Monaco DR, Sie BM, Nirschl TR, Knight AC, Sampson HA, Nowak-Wegrzyn A, Wood RA, Hamilton RG, Frischmeyer-Guerrerio PA, Larman HB. *Nature Communications* · January 22, 2021 · DOI: [10.1038/s41467-020-20622-1](https://doi.org/10.1038/s41467-020-20622-1) How to cite ### AMA Monaco DR, Sie BM, Nirschl TR, et al. Profiling serum antibodies with a pan allergen phage library identifies key wheat allergy epitopes. *Nat Commun*. 2021;12(1):379. doi:10.1038/s41467-020-20622-1 ### APA ``` Monaco, D. R., Sie, B. M., Nirschl, T. R., Knight, A. C., Sampson, H. A., Nowak-Wegrzyn, A., Wood, R. A., Hamilton, R. G., Frischmeyer-Guerrerio, P. A., & Larman, H. B. (2021). Profiling serum antibodies with a pan allergen phage library identifies key wheat allergy epitopes. *Nature Communications*, 12(1), 379. https://doi.org/10.1038/s41467-020-20622-1 ``` ### BibTeX ``` @article{monaco2021allerscan, title = {Profiling serum antibodies with a pan allergen phage library identifies key wheat allergy epitopes}, author = {Monaco, Daniel R. and Sie, Brandon M. and Nirschl, Thomas R. and Knight, Audrey C. and Sampson, Hugh A. and Nowak-Wegrzyn, Anna and Wood, Robert A. and Hamilton, Robert G. and Frischmeyer-Guerrerio, Pamela A. and Larman, H. Benjamin}, journal = {Nature Communications}, volume = {12}, number = {1}, pages = {379}, year = {2021}, doi = {10.1038/s41467-020-20622-1} } ``` Monaco and colleagues introduce AllerScan, a programmable phage-display library encoding 19,332 overlapping 56-amino-acid peptide tiles drawn from all 1,847 proteins in the Allergome database. Applied to 58 food-allergic and 25 healthy-control sera, AllerScan resolves the wheat-specific antibody response at single-epitope resolution, separating wheat-allergic from wheat-sensitized individuals and revealing a dominant alpha-purothionin (Tri a 37) IgE epitope. [ Read publication at Nature Communications ](https://doi.org/10.1038/s41467-020-20622-1) In this publication: - AllerScan library encodes 19,332 overlapping 56-amino-acid peptide tiles drawn from all 1,847 proteins in the Allergome database, displayed on T7 bacteriophage for IgE/IgG profiling. - 58 food-allergic patients and 25 healthy controls profiled at single-epitope resolution, separating wheat-allergic from wheat-sensitized phenotypes. - A dominant alpha-purothionin (Tri a 37) IgE epitope emerged as a key serological discriminator of wheat-allergic patients. - The pan-allergen library framework generalizes beyond wheat — positioning AllerScan as a single-workflow assay for allergen-wide epitope mapping across food, environmental, and contact allergens. Wheat is one of the most common food allergens in children, but distinguishing true wheat allergy (IgE-mediated, anaphylaxis-prone) from wheat sensitization (asymptomatic IgE positivity) is clinically difficult with conventional whole-protein assays. The same patient may have measurable wheat-specific IgE without symptoms, or experience anaphylaxis from a single named allergen out of dozens of wheat proteins. Identifying which IgE epitopes drive clinical disease requires resolution that whole-extract assays cannot deliver. To address that gap, the authors built AllerScan, a programmable phage-display library encoding 19,332 overlapping 56-amino-acid peptide tiles drawn from all 1,847 proteins listed in the Allergome database. The library is displayed on T7 bacteriophage and assayed via phage immunoprecipitation sequencing (PhIP-seq), which captures antibody-bound phage from serum and reads them out by next-generation sequencing — producing a residue-resolved map of the patient's allergen-specific antibody repertoire from microliters of serum. Applied to 58 food-allergic patients and 25 healthy controls, AllerScan resolved wheat-specific IgE responses at single-epitope resolution. The analysis cleanly separated wheat-allergic patients from wheat-sensitized individuals and surfaced a dominant IgE epitope on alpha-purothionin (Tri a 37) as a serological hallmark of true wheat allergy. Beyond wheat, the pan-allergen design generalizes — AllerScan can in principle profile epitope-resolved IgE/IgG responses across the entire allergome in a single assay, opening a path toward more accurate allergy diagnostics and personalized immunotherapy planning. 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