Functional characterisation of pigeon egg proteins based on data-independent acquisition quantitative proteomics

1. This study characterised proteomic differences among pigeon, chicken and quail eggs and explored the functional properties of pigeon egg proteins.2. Nine eggs each from White King pigeons (WKP), nine Hy-Line Brown chickens (HLC) and nine Shendan No.1 quail (S1Q) were selected and pooled into three replicates for each species. Data-independent acquisition (DIA)-based quantitative proteomics was employed to identify differentially expressed proteins, followed by bioinformatics analyses.3. A total of 8,835 peptides corresponding to 937 proteins were identified and quantified across nine samples. In the WKPvs.HLC comparison, 423 proteins were differentially expressed, including 178 upregulated and 245 downregulated proteins. In the WKPvs.S1Q comparison, 479 proteins showed significant expression changes, with 190 upregulated and 289 downregulated proteins. Gene Ontology (GO), Kyoto Encyclopaedia of Genes and Genomes (KEGG) enrichment and protein-protein interaction (PPI) network analyses revealed that WKP egg proteins were significantly enriched. This was related to lipid transport and metabolism, immune regulation and antioxidant activity, transparent albumen gel formation and wound healing.4. These results demonstrate distinct proteomic profiles between pigeon eggs and other poultry eggs. Overall, pigeon eggs possess unique functional protein characteristics, providing a molecular basis for their further development and utilisation as a potential functional protein source.