TY  - JOUR
AU  - Aili, S.R.
AU  - Touchard, A.
AU  - Hayward, R.
AU  - Robinson, S.D.
AU  - Pineda, S.S.
AU  - Lalagüe, H.
AU  - Mrinalini
AU  - Vetter, I.
AU  - Undheim, E.A.B.
AU  - Kini, R.M.
AU  - Escoubas, P.
AU  - Padula, M.P.
AU  - Myers, G.S.A.
AU  - Nicholson, G.M.
PY  - 2020//
TI  - An integrated proteomic and transcriptomic analysis reveals the venom complexity of the bullet ant Paraponera clavata
T2  - Toxins
JO  - Toxins
VL  - 12
IS  - 5
PB  - Mdpi Ag
KW  - DRG neurons
KW  - Hyaluronidase
KW  - Neurotoxins
KW  - Paraponeritoxin
KW  - Phospholipases
KW  - Rp-Hplc
KW  - alpha latrotoxin
KW  - ant venom
KW  - arginine kinase
KW  - cathepsin
KW  - contig
KW  - defensin 2
KW  - icarapin
KW  - metalloproteinase
KW  - neurotoxin
KW  - novel toxin like protein
KW  - phospholipase
KW  - phospholipase A2
KW  - poneratoxin
KW  - proteome
KW  - serine proteinase
KW  - transcriptome
KW  - unclassified drug
KW  - amino acid sequence
KW  - ant
KW  - Article
KW  - liquid chromatography-mass spectrometry
KW  - neurotoxicity
KW  - nonhuman
KW  - Paraponera clavata
KW  - protein expression
KW  - proteomics
KW  - sequence database
KW  - tandem mass spectrometry
KW  - transcriptomics
KW  - venom gland
N2  - 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.
SN  - 20726651 (Issn)
UR  - http://dx.doi.org/10.3390/toxins12050324
N1  - exported from refbase (http://php.ecofog.gf/refbase/show.php?record=972), last updated on Thu, 28 Jan 2021 14:54:58 -0300
ID  - Aili_etal2020
ER  -