| Autor: |
Feás X; Academy of Veterinary Sciences of Galicia, 15707 Santiago de Compostela, Spain.; Fundación Instituto de Investigación Sanitaria de Santiago de Compostela (FIDIS), Hospital Clínico, 15706 Santiago de Compostela, Spain., Alonso-Sampedro M; Fundación Instituto de Investigación Sanitaria de Santiago de Compostela (FIDIS), Hospital Clínico, 15706 Santiago de Compostela, Spain.; Research Methods Group (RESMET), Health Research Institute of Santiago de Compostela (IDIS), University Hospital of Santiago de Compostela, 15706 Santiago de Compostela, Spain.; Network for Research on Chronicity, Primary Care, and Health Promotion (RICAPPS-ISCIII/RD21/0016/0022), University Hospital of Santiago de Compostela, 15706 Santiago de Compostela, Spain., Bravo SB; Fundación Instituto de Investigación Sanitaria de Santiago de Compostela (FIDIS), Hospital Clínico, 15706 Santiago de Compostela, Spain.; Proteomic Unit, Health Research Institute of Santiago de Compostela (IDIS), University Hospital of Santiago de Compostela, 15706 Santiago de Compostela, Spain., Vidal C; Fundación Instituto de Investigación Sanitaria de Santiago de Compostela (FIDIS), Hospital Clínico, 15706 Santiago de Compostela, Spain.; Research Methods Group (RESMET), Health Research Institute of Santiago de Compostela (IDIS), University Hospital of Santiago de Compostela, 15706 Santiago de Compostela, Spain.; Network for Research on Chronicity, Primary Care, and Health Promotion (RICAPPS-ISCIII/RD21/0016/0022), University Hospital of Santiago de Compostela, 15706 Santiago de Compostela, Spain.; Allergy Department, University Hospital of Santiago de Compostela, 15706 Santiago de Compostela, Spain.; Department of Psychiatry, Radiology, Public Health, Nursing and Medicine, Faculty of Medicine, University of Santiago de Compostela (USC), 15782 Santiago de Compostela, Spain. |
| Abstrakt: |
This study aimed to investigate the venom sac extracts (VSEs) of the European hornet (EH) Vespa crabro (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% ( n = 110) showed significant differential expression between VSE-G and VSE-W. In this set, 57.3% ( n = 63) were upregulated and 42.7% ( n = 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. |
