Proteomic analysis of the distribution of the major seed allergens in wild, landrace, ancestral, and modern soybean genotypes

Xu, Chenping; Caperna, Thomas J.; Garrett, Wesley M.; Cregan, Perry B.; Bae, Hyeun‐Jong; Luthria, Devanand L.; Natarajan, Savithiry

doi:10.1002/jsfa.3017

Cited by 23 publications

(18 citation statements)

References 36 publications

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“…A similar study of Japanese lines did not reveal any P34 null lines (Ogawa and others 2000). Xu and others (2007) also showed that P34 was present in 16 soybean genotypes examined by 2D SDS‐PAGE electrophoresis and MS‐spectrometry analysis. However, P34 spots showed weak intensity in the wild genotype compared to that in the landrace genotype.…”

Section: Resultsmentioning

confidence: 79%

Purification, Thermal Stability, and Antigenicity of the Immunodominant Soybean Allergen P34 in Soy Cultivars, Ingredients, and Products

Wilson

Martínez‐Villaluenga

Mejía

2008

Journal of Food Science

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Protein P34 (Gly m Bd 30K) is the immunodominant allergen in soybean (Glycine max L.). The objectives of this study were (1) to study the effect of thermal treatment on P34 antigenicity and secondary structure after isolation and purification of P34 from soybean by chromatographic techniques; (2) to identify the variability of P34 allergen within 138 accessions from a diverse USDA soybean germplasm collection by ELISA; and (3) to quantify P34 immunoreactivity in various commercial soy ingredients and products. Thermal processing decreased P34 antigenicity. Soybean accessions with the highest P34 content were ancestral (12 mg/g defatted flour) followed by modern (10 mg/g defatted flour) and exotic (8 mg/g defatted flour). The cultivar that emerged as the lowest-expressing P34 accession was PI548657 (2.3 mg/g defatted flour). Among commercial soy ingredients, soy flour yielded the highest P34 antigenicity (32 mg/g extracted protein) followed by soy protein isolate (29 mg/g extracted protein) and soy protein concentrate (24 mg/g extracted protein). Among soy consumer products, soymilk presented the highest P34 antigenicity, ranging from 7 to 23 mg/g extracted protein, followed by tempeh (8 mg/g extracted protein), soy infant formula (3.4 mg/g extracted protein), soy powder (2 mg/g extracted protein), and soy cheese products (0.50 mg/g extracted protein). Korean miso, soy sauce, soy chili mix, soy nuts, soy cream cheese, soy meat patty, texturized soy protein, and soy cereal exhibited undetectable P34 antigenicity (detection limit = 0.45 ng). Selecting soybean varieties with low levels of this allergen, or via processing, could potentially make soybean products less antigenic.

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Section: Resultsmentioning

confidence: 79%

Purification, Thermal Stability, and Antigenicity of the Immunodominant Soybean Allergen P34 in Soy Cultivars, Ingredients, and Products

Wilson

Martínez‐Villaluenga

Mejía

2008

Journal of Food Science

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“…The Gly m Bd 30K protein was identified as P34, a papain superfamily cysteine proteinase type of enzyme (Kalinski et al, 1990). P34 is not an abundant seed protein, but it is consistently present in nearly all germplasm accessions evaluated (Joseph et al, 2006; Xu et al, 2007; Yaklich et al, 1999).…”

mentioning

confidence: 98%

Association of a Four‐Basepair Insertion in the P34 Gene with the Low‐Allergen Trait in Soybean

Bilyeu

Ren²,

Nguyen

et al. 2009

The Plant Genome

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The value of soybean [Glycine max (L.) Merr.] is determined in part by functionality of major seed components, extractable oil and high protein meal. Soybean meal is an important protein source for animal feeds, and use of soybean meal by the food industry is increasing. Food allergens have negative impacts for both foods and feeds. The major soybean allergen, Gly m Bd 30K, was identifi ed as the P34 protein, a low abundance but highly conserved seed protein. Recently, two soybean germplasm accessions (PI 567476 and PI 603570A) were identifi ed as having reduced P34 content without other collateral changes in seed protein composition. In order to develop molecular markers to enhance breeding for low P34, our objective was to characterize the P34 gene region in wild-type and low-P34 soybean lines and exploit any sequence differences to allow direct selection for mutant P34 alleles. The results indicated the two low-P34 germplasm accessions contain a four-basepair insertion at the P34 start codon. The mutant allele may inhibit effi cient translation initiation of the P34 protein. Inheritance of the mutant P34 alleles completely associated with the low-P34 phenotype. Molecular markers were developed that were based on the mutant allele of the P34 gene.

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“…Protein extract and 2-DE were carried out according to the previous study (Xu et al, 2007). Bio-Protein Assay Kit (5000202, 5000203) was used to determine the protein concentrations in the samples.…”

Section: Proteome Analysismentioning

confidence: 99%

“…Two-dimensional gel electrophoresis has been used to analyze the differences between wild and cultivated soybean seeds in terms of protein composition (Li et al, 2007;Xu et al, 2007;Natarajan et al, 2012). However, as far as we know, the difference between the proteome of wild soybean roots and that of cultivated soybean roots has not yet been reported.…”

Section: Introductionmentioning

confidence: 99%

Anatomical Observation and Proteomics Analysis of Root Tips of Wild and Cultivated Soybeans

Xing¹,

Zhang²,

Ca³

et al. 2017

IJAB

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Wild and cultivated soybeans from different areas of China were used as materials for paraffin cross-sections of the juncture between the root elongation and maturation zones of wild and cultivated soybeans during the seedling stage. It was found that the casparian band of the endodermis and duct of metaxylem in the anatomical structure of the cultivated soybean developed faster than those of the wild soybean. Rapid development of these structures sped up transmission and enhanced support capacity. Meanwhile, two-dimensional electrophoresis was adopted to analyze the differences between the wild and cultivated soybean populations in terms of protein expression during the seedling stage. Our results showed that expression levels of 28 proteins from among the wild and cultivated soybean populations were significantly different from one another. In the cultivated population, the protein expression levels were up-regulated in four protein spots and down-regulated in 24 protein spots. Down-regulated proteins were associated with secondary metabolites and metabolism of antibiotics. Decrease in the expression these proteins may speed up nodule formation. These results showed that early growth and development of the cultivated soybean roots occurred at a significantly faster rate than those of the wild soybean. The increased rates of these processes accelerate root shape formation and improve root function. In conclusion, this study systematically explored the anatomical structure and differentially expressed proteins of roots between wild and cultivated soybean, and differentially expressed proteins identified here will be the valuable resource for studying soybean root differences resulting from domestication.

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Proteomic analysis of the distribution of the major seed allergens in wild, landrace, ancestral, and modern soybean genotypes

Cited by 23 publications

References 36 publications

Purification, Thermal Stability, and Antigenicity of the Immunodominant Soybean Allergen P34 in Soy Cultivars, Ingredients, and Products

Purification, Thermal Stability, and Antigenicity of the Immunodominant Soybean Allergen P34 in Soy Cultivars, Ingredients, and Products

Association of a Four‐Basepair Insertion in the P34 Gene with the Low‐Allergen Trait in Soybean

Anatomical Observation and Proteomics Analysis of Root Tips of Wild and Cultivated Soybeans

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