Peeking into the Stingers: A Comprehensive SWATH-MS Study of the European Hornet Vespa crabro (Linnaeus, 1758) (Hymenoptera: Vespidae) Venom Sac Extracts

This study aimed to investigate the venom sac extracts (VSEs) of the European hornet (EH) (Linnaeus, 1758) (Hymenoptera: Vespidae), focusing on the differences between stinging females, gynes (G), and workers (W), at the protein level. Using a quantitative "Sequential Window Acquisition of all...

Full description

Saved in:
Bibliographic Details
Published in:International journal of molecular sciences 2024-04, Vol.25 (7), p.3798
Main Authors: Feás, Xesús, Alonso-Sampedro, Manuela, Bravo, Susana Belén, Vidal, Carmen
Format: Article
Language:English
Subjects:
Allergens
Allergies
Animals
Bees
castes
Enzymes
European hornet
Female
Females
gynes
Hyaluronoglucosaminidase
Hypersensitivity
Insects
Mass spectrometry
Metabolism
Phospholipases A1
Proteins
Proteomics
Quantitative analysis
Scientific imaging
Venom
venom sac
Vespa crabro
Wasps
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:This study aimed to investigate the venom sac extracts (VSEs) of the European hornet (EH) (Linnaeus, 1758) (Hymenoptera: Vespidae), focusing on the differences between stinging females, gynes (G), and workers (W), at the protein level. Using a quantitative "Sequential Window Acquisition of all Theoretical Fragment Ion Mass Spectra" (SWATH-MS) analysis, we identified and quantified a total of 240 proteins. Notably, within the group, 45.8% ( = 110) showed significant differential expression between VSE-G and VSE-W. In this set, 57.3% ( = 63) were upregulated and 42.7% ( = 47) downregulated in the G. Additionally, the two-hundred quantified proteins from the class Insecta belong to sixteen different species, six of them to the Hymenoptera/Apidae lineage, comprising seven proteins with known potential allergenicity. Thus, phospholipase A1 (Vesp v 1), phospholipase A1 verutoxin 2b (VT-2b), hyaluronidase A (Vesp v 2A), hyaluronidase B (Vesp v 2B), and venom allergen 5 (Vesp v 5) were significantly downregulated in the G, and vitellogenin (Vesp v 6) was upregulated. Overall, 46% of the VSE proteins showed differential expression, with a majority being upregulated in G. Data are available via ProteomeXchange with identifier PXD047955. These findings shed light on the proteomic differences in VSE between EH castes, potentially contributing to our understanding of their behavior and offering insights for allergy research.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms25073798