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Identification and characterisation of novel wasp mastoparans and chemotactic peptides from the venom of social wasp Polistes stigma (Hymenoptera: Vespidae: Polistinae).

ABSTRACT: Polistes stigma is a common social wasp found in continental Southeast Asia. Despite its wide distribution and abundance, hitherto, there are no studies on small or medium molecular weight components of the venom. For the first time, this study has described the amino acid sequences and its post-translation modifications (PTM's) of four wasp-mastoparans (Ps 1524, Ps 1540, Ps 1556 and Ps 1630), three chemotactic peptides (Ps1417, Ps1434 and Ps1474) and one more (Ps1549) lysine rich peptide from the venom of P. stigma. There were 27 mass traces obtained from the crude natural venom, in which the complete amino acid sequences of 8 peptides were solved. Further, single disulphide bonded peptides uncommon in wasp venoms were identified. The mastoparan peptides were rich in hydrophobic residues. In addition, the peptides Ps1549, Ps1630, Ps1434 and Ps1417 were found to have unusual PTM's of C-terminal amidation. This preliminary study comprehends the untapped compounds present in wasp venom that are equally valuable to widely studied venoms of snakes, spiders and cone snails.

SUBMITTER: Rajesh RP

PROVIDER: S-EPMC8169029 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Background Between 9.3 and 28.5% of world population are estimated to be allergic to the protein components of Hymenoptera venom and among them, the hyaluronidase (HYAL) is one of the most important, although the nature of its IgE binding epitopes is unknown. Methods Enzyme was purified from P. paulista venom by cation exchange chromatography in AKTA-FPLC system with a Hiprep CM FF column. Fractions with HYAL activity were pooled, lyophilized, dialyzed against distilled water in presence of protease inhibitor (PMSF) and subjected to SDS-PAGE 15%. The only protein bands visualized were submitted to tryptic digestion and to MALDI-ToF/ToF mass spectrometry. Digested peptides produced were compared with partial/complete protein sequences from Data Bank including with the HYAL (Q9U6V9) of Polistes annularis venom used as model. Western blotting was performed with Pp-HYAL-specific antibody to test the identity of pure protein. Results All analysis performed identified the pure protein as an HYAL present in P.paulista venom, which also had its cDNA sequence (GI:302201582) cloned and determined in previous studies, being its high similarity with the Polistes annularis enzyme already confirmed. The mature allergenic protein has 338 amino acids and a molecular weight of 39 KDa. The same allergen is known in other insects, venoms and immunological cross reactivity may sometimes be observed among closely related species. Here, the immunoblotting assay revealed that the Pp-HYAL-specific antibody used recognized the correspondent protein in the purified fraction and in the crude venom of P. paulista, but not in the Apis mellifera and Solenopsis invicta venoms. Conclusions The methodology used was able to purify the allergen, which is a key step in the characterization of its binding epitopes. Such knowledge has direct implications in accuracy of diagnostic procedures and strategies for specific immunotherapy of allergic patients to the venom of this insect. Funding: Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP).

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Identification and characterisation of novel wasp mastoparans and chemotactic peptides from the venom of social wasp Polistes stigma (Hymenoptera: Vespidae: Polistinae).

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