Highlights
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- Polybiapaulista is a social wasp from Southeast Brazil, where it causes severe envenoming.
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- Only five of these peptides are structurally and functionally known in its venom.
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- P. paulista venom was investigated for profiling its peptidome.
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- Fourteen major peptides were detected and sequenced, being novel ones.
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- The novel peptides were wasp kinins, chemotactic components, and mastoparans.
Abstract
Most crude venom from Polybiapaulista
is composed of short, linear peptides; however, only five of these
peptides are structurally and functionally characterized. Therefore, the
peptides in this venom were profiled using an HPLC-IT-TOF/MS and MSn system. The presence of type -d and -w
ions that are generated from the fragmentation of the side chains was
used to resolve I/L ambiguity. The distinction between K and Q residues
was achieved through esterification of the α- and ε-amino groups in the
peptide chains, followed by mass spectrometry analysis. Fourteen major
peptides were detected in P. paulista venom and
sequenced; all the peptides were synthesized on solid-phase and
submitted to a series of bioassays. Five of them had been previously
characterized, and nine were novel toxins. The novel peptides correspond
to two wasp kinins, two chemotactic components, three mastoparans, and
two peptides of unknown function. The seven novel peptides with
identified functions appear to act synergistically with the previously
known ones, constituting three well-known families of peptide toxins
(wasp kinins, chemotactic peptides, and mastoparans) in the venom of
social wasps. These multifunctional toxins can cause pain, oedema
formation, haemolysis, chemotaxis of PMNLs, and mast cell degranulation
in victims who are stung by wasps.
Graphical abstract
Keywords
- Peptidomics;
- RP-HPLC;
- ESI-IT-TOF/MS;
- Polycationic peptides;
- Wasp venom
Copyright © 2015 Elsevier Ltd. All rights reserved.
