Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2007 Feb;27(1):1-27.
doi: 10.1016/j.iac.2006.11.005.

Bioinformatics approaches to classifying allergens and predicting cross-reactivity

Catherine H Schein  1 , Ovidiu Ivanciuc, Werner Braun
Affiliations
Review

Bioinformatics approaches to classifying allergens and predicting cross-reactivity

Catherine H Schein et al. Immunol Allergy Clin North Am. 2007 Feb.

Abstract

Allergenic proteins from very different environmental sources have similar sequences and structures. This fact may account for multiple allergen syndromes, whereby a myriad of diverse plants and foods may induce a similar IgE-based reaction in certain patients. Identifying the common triggering protein in these sources, in silico, can aid designing individualized therapy for allergen sufferers. This article provides an overview of databases on allergenic proteins, and ways to identify common proteins that may be the cause of multiple allergy syndromes. The major emphasis is on the relational Structural Database of Allergenic Proteins (SDAP []), which includes cross-referenced data on the sequence, structure, and IgE epitopes of over 800 allergenic proteins, coupled with specially developed bioinformatics tools to group all allergens and identify discrete areas that may account for cross-reactivity. SDAP is freely available on the Web to clinicians and patients.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Different products can contain similar allergenic proteins. In this case, an allergen, Jun a 3, originally isolated from the pollen of mountain cedar was found to be a member of the PR5 family of proteins, and was modeled based on its similarity to a protein of known structure, thaumatin [23]. Subsequently, similar allergenic proteins were isolated from many food plants [24], including bell pepper (Cap a 1), cherry (Pru av 2), kiwi (Act c 2), tomato (Lyc e NP24), and apple (Mal d 2).
Figure 2
Figure 2
IgE epitopes mapped on the experimental structure (PDB 1AQZ) of Asp f 1 (a and b) and out MPACK model of Asp f 3 (c and d), two allergens from the fungus causing aspergillosis.
Figure 3
Figure 3
PDB structures for allergens from the four most abundant Pfam families: (a) Pru p 3 (PF00234, protease inhibitor/seed storage/LTP family); (b) Hev b 8, (PF00235, profilin); (c) Bet v 4, (PF00036, EF hand); (d) Phl p 2, (PF01357, pollen allergen).
See this image and copyright information in PMC

References

    1. Sampson HA. Food allergy. Part 2: Diagnosis and management. J Allergy Clin Immunol. 1999;103(6):981–989. - PubMed
    1. Sampson HA. Food allergy. Part 1: Immunopathogenesis and clinical disorders. J Allergy Clin Immunol. 1999;103(5):717–728. - PubMed
    1. Sampson H. Food allergy: When mucosal immunity goes wrong. J Allergy Clin Immunol. 2005;115:139–141. - PubMed
    1. Vanek-Krebitz M, Hoffmannsommergruber K, Machado MLD, et al. Cloning and Sequencing of Mal-D-1, the Major Allergen from Apple (Malus-Domestica), and Its Immunological Relationship to Bet-V-1, the Major Birch Pollen Allergen. Biochem Biophys Res Commun. 1995;214(2):538–551. - PubMed
    1. Scheurer S, Son DY, Boehm M, et al. Cross-reactivity and epitope analysis of Pru a 1, the major cherry allergen. Mol Immunol. 1999;36(3):155–167. - PubMed

Publication types