Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Predicting the allergenicity of legume proteins using a PBMC gene expression assay_Biomarker search study

ABSTRACT: Food proteins differ in their allergenic potential. Currently, there is no predictive and validated bio-assay to evaluate the allergenicity of novel food proteins. The objective of this study was to investigate the potential of a human peripheral blood mononuclear cell (PBMC) gene expression assay to identify biomarkers to predict the allergenicity of legume proteins. PBMCs from healthy donors were exposed to weakly and strongly allergenic legume proteins. Inclusion of multiple protein pairs from 2S albumins (lupine and peanut) and 7S globulins (white bean and soybean) in a larger study, led to the selection of CCL2, CCL7, and RASD2 as biomarkers to distinguish weakly from strongly allergenic proteins.

ORGANISM(S): Homo sapiens

PROVIDER: GSE169030 | GEO | 2021/03/17

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Predicting the allergenicity of legume proteins using a PBMC gene expression assay_Pilot experiment

Project description:Food proteins differ in their allergenic potential. Currently, there is no predictive and validated bio-assay to evaluate the allergenicity of novel food proteins. The objective of this study was to investigate the potential of a human peripheral blood mononuclear cell (PBMC) gene expression assay to identify biomarkers to predict the allergenicity of legume proteins. PBMCs from healthy donors were exposed to weakly and strongly allergenic legume proteins. Possible biomarkers for allergenicity were investigated by exposing PBMCs to a protein pair of weakly (white bean) and strongly allergenic (soybean) 7S globulins in a pilot experiment. Gene expression was measured by RNA-sequencing and differentially expressed genes were selected as biomarkers. 153 genes were identified as having significantly different expression levels to the 7S globulin of white bean compared to soybean.

2021-03-17 | GSE168698 | GEO

Roasted English Walnut Label-Free LC-MS/MS Quantification

Project description:Thermal processing of allergenic foods has the potential to induce a number of changes in the constituent allergens, but many of the effects of heat treatment are poorly defined. Like numerous other commonly allergenic tree nuts, walnuts often undergo heat treatment, such as roasting, prior to consumption. This study evaluated the changes in solubility and detectability of allergens from roasted walnuts using tandem mass spectrometry methods. Walnuts were roasted at 132 °C or 180 °C for 5, 10, or 20 minutes prior to preparation for LC-MS/MS using sequential or simultaneous protocols for extraction and trypsin digestion. LC-MS/MS data analysis incorporated label-free quantification and Maillard adduct screening. Relatively minor changes in detection were demonstrated following roasting in some allergenic proteins (2S albumin, LTP, and the 7S vicilin N-terminal region) with the LC-MS/MS method. The mature 7S vicilin and 11S legumin, however, showed significantly increased detection in the highest heat treatment sample when using the simultaneous extraction/digestion protocol, an effect likely due to increased digestibility of the proteins following heating. The results of this study indicate that individual walnut allergens respond differently to thermal processing, and the detection of these proteins by LC-MS/MS is dependent on the protein in question, its susceptibility to proteolytic digestion, the degree of thermal processing, and the sample preparation methodology.

2016-05-18 | PXD000907 | Pride

Legume Diet Satiety Pilot Study

Project description:This pilot study is designed to test the effects of a high legume (dried bean) diet on hunger and other indicators of health over the course of eight weeks, compared to a more conventional healthy diet.

| 2176646 | ecrin-mdr-crc

Predicting the allergenicity of legume proteins using a PBMC gene expression assay

Project description:Predicting the allergenicity of legume proteins using a PBMC gene expression assay

| PRJNA714929 | ENA

Predicting the allergenicity of legume proteins using a PBMC gene expression assay_Pilot experiment

Project description:Predicting the allergenicity of legume proteins using a PBMC gene expression assay_Pilot experiment

| PRJNA714918 | ENA

Transcription profiling of Medicago trunculata leaf tissue over-expressing Legume Anthocyanin Production

Project description:Transcription profiling of leaf tissue from Medicago truncatula over-expressing Legume Anthocyanin Production.

2009-10-13 | E-MEXP-1854 | biostudies-arrayexpress

GNPS - legume consumption untargeted MS data

Project description:Legume consumption untargeted MS data. SEED grant protocol; methanol extraction.

2019-12-05 | MSV000084663 | GNPS

Transcription profiling of Medicago sativa leaf tissue in transgenic alfalfa expressing Legume Anthocyanin Production

Project description:Gene expression profiling of leaf tissue in transgenic alfalfa expressing Legume Anthocyanin Production 1.

2009-10-13 | E-MEXP-1855 | biostudies-arrayexpress

Proteomic analysis of rhLF expressed in Komagataella phaffii

Project description:Prior to the introduction of novel food ingredients into the food supply, safety risk assessments are required, and numerous prediction models have been developed and validated to evaluate safety. The allergenic risk potential of Helaina recombinant human lactoferrin (rhLF, Effera™), produced in Komagataella phaffii (K. phaffii) was assessed by literature search, bioinformatics sequence comparisons to known allergens, glycan allergenicity assessment, and a simulated pepsin digestion model. The literature search identified no allergenic risk for Helaina rhLF, K. phaffii, or its glycans. Bioinformatics search strategies showed no significant risk for cross-reactivity or allergenicity between rhLF or the 36 residual host proteins and known human allergens. Helaina rhLF was also rapidly digested in simulated gastric fluid and its digestibility profile was comparable to human milk lactoferrin (hmLF), further demonstrating a low allergenic risk and similarity to the hmLF form. Collectively, these results demonstrate a low allergenic risk potential of Helaina rhLF and do not support the need for further clinical testing or serum IgE binding to evaluate Helaina rhLF for risk of food allergy prior to addition into the food supply.

2024-10-17 | PXD053985 | Pride

Predicting the allergenicity of legume proteins using a PBMC gene expression assay_Biomarker search study

Project description:Predicting the allergenicity of legume proteins using a PBMC gene expression assay_Biomarker search study

| PRJNA714933 | ENA