified four times the number of proteins previously identified using 2D-PAGE alone. In addition to this, by mining the transcriptomic data, we identified several novel peptide sequences for future pharmacological investigations, some of which conform with inhibitor cysteine knot motifs. These types of peptides have the potential to be developed into pharmaceutical or bioinsecticide peptides.https://www.mdpi.com/2072-6651/12/5/324neurotoxinsphospholipaseshyaluronidaseRP-HPLCDRG neuronsparaponeritoxin
collection DOAJ
language English
format Article
sources DOAJ
author Samira R. Aili
Axel Touchard
Regan Hayward
Samuel D. Robinson
Sandy S. Pineda
Hadrien Lalagüe
Mrinalini Mrinalinie.undheim@uq.edu.au
Irina Vetter
Eivind A. B. Undheim
R. Manjunatha Kini
Pierre Escoubas
Matthew P. Padula
Garry S. A. Myers
Graham M. Nicholson
spellingShingle Samira R. Aili
Axel Touchard
Regan Hayward
Samuel D. Robinson
Sandy S. Pineda
Hadrien Lalagüe
Mrinalini Mrinalinie.undheim@uq.edu.au
Irina Vetter
Eivind A. B. Undheim
R. Manjunatha Kini
Pierre Escoubas
Matthew P. Padula
Garry S. A. Myers
Graham M. Nicholson
An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant <i>Paraponera clavata</i>
Toxins
neurotoxins
phospholipases
hyaluronidase
RP-HPLC
DRG neurons
paraponeritoxin
author_facet Samira R. Aili
Axel Touchard
Regan Hayward
Samuel D. Robinson
Sandy S. Pineda
Hadrien Lalagüe
Mrinalini Mrinalinie.undheim@uq.edu.au
Irina Vetter
Eivind A. B. Undheim
R. Manjunatha Kini
Pierre Escoubas
Matthew P. Padula
Garry S. A. Myers
Graham M. Nicholson
author_sort Samira R. Aili
title An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant <i>Paraponera clavata</i>
title_short An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant <i>Paraponera clavata</i>
title_full An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant <i>Paraponera clavata</i>
title_fullStr An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant <i>Paraponera clavata</i>
title_full_unstemmed An Integrated Proteomic and Transcriptomic Analysis Reveals the Venom Complexity of the Bullet Ant <i>Paraponera clavata</i>
title_sort integrated proteomic and transcriptomic analysis reveals the venom complexity of the bullet ant <i>paraponera clavata</i>
publisher MDPI AG
series Toxins
issn 2072-6651
publishDate 2020-05-01
description A critical hurdle in ant venom proteomic investigations is the lack of databases to comprehensively and specifically identify the sequence and function of venom proteins and peptides. To resolve this, we used venom gland transcriptomics to generate a sequence database that was used to assign the tandem mass spectrometry (MS) fragmentation spectra of venom peptides and proteins to specific transcripts. This was performed alongside a shotgun liquid chromatography–mass spectrometry (LC-MS/MS) analysis of the venom to confirm that these assigned transcripts were expressed as proteins. Through the combined transcriptomic and proteomic investigation of <i>Paraponera clavata </i>venom, we identified four times the number of proteins previously identified using 2D-PAGE alone. In addition to this, by mining the transcriptomic data, we identified several novel peptide sequences for future pharmacological investigations, some of which conform with inhibitor cysteine knot motifs. These types of peptides have the potential to be developed into pharmaceutical or bioinsecticide peptides.
topic neurotoxins
phospholipases
hyaluronidase
RP-HPLC
DRG neurons
paraponeritoxin
url https://www.mdpi.com/2072-6651/12/5/324
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