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.
Toxins 2020, 12(5), 324
DOI: 10.3390/toxins12050324
Published: 14 May 2020
Publication webpage.
Samira R. Aili, Axel Touchard, Regan Hayward, Samuel D. Robinson, Sandy S. Pineda, Hadrien Lalagüe, Mrinalini, Irina Vetter, Eivind A. B. Undheim*, R. Manjunatha Kini, Pierre Escoubas, Matthew P. Padula, Garry S. A. Myers, and Graham M. Nicholson in Toxins.
* Centre for Ecological and Evolutionary Synthesis (CEES), Department of Biosciences, University of Oslo, Oslo, Norway. See the publication webpage for full author information.