| Record |
| Author |
Aili, S.R.; Touchard, A.; Hayward, R.; Robinson, S.D.; Pineda, S.S.; Lalagüe, H.; Mrinalini; Vetter, I.; Undheim, E.A.B.; Kini, R.M.; Escoubas, P.; Padula, M.P.; Myers, G.S.A.; Nicholson, G.M. |
| Title |
An integrated proteomic and transcriptomic analysis reveals the venom complexity of the bullet ant Paraponera clavata |
Type |
Journal Article |
| Year |
2020 |
Publication |
Toxins |
Abbreviated Journal |
Toxins |
| Volume |
12 |
Issue |
5 |
Pages |
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| Keywords |
DRG neurons; Hyaluronidase; Neurotoxins; Paraponeritoxin; Phospholipases; Rp-Hplc; alpha latrotoxin; ant venom; arginine kinase; cathepsin; contig; defensin 2; hyaluronidase; icarapin; metalloproteinase; neurotoxin; novel toxin like protein; phospholipase; phospholipase A2; poneratoxin; proteome; serine proteinase; transcriptome; unclassified drug; amino acid sequence; ant; Article; liquid chromatography-mass spectrometry; neurotoxicity; nonhuman; Paraponera clavata; protein expression; proteomics; sequence database; tandem mass spectrometry; transcriptomics; venom gland |
| Abstract |
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 Paraponera clavata 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. © 2020 by the authors. Licensee MDPI, Basel, Switzerland. |
| Address |
Faculty of Science, University of Nice, Nice, 06000, France |
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| Publisher |
Mdpi Ag |
Place of Publication |
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| ISSN |
20726651 (Issn) |
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| Call Number |
EcoFoG @ webmaster @ |
Serial  |
972 |
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