Abstract
We previously identified 92 toxin-like peptides and proteins, including pilosulin-like peptides 1–6 from the predatory ant Odontomachus monticola, by transcriptome analysis. Here, to further characterize venom components, we analyzed the venom and venom sac extract by ESI-MS/MS with or without trypsin digestion and reducing agent. As the low-molecular-mass components, we found amino acids (leucine/isoleucine, phenylalanine, and tryptophan) and biogenic amines (histamine and tyramine) in the venom and venom sac extract. As the higher molecular mass components, we found peptides and proteins such as pilosulin-like peptides, phospholipase A2s, hyaluronidase, venom dipeptidyl peptidases, conotoxin-like peptide, and icarapin-like peptide. In addition to pilosulin-like peptides 1–6, we found three novel pilosulin-like peptides that were overlooked by transcriptome analysis. Moreover, pilosulin-like peptides 1–6 were chemically synthesized, and some of them displayed antimicrobial, hemolytic, and histamine-releasing activities.
Highlights
Ants (Hymenoptera: Formicidae) have been believed to share the same ancestor with bees and wasps, and have many traits in common with them
Among the low-mass components, we found two biogenic amines and the low-mass components, we found two biogenic amines andsac three aminoAmong acids in the venom and venom three amino acids in the venom and venom sac extract of O. monticola by retention time comparison and elemental analysis (Figure 1)
Among the toxin-like components we found pilosulin-like peptides, phospholipase A2 s, hyaluronidase, and venom dipeptidyl peptidases of which amino acid sequences have some similarities to those of Apis mellifera orthologues in our previous study [10]
Summary
Ants (Hymenoptera: Formicidae) have been believed to share the same ancestor with bees and wasps, and have many traits in common with them. Since most ant species have a sting with venoms including formic acid, hydrocarbons, amines, peptides, and proteins, for predatory purpose [1], the venom components have been attractive as potential lead compounds for drug development. One of the peptide components in the ant venom is the pilosulin-like peptide. Isolated pilosulin 1 cDNA from a Myrmecia pilosula cDNA library in 1993 [2], many pilosulin and pilosulin-like peptides have been identified from various ant species [3,4,5]. Pilosula cDNA library in 1993 [2], many pilosulin and pilosulinpilosulin cDNA from a Myrmecia like peptides have been identified from various antin species [3,4,5].
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