Lentil allergens identification and quantification: An update from omics perspective

Halima, Oumma; Najar, Fares Z.; Wahab, Asfia; Gamagedara, Sanjeewa; Chowdhury, Akibul Islam; Foster, Steven B.; Shaheen, Nazma; Ahsan, Nagib

doi:10.1016/j.fochms.2022.100109

Cited by 6 publications

(5 citation statements)

References 89 publications

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“…Song et al 10.3389/fpls.2024.1355902 (Halima et al, 2022). One goal in crop breeding for better seed nutrition quality is to reduce levels of anti-nutritional factors, such as allergens (Song et al, 2022).…”

Section: Discussionmentioning

confidence: 99%

“…Allergens in lentil have been a significant concern due to increased consumption in parts of the world ( Sackesen et al., 2020 ). Numerous efforts have been made to identify and qualify lentil allergens, but lentil allergy management through modifications in food systems requires further development ( Halima et al., 2022 ). One goal in crop breeding for better seed nutrition quality is to reduce levels of anti-nutritional factors, such as allergens ( Song et al., 2022 ).…”

Section: Discussionmentioning

confidence: 99%

“…LTPs can easily bind to multiple types of lipid molecules such as fatty acids and phospholipids ( Shenkarev et al., 2017 ). Although Len c3 is less abundant compared with Len c1 and Len c2, LTPs are highly cross-reactive and are considered as one of the main plant allergens ( Shenkarev et al., 2017 ; Halima et al., 2022 ).…”

Section: Introductionmentioning

confidence: 99%

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Applying a non-GMO breeding approach with an identified natural variation to reduce food allergen Len c3 in Lens culinaris seeds

Song,

Mavraganis,

Shen

et al. 2024

Front. Plant Sci.

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Lentils (Lens culinaris) are produced in diverse agroecological regions and are consumed as one of the most important food legumes worldwide. Lentils possess a nutritional profile from a human health perspective that is not only nutrient dense but also offers a better balance between protein and carbohydrates. However, lentil causes food allergy, which has been a significant concern due to increased consumption in parts of the world. Len c3, a non-specific lipid transfer protein (LTP), was identified as one of the allergens in lentil seeds. In this study, we identified an LTP gene Lcu.2RBY.4g013600 that encodes the lentil allergen Len c3. We then focused on gene screening from a collection of natural accessions to search for natural mutations of the Len c3 allergen-encoding gene. A natural lentil line M11 was identified with mutations at LcLTP3b and low accumulation of vicilin through genomic-assisted approaches. Furthermore, we generated a pool of lentil germplasms with LcLTP3b mutation background through crossing the identified lentil plant M11 with two lentil cultivars, CDC Redmoon and CDC Gold. These generated lentil hybrids can be used as a breeding resource targeting at reducing allergen risk in lentil consumption.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Applying a non-GMO breeding approach with an identified natural variation to reduce food allergen Len c3 in Lens culinaris seeds

Song,

Mavraganis,

Shen

et al. 2024

Front. Plant Sci.

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“…Even though our findings showed that the major mung bean allergens remained unchanged throughout the cultivars, we continued to focus on the differentially expressed proteins that overlapped with the high-yielding cultivar (MC5) in order to find any potential allergens across the cultivars (Figure A,B). In silico analysis has been successfully employed to determine the potential allergenicity of many plant proteins. − A total of 69 protein sequences were subjected to AllerCatPro − and pLM4AIg, an online-based pipeline to determine the protein allergenicity potential. Three proteins, PDF1, BGAL and BG7S, were identified as potential allergens by both platforms (Figure D, Table S5).…”

Section: Discussionmentioning

confidence: 99%

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

Shaheen,

Hossen,

Akhter

et al. 2024

J. Agric. Food Chem.

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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, diseaseresistant 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.

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“…However, the guidelines were considered overly conservative and ought to be reviewed after over two decades [ 48 ]. Therefore, the data were validated using the AllerCatPro 2.0 program due to its superior accuracy in allergen prediction and its ability to provide comprehensive allergen profiling [ 49 , 50 ]. The analysis revealed that three of the five most abundant proteins had features of allergenicity and could be a cause of concern for certain demographics, particularly people with a tree nut allergy or gluten intolerance.…”

Section: Discussionmentioning

confidence: 99%

Cottonseed Meal Protein Isolate as a New Source of Alternative Proteins: A Proteomics Perspective

Tan

Kwan

Lee

et al. 2022

IJMS

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Cottonseed meal (CSM) is a good source of dietary proteins but is unsuitable for human consumption due to its gossypol content. To unlock its potential, we developed a protein extraction process with a gossypol removal treatment to generate CSM protein isolate (CSMPI) with ultra-low gossypol content. This process successfully reduced the free and total gossypol content to 4.8 ppm and 147.2 ppm, respectively, far below the US FDA limit. In addition, the functional characterisation of CSMPI revealed a better oil absorption capacity and water solubility than pea protein isolate. Proteome profiling showed that the treatment improved protein identification, while SDS-PAGE analysis indicated that the treatment did not induce protein degradation. Amino acid analysis revealed that post-treated CSMPI was rich in branched-chain amino acids (BCAAs). Mass spectrometry analysis of various protein fractions obtained from an in vitro digestibility assay helped to establish the digestibility profile of CSM proteins. Several potential allergens in CSMPI were also found using allergenic prediction software, but further evaluation based on their digestibility profiles and literature reviews suggests that the likelihood of CSMPI allergenicity remains low. Overall, our results help to navigate and direct the application of CSMPIs as alternative proteins toward nutritive human food application.

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Lentil allergens identification and quantification: An update from omics perspective

Cited by 6 publications

References 89 publications

Applying a non-GMO breeding approach with an identified natural variation to reduce food allergen Len c3 in Lens culinaris seeds

Applying a non-GMO breeding approach with an identified natural variation to reduce food allergen Len c3 in Lens culinaris seeds

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

Cottonseed Meal Protein Isolate as a New Source of Alternative Proteins: A Proteomics Perspective

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