Comparative Seed Proteome Profile Reveals No Alternation of Major Allergens in High-Yielding Mung Bean Cultivars

• Published in: Journal of agricultural and food chemistry 2024-06, Vol.72 (24), p.13957-13965
• Main Authors: Shaheen, Nazma, Hossen, Md. Sujan, Akhter, Kazi Turjaun, Halima, Oumma, Hasan, Md. Kamrul, Wahab, Asfia, Gamagedara, Sanjeewa, Bhargava, Kanika, Holmes, Tawni, Najar, Fares Z., Khandaker, Morshed, Peng, Zongkai, Yang, Zhibo, Ahsan, Nagib
• Format: Article
• Language: English
• Subjects: Food Safety and Toxicology
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/acs.jafc.4c01054

Mung bean contains up to 32.6% protein and is one of the great sources of plant-based protein. Because many allergens also function as defense-related proteins, it is important to determine their abundance levels in the high-yielding, disease-resistant cultivars. In this study, for the first time, we compared the seed proteome of high-yielding mung bean cultivars developed by a conventional breeding approach. Using a label-free quantitative proteomic platform, we successfully identified and quantified a total of 1373 proteins. Comparative analysis between the high-yielding disease-resistant cultivar (MC5) and the other three cultivars showed that a total of 69 common proteins were significantly altered in their abundances across all cultivars. Bioinformatic analysis of these altered proteins demonstrated that PDF1 (a defensin-like protein) exhibited high sequence similarity and epitope matching with the established peanut allergens, indicating a potential mung bean allergen that showed a cultivar-specific response. Conversely, known mung bean allergen proteins such as PR-2/PR-10 (Vig r 1), Vig r 2, Vig r 4, LTP1, β-conglycinin, and glycinin G4 showed no alternation in the MC5 compared to other cultivars. Taken together, our findings suggest that the known allergen profiles may not be impacted by the conventional plant breeding method to develop improved mung bean cultivars.