Deciphering the Molecular Diversity of an Ant Venom Peptidome through a Venomics Approach.

Abstract:

:The peptide toxins in the venoms of small invertebrates such as stinging ants have rarely been studied due to the limited amount of venom available per individual. We used a venomics strategy to identify the molecular diversity of the venom peptidome for the myrmicine ant Tetramorium bicarinatum. The methodology included (i) peptidomics, in which the venom peptides are sequenced through a de novo mass spectrometry approach or Edman degradation; (ii) transcriptomics, based on RT-PCR-cloning and DNA sequencing; and (iii) the data mining of the RNA-seq in the available transcriptome. Mass spectrometry analysis revealed about 2800 peptides in the venom. However, the de novo sequencing suggested that most of these peptides arose from processing or the artifactual fragmentations of full-length mature peptides. These peptides, called "myrmicitoxins", are produced by a limited number of genes. Thirty-seven peptide precursors were identified and classified into three superfamilies. These precursors are related to pilosulin, secapin or are new ant venom prepro-peptides. The mature myrmicitoxins display sequence homologies with antimicrobial, cytolytic and neurotoxic peptides. The venomics strategy enabled several post-translational modifications in some peptides such as O-glycosylation to be identified. This study provides novel insights into the molecular diversity and evolution of ant venoms.

journal_name

J Proteome Res

authors

Touchard A,Téné N,Song PCT,Lefranc B,Leprince J,Treilhou M,Bonnafé E

doi

10.1021/acs.jproteome.8b00452

subject

Has Abstract

pub_date

2018-10-05 00:00:00

pages

3503-3516

issue

10

eissn

1535-3893

issn

1535-3907

journal_volume

17

pub_type

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