ArticlePloS one2021
Shotgun proteomics of Brassica rapa seed proteins identifies vicilin as a major seed storage protein in the mature seed.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Nutritional and Functional Potential of Rapeseed and Canola Proteins: Advances in Protein Extraction, Phenolic Removal, and Food Applications.Comprehensive reviews in food science and food safety · 2026Review
- Genome-Wide Association Study for Markers Related to Protein, Fiber (ADF and NDF) and Oil Content in Winter Oilseed Rape Seeds (International journal of molecular sciences · 2025Article
- Proteomic changes associated with health benefit properties in fresh and preserved mustard greens.Food chemistry. Molecular sciences · 2025Article
- Structural, physicochemical, and functional properties of white and blue lupin vicilin and legumin fractions.Food chemistry: X · 2025Article
- Genotype-Driven Proteomic Diversity in Macadamia Nuts: Implications for Allergenicity, Nutritional Quality, and Breeding Strategies.Journal of agricultural and food chemistry · 2025Article
- In Silico Proteomic Profiling and Bioactive Peptide Potential of Rapeseed Meal.Foods (Basel, Switzerland) · 2025Article
- Proteomic Analysis of the Major Alkali-Soluble Inca Peanut (Foods (Basel, Switzerland) · 2024Article
- Recent Progress in Terrestrial Biota Derived Antibacterial Agents for Medical Applications.Molecules (Basel, Switzerland) · 2024Review
- Brassicaceae Mustards: Phytochemical Constituents, Pharmacological Effects, and Mechanisms of Action against Human Disease.International journal of molecular sciences · 2024Review
- Proteomic profile of tepary bean seed storage proteins in germination with low water potential.Proteome science · 2024Article
- Dissection of quantitative trait nucleotides and candidate genes associated with agronomic and yield-related traits under drought stress in rapeseed varieties: integration of genome-wide association study and transcriptomic analysis.Frontiers in plant science · 2024Article
- Shotgun proteomics of quinoa seeds reveals chitinases enrichment under rainfed conditions.Scientific reports · 2023Article
- Plant dehydrins and dehydrin-like proteins: characterization and participation in abiotic stress response.Frontiers in plant science · 2023Review
- Review
- Lentil allergens identification and quantification: An update from omics perspective.Food chemistry. Molecular sciences · 2022Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins make up a large percentage of the Brassica seed and are second only to the oil in economic importance with uses for both animal and human nutrition. The most abundant proteins reported in the seeds of Brassica are the seed storage proteins cruciferin and napin, belonging to the 12S globulin and 2S albumin families of proteins, respectively. To gain insight into the Brassica rapa seed proteome and to confirm the presence and relative quantity of proteins encoded by candidate seed storage genes in the mature seed, shotgun proteomics was carried out on protein extracts from seeds of B. rapa inbred line R-o-18. Following liquid chromatography tandem mass spectrometry, a total of 34016 spectra were mapped to 323 proteins, where 233 proteins were identified in 3 out of 4 biological replicates by at least 2 unique peptides. 2S albumin like napin seed storage proteins (SSPs), 11/12S globulin like cruciferin SSPs and 7S globulin like vicilin SSPs were identified in the samples, along with other notable proteins including oil body proteins, namely ten oleosins and two oil body-associated proteins. The identification of vicilin like proteins in the mature B. rapa seed represents the first account of these proteins in the Brassicaceae and analysis indicates high conservation of sequence motifs to other 7S vicilin-like allergenic proteins as well as conservation of major allergenic epitopes in the proteins. This study enriches our existing knowledge on rapeseed seed proteins and provides a robust foundation and rational basis for plant bioengineering of seed storage proteins.
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