PXD079138-1

PXD079138 is an original dataset announced via ProteomeXchange.

Title	Exploratory Proteomic Characterization of Apis mellifera Venom Across an Environmental Gradient in Central Chile
Description	Background: Bee venom (Apis mellifera) is a complex biological secretion rich in peptides, enzymes, and bioactive molecules with recognized pharmacological potential. Environmental factors may influence venom composition, yet geographic variation in the bee venom proteome remains insufficiently characterized, particularly in Mediterranean ecosystems of South America, including Chile. Methods: Venom samples obtained from multiple colonies of Apis mellifera within each geographic area in the Valparaíso Region of central Chile, were pooled to generate one composite biological sample per zone: Sea Level (SL), Inland Valley (IV), and Andean Foothills (AF). Two analytical aliquots from each pooled sample were processed independently for analysis. Proteomic profiling was performed using chromatography–tandem mass spectrometry (LC–MS/MS) with a data-dependent acquisition workflow. Label-free quantification based on spectral counts was used to assess differential protein expression across zones. Results: A total of 679 proteins were identified across all LC–MS/MS runs, including 604 proteins detected in SL samples, 530 in IV, and 395 in AF samples, with 360 proteins consistently quantified across the analytical duplicates from the three geographic zones and included in pairwise comparisons. Approximately 25–28% of quantified proteins were differentially expressed (DEPs) across pairwise analytical comparisons, suggesting geographically associated variation in venom composition. SL samples exhibited relative enrichment of classical venom components, including melittin, phospholipase A2, and venom-associated enzymes, consistent with a more toxin-oriented proteomic profile. In contrast, AF and IV samples showed increased abundance of proteins associated with stress response, metabolism, and secretion, including heat shock proteins, redox enzymes, and major royal jelly proteins (MRJPs), suggesting a shift toward physiological adaptation and glandular secretion-related processes. Conclusion: These findings suggest that bee venom proteome may vary across environmental gradients, reflecting both conserved and context-dependent components. The observed shift between toxin-dominated and stress-associated proteomic profiles is consistent with the concept of environmentally associated plasticity in venom composition. This variability has important implications for the pharmacological use and standardization of bee venom, highlighting the need to consider geographic origin in biomedical applications. Further studies integrating ecological, biochemical, and pharmacological approaches are needed to evaluate the functional and translational relevance of these proteomic differences.
HostingRepository	PRIDE
AnnounceDate	2026-09-04
AnnouncementXML	Submission_2026-09-04_14:22:47.715.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Guillermo Nourdin
SpeciesList	scientific name: Apis mellifera (Honeybee); NCBI TaxID: NEWT:7460;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	timsTOF Pro 2

Revision	Datetime	Status	ChangeLog Entry
0	2026-06-01 09:06:20	ID requested
⏵ 1	2026-09-04 14:22:48	announced
2	2026-09-04 14:24:12	announced	2026-09-04: Updated project metadata.

Dataset with its publication pending

submitter keyword: Bee venom, Proteomics, Geographic variation, Differential expression

Jose Luis Marcos
contact affiliation	Departamento de Ciencias Veterinarias, Carrera de Medicina Veterinaria, Facultad de Ciencias de la Vida, Universidad Vina del Mar, Vina del Mar, Chile
contact email	jmarcos@uvm.cl
lab head
Guillermo Nourdin
contact affiliation	MELISA Institute
contact email	gnourdin@melisainstitute.org
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD079138

PRIDE project URI

• PRIDE
  1. PXD079138
     1. Label: PRIDE project
     2. Name: Exploratory Proteomic Characterization of Apis mellifera Venom Across an Environmental Gradient in Central Chile