ArticleMolecular pathology : MP2001
The molecular basis of allergenicity: comparative analysis of the three dimensional structures of diverse allergens reveals a common structural motif.
Article in Molecular pathology : MP, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 24 citations in OpenAlex.
- Glutathione exposes sequential IgE-epitopes in ovomucoid relevant in persistent egg allergy.Molecular nutrition & food research · 2013Article
- The protease allergen Pen c 13 induces allergic airway inflammation and changes in epithelial barrier integrity and function in a murine model.The Journal of biological chemistry · 2011Article
- Scientific Opinion on the assessment of allergenicity of GM plants and microorganisms and derived food and feed.EFSA journal. European Food Safety Authority · 2010Article
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Authors and funding
2 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundAlthough a large number of allergens have been characterised, the structural, functional, and biochemical features that these molecules have in common, and that could explain their ability to elicit powerful IgE antibody responses, are still uncertain. Recently, there has been considerable interest in the role of the cysteine protease activity of the house dust mite allergen Der p 1 in biasing the immune response in favour of IgE production.
aimsTo search for remote homologues of Der p 1 with sequences similar to the 30 conserved amino acids surrounding the catalytic cysteine residue (Cys34).
methodsPotential homologues were analysed by examining their three dimensional structures and multiple sequence alignments using the programs PROPSEARCH, ClustalW, GeneDoc, and Swiss Pdb Viewer.
resultsDiverse allergens (for example, the plant cysteine protease papain, the transport protein lipocalin Mus m 1, and the ragweed allergen Amb a 5) have a similar structural motif; namely, a groove resembling the substrate binding groove of Der p 1. The groove is located inside an alpha-beta motif, between an alpha helix on one side and an antiparallel beta sheet on the other side. A similar common motif (a cysteine stabilised alpha-beta fold) can also be found in some toxins and defensins.
conclusionAllergens of diverse sources have a common structural motif, namely a groove located inside an alpha-beta motif, which could potentially serve as a ligand binding site.
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