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Panallergens and their impact on the allergic patient

Hauser, Michael, Roulias, Anargyros, Ferreira, Fátima, Egger, Matthias·2010·Allergy, Asthma & Clinical Immunology
DOI 10.1186/1710-1492-6-1PMC PMC2830198
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Abstract

The panallergen concept encompasses families of related proteins, which are involved in general vital processes and thus, widely distributed throughout nature. Plant panallergens share highly conserved sequence regions, structure, and function. They are responsible for many IgE cross-reactions even between unrelated pollen and plant food allergen sources. Although usually considered as minor allergens, sensitization to panallergens might be problematic as it bears the risk of developing multiple sensitizations. Clinical manifestations seem to be tightly connected with geographical and exposure factors. Future population- and disease-based screenings should provide new insights on panallergens and their contribution to disease manifestations. Such information requires molecule-based diagnostics and will be valuable for developing patient-tailored prophylactic and therapeutic approaches. In this article, we focus on profilins, non-specific lipid transfer proteins, polcalcins, and Bet v 1-related proteins and discuss possible consequences of panallergen sensitization for the allergic patient. Based on their pattern of IgE cross-reactivity, which is reflected by their distribution in the plant kingdom, we propose a novel classification of panallergens into ubiquitously spread "real panallergens" (e.g. profilins) and widespread "eurallergens" (e.g. polcalcins). "Stenallergens" display more limited distribution and cross-reactivity patterns, and "monallergens" are restricted to a single allergen source.

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Figures

Figure 1 Three-dimensional structures of allergenic profilins. Secondary structure elements (A) are displayed in green (α-helices) and yellow (β-sheets). The distribution of hydrophilic (blue) and hydrophobic (red) amino acids over the molecular surface is depicted in B. All models were obtained from the Protein Structure Database http://www.pdb.org/pdb/home/home.do and visualized with chimera http://www.cgl.ucsf.edu/chimera/
Figure 1 Three-dimensional structures of allergenic profilins. Secondary structure elements (A) are displayed in green (α-helices) and yellow (β-sheets). The distribution of hydrophilic (blue) and hydrophobic (red) amino acids over the molecular surface is depicted in B. All models were obtained from the Protein Structure Database http://www.pdb.org/pdb/home/home.do and visualized with chimera http://www.cgl.ucsf.edu/chimera/CC BY · PubMed Central
Figure 2 Three-dimensional structures of allergenic polcalcins. Monomeric birch Bet v 4, dimeric timothy grass Phl p 7, and tetrameric goosefoot Che a 3 represent 2EF-polcalcins from tree, grass, and weed pollen. Molecules are depicted in their "holo"-conformation with bound calcium ions illustrated as red balls. Secondary structure elements (A) are shown in green (α-helices) and yellow (β-sheets). The distribution of hydrophilic (blue) and hydrophobic (red) amino acids over the molecular surface is depicted in B. All models were obtained from the Protein Structure Database http://www.pdb.org/pdb/home/home.do and visualized with chimera http://www.cgl.ucsf.edu/chimera/
Figure 2 Three-dimensional structures of allergenic polcalcins. Monomeric birch Bet v 4, dimeric timothy grass Phl p 7, and tetrameric goosefoot Che a 3 represent 2EF-polcalcins from tree, grass, and weed pollen. Molecules are depicted in their "holo"-conformation with bound calcium ions illustrated as red balls. Secondary structure elements (A) are shown in green (α-helices) and yellow (β-sheets). The distribution of hydrophilic (blue) and hydrophobic (red) amino acids over the molecular surface is depicted in B. All models were obtained from the Protein Structure Database http://www.pdb.org/pdb/home/home.do and visualized with chimera http://www.cgl.ucsf.edu/chimera/CC BY · PubMed Central
Figure 3 Three-dimensional structures of nsLTPs. NsLTPs share a common fold that is composed of 4 α-helices (highlighted in green) and stabilized by 4 disulfide bonds (shown in red) to form a central tunnel for ligand interaction (A). The distribution of hydrophilic (blue) and hydrophobic (red) amino acids over the molecular surface is depicted in B. All models were obtained from the Protein Structure Database http://www.pdb.org/pdb/home/home.do and visualized with chimera http://www.cgl.ucsf.edu/chimera/
Figure 3 Three-dimensional structures of nsLTPs. NsLTPs share a common fold that is composed of 4 α-helices (highlighted in green) and stabilized by 4 disulfide bonds (shown in red) to form a central tunnel for ligand interaction (A). The distribution of hydrophilic (blue) and hydrophobic (red) amino acids over the molecular surface is depicted in B. All models were obtained from the Protein Structure Database http://www.pdb.org/pdb/home/home.do and visualized with chimera http://www.cgl.ucsf.edu/chimera/CC BY · PubMed Central
Figure 4 Three-dimensional structures of birch pollen Bet v 1 and homologous food allergens. Structures reveal a typical alpha/beta fold that is responsible for IgE cross-reactivity among related and unrelated species. Secondary structure elements (A) are displayed in green (α-helices), yellow (β-sheets), and grey (loops and turns). The distribution of hydrophilic (blue) and hydrophobic (red) amino acids over the molecular surface is depicted in B. All models were obtained from the Protein Structure Database http://www.pdb.org/pdb/home/home.do and visualized with chimera http://www.cgl.ucsf.edu/chimera/
Figure 4 Three-dimensional structures of birch pollen Bet v 1 and homologous food allergens. Structures reveal a typical alpha/beta fold that is responsible for IgE cross-reactivity among related and unrelated species. Secondary structure elements (A) are displayed in green (α-helices), yellow (β-sheets), and grey (loops and turns). The distribution of hydrophilic (blue) and hydrophobic (red) amino acids over the molecular surface is depicted in B. All models were obtained from the Protein Structure Database http://www.pdb.org/pdb/home/home.do and visualized with chimera http://www.cgl.ucsf.edu/chimera/CC BY · PubMed Central

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Metadata

Authors
Hauser, M., Roulias, A., Ferreira, F., & Egger, M.
Venue
Allergy, Asthma & Clinical Immunology
Publisher
Springer Science and Business Media LLC
Published
2010-01-18
Volume
6
Issue
1
ISSN
1710-1492
DOI
10.1186/1710-1492-6-1
PMC
PMC2830198
Cited by
243
References
1
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Panallergens and their impact on the allergic patient. https://app.cochat.ai/papers/10.1186/1710-1492-6-1
The paper
Hauser, M., Roulias, A., Ferreira, F., & Egger, M. (2010). Panallergens and their impact on the allergic patient. Allergy, Asthma & Clinical Immunology. https://doi.org/10.1186/1710-1492-6-1