One in four atopic children aged 0-5 were allergic to 2S albumin storage proteins, with peanut allergens most common, and proteomic analysis revealed altered serum protein-peptide patterns that could help predict plant food sensitization.
25% allergic to 2S albuminsamong 76 atopic children aged 0-5, with peanut allergens Ara h 1 and Ara h 2 being the most frequent triggers
What the researchers found
Among 76 atopic children aged 0-5, sensitization rates to plant storage proteins were: 25% to 2S albumins, 19.7% to 7S globulins, 13.2% to 11S globulins, and 1.3% to cereal prolamins. The most common allergens were peanut proteins: Ara h 1 (18.4%), Ara h 2 (17.1%), Ara h 6 (15.8%), and Ara h 3 (11.8%), with mean sIgE concentrations of 10.93, 15.353, 15.359, and 9.038 kUA/L respectively.
MALDI-TOF mass spectrometry revealed that four proteins were altered in children allergic to storage proteins: cell cycle control protein 50A, testis-expressed sequence 13B, DENN domain-containing protein 5A, and SKI family transcriptional corepressor 2.
Why it matters
Plant food allergies in young children are a growing concern, and peanut allergy in particular can be life-threatening. Understanding the molecular signatures in blood that accompany these allergies could lead to better diagnostic tools and earlier identification of at-risk children. The proteomic approach opens a window into the broader biological consequences of food allergy beyond just IgE levels.
How the study worked
The study analyzed 76 children aged 0-5 with chronic atopic dermatitis symptoms. Sensitization to 26 plant storage proteins was assessed using the Allergy Explorer ALEX2 multiplex immunoassay. Serum protein-peptide patterns were analyzed using MALDI-TOF mass spectrometry to compare proteomic profiles between children allergic to storage proteins and those who were not.
What this study cannot tell us
The sample size of 76 children is relatively small for drawing broad conclusions about allergy prevalence. The study was limited to children with atopic dermatitis, who have a higher baseline risk of food allergies. The proteomic findings are exploratory and need validation in larger cohorts. The clinical significance of the four altered proteins is not yet clear.
How to read the evidence
This is a cross-sectional observational study with a small sample of 76 children. While the proteomic analysis is rigorous, the findings are exploratory and require validation in larger populations.
When this study was published
Published in 2023, this study represents recent work combining allergy diagnostics with proteomic analysis to better understand food allergy at a molecular level.
The bigger picture
This study combines traditional allergy diagnostics with cutting-edge proteomics to paint a more complete picture of plant food allergy in young children. The discovery that specific serum proteins are altered in allergic children suggests systemic molecular changes beyond simple IgE production. This kind of multi-level approach could eventually enable precision allergy diagnostics and risk prediction.
Questions still open
- Could the altered serum peptide patterns serve as early biomarkers to predict which atopic children will develop food allergies?
- What is the functional role of the four identified proteins in the allergic response?
- Would these proteomic signatures be different in older children or adults with the same allergies?
Common questions
What are plant storage proteins and why do children react to them?
Could a blood test predict which children will develop food allergies?
Read the original research
Changes in Serum Protein-Peptide Patterns in Atopic Children Allergic to Plant Storage Proteins.
International journal of molecular sciences, 24(2)
Citation
Packi, Kacper; Matysiak, Joanna; Matuszewska, Eliza; Bręborowicz, Anna; Matysiak, Jan. (2023). Changes in Serum Protein-Peptide Patterns in Atopic Children Allergic to Plant Storage Proteins.. International journal of molecular sciences, 24(2). https://doi.org/10.3390/ijms24021804