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Spatial clustering of the IgE epitopes on the major timothy grass pollen allergen Phl p 1: importance for allergenic activity.
J Allergy Clin Immunol. 2006 Jun; 117(6):1336-43.JA

Abstract

BACKGROUND

The major timothy grass pollen allergen Phl p 1 is one of the most potent and frequently recognized environmental allergens.

OBJECTIVE

We sought to study at a molecular and structural level the IgE recognition of Phl p 1 and its relation to allergenic activity.

METHODS

Monoclonal human IgE antibody fragments specific for Phl p 1 and group 1 allergens from various grasses were isolated from a combinatorial library made of lymphocytes from patients with grass pollen allergy. Recombinant Phl p 1 fragments and the 3-dimensional structure of Phl p 1 were used to localize the major binding site for the IgE antibodies. A rPhl p 1 fragment containing this binding site was expressed in Escherichia coli, purified, and tested for IgE reactivity and allergenic activity with sera and basophils from patients with grass pollen allergy.

RESULTS

Monoclonal antibodies, as well as polyclonal serum IgE, from patients with grass pollen allergy defined a C-terminal fragment of Phl p 1 that represents a sterically oriented portion on the Phl p 1 structure. This Phl p 1 portion bound most of the allergen-specific IgE antibodies and contained the majority of the allergenic activity of Phl p 1.

CONCLUSION

IgE recognition of spatially clustered epitopes on allergens might be a general factor determining their allergenic activity.

CLINICAL IMPLICATIONS

Geographic distribution of IgE epitopes on an allergen might influence its allergenic activity and hence explain discrepancies between diagnostic test results based on IgE serology and provocation testing. It might also form a basis for the development of low allergenic vaccines.

Authors+Show Affiliations

Department of Pathophysiology, Center for Physiology and Pathophysiology, Medical University of Vienna, Austria.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16750995

Citation

Flicker, Sabine, et al. "Spatial Clustering of the IgE Epitopes On the Major Timothy Grass Pollen Allergen Phl P 1: Importance for Allergenic Activity." The Journal of Allergy and Clinical Immunology, vol. 117, no. 6, 2006, pp. 1336-43.
Flicker S, Steinberger P, Ball T, et al. Spatial clustering of the IgE epitopes on the major timothy grass pollen allergen Phl p 1: importance for allergenic activity. J Allergy Clin Immunol. 2006;117(6):1336-43.
Flicker, S., Steinberger, P., Ball, T., Krauth, M. T., Verdino, P., Valent, P., Almo, S., & Valenta, R. (2006). Spatial clustering of the IgE epitopes on the major timothy grass pollen allergen Phl p 1: importance for allergenic activity. The Journal of Allergy and Clinical Immunology, 117(6), 1336-43.
Flicker S, et al. Spatial Clustering of the IgE Epitopes On the Major Timothy Grass Pollen Allergen Phl P 1: Importance for Allergenic Activity. J Allergy Clin Immunol. 2006;117(6):1336-43. PubMed PMID: 16750995.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Spatial clustering of the IgE epitopes on the major timothy grass pollen allergen Phl p 1: importance for allergenic activity. AU - Flicker,Sabine, AU - Steinberger,Peter, AU - Ball,Tanja, AU - Krauth,Maria-Theresa, AU - Verdino,Petra, AU - Valent,Peter, AU - Almo,Steve, AU - Valenta,Rudolf, Y1 - 2006/04/27/ PY - 2005/11/08/received PY - 2006/01/04/revised PY - 2006/02/03/accepted PY - 2006/6/6/pubmed PY - 2006/7/20/medline PY - 2006/6/6/entrez SP - 1336 EP - 43 JF - The Journal of allergy and clinical immunology JO - J Allergy Clin Immunol VL - 117 IS - 6 N2 - BACKGROUND: The major timothy grass pollen allergen Phl p 1 is one of the most potent and frequently recognized environmental allergens. OBJECTIVE: We sought to study at a molecular and structural level the IgE recognition of Phl p 1 and its relation to allergenic activity. METHODS: Monoclonal human IgE antibody fragments specific for Phl p 1 and group 1 allergens from various grasses were isolated from a combinatorial library made of lymphocytes from patients with grass pollen allergy. Recombinant Phl p 1 fragments and the 3-dimensional structure of Phl p 1 were used to localize the major binding site for the IgE antibodies. A rPhl p 1 fragment containing this binding site was expressed in Escherichia coli, purified, and tested for IgE reactivity and allergenic activity with sera and basophils from patients with grass pollen allergy. RESULTS: Monoclonal antibodies, as well as polyclonal serum IgE, from patients with grass pollen allergy defined a C-terminal fragment of Phl p 1 that represents a sterically oriented portion on the Phl p 1 structure. This Phl p 1 portion bound most of the allergen-specific IgE antibodies and contained the majority of the allergenic activity of Phl p 1. CONCLUSION: IgE recognition of spatially clustered epitopes on allergens might be a general factor determining their allergenic activity. CLINICAL IMPLICATIONS: Geographic distribution of IgE epitopes on an allergen might influence its allergenic activity and hence explain discrepancies between diagnostic test results based on IgE serology and provocation testing. It might also form a basis for the development of low allergenic vaccines. SN - 0091-6749 UR - https://www.unboundmedicine.com/medline/citation/16750995/Spatial_clustering_of_the_IgE_epitopes_on_the_major_timothy_grass_pollen_allergen_Phl_p_1:_importance_for_allergenic_activity_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0091-6749(06)00324-1 DB - PRIME DP - Unbound Medicine ER -