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Increasing Coverage of Proteome Identification of the Fruiting Body of Agaricus bisporus by Shotgun Proteomics

Summary

This research provides the most detailed analysis to date of proteins present in button mushrooms using advanced laboratory techniques. The findings help us better understand the molecular composition of these commonly consumed mushrooms. Impact on everyday life: – Improved understanding of mushroom nutrition and health benefits – Better knowledge to develop more nutritious mushroom varieties – Enhanced ability to identify beneficial compounds in mushrooms – Potential for developing mushrooms with increased antioxidant properties – Better quality control methods for mushroom production

Background

The button mushroom Agaricus bisporus is a widely cultivated and consumed edible fungus. While previous proteomics studies have been limited by 2D-PAGE technology, advances in mass spectrometry and shotgun proteomics now enable more comprehensive protein identification. This study aimed to provide deeper proteome coverage of A. bisporus fruiting bodies using multiple MudPIT runs.

Objective

To increase coverage of protein identification in Agaricus bisporus fruiting bodies by conducting and merging multiple MudPIT (Multi-Protein Identification Technology) runs for shotgun proteomics analysis.

Results

The analysis identified 3,093 non-redundant proteins with wide ranges of pI values and molecular masses, indicating unbiased protein identification. K5XI50 (Aldedh domain-containing protein) and K5XEW1 (Ubiquitin-like domain-containing protein) were found to be highly abundant. Only 53% of identified proteins had known functions, while 47% remained uncharacterized. Gene Ontology analysis revealed proteins were mainly associated with biological processes, with coiled-coil (12.8%) and nucleotide binding (8.21%) categories being dominant.

Conclusion

The shotgun proteomics approach successfully identified over 3,000 proteins in A. bisporus fruiting bodies, providing the most comprehensive proteome coverage to date. The identification of many uncharacterized proteins supports their existence and potential roles. KEGG analysis revealed enrichment of proteins involved in biosynthesis of secondary metabolites and tyrosine metabolism, suggesting association with antioxidant metabolites.
  • Published in:Foods,
  • Study Type:Laboratory Research,
  • Source: 10.3390/foods9050632
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