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Molecular and immunologic characterization of a highly cross-reactive two EF-hand calcium-binding alder pollen allergen, Aln g 4: structural basis for calcium-modulated IgE recognition.
J Immunol. 1998 Dec 15; 161(12):7031-9.JI

Abstract

Serum IgE was used to isolate a cDNA coding for a 9.4-kDa two EF-hand calcium-binding allergen, Aln g 4, from a lambda gt11 expression cDNA library constructed from alder (Alnus glutinosa) pollen. rAln g 4 was overexpressed in Escherichia coli and purified to homogeneity. It reacted with serum IgE from 18% of pollen-allergic patients (n = 122); shared IgE epitopes with homologous allergens present in tree, grass, and weed pollens; and thus belongs to a family of highly cross-reactive pollen allergens. Exposure of two E. coli-expressed rAln g 4 fragments comprising amino acids 1-41 and 42-85 to patients' IgE Abs, as well as to a rabbit antiserum raised against purified rAln g 4, indicated that most of the B cell epitopes reside in the N-terminal portion of the protein. IgE recognition of Aln g 4 was strongly modulated by the presence or absence of calcium. Circular dichroism analysis of rAln g 4 revealed that the protein consisted mostly of alpha helical secondary structure and possessed a remarkable thermal stability and refolding capacity, a property that was greatly reduced after calcium depletion. Circular dichroism analysis of the calcium-bound and apo form of rAln g 4 indicated that calcium-induced modulation of IgE binding could be due to changes in the protein conformation. Purified rAln g 4 elicited dose-dependent basophil histamine release and immediate type skin reactions in sensitized patients. It may hence be useful for allergy diagnosis and for specific immunotherapy.

Authors+Show Affiliations

Department of General and Experimental Pathology, AKH, 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 availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

9862740

Citation

Hayek, B, et al. "Molecular and Immunologic Characterization of a Highly Cross-reactive Two EF-hand Calcium-binding Alder Pollen Allergen, Aln G 4: Structural Basis for Calcium-modulated IgE Recognition." Journal of Immunology (Baltimore, Md. : 1950), vol. 161, no. 12, 1998, pp. 7031-9.
Hayek B, Vangelista L, Pastore A, et al. Molecular and immunologic characterization of a highly cross-reactive two EF-hand calcium-binding alder pollen allergen, Aln g 4: structural basis for calcium-modulated IgE recognition. J Immunol. 1998;161(12):7031-9.
Hayek, B., Vangelista, L., Pastore, A., Sperr, W. R., Valent, P., Vrtala, S., Niederberger, V., Twardosz, A., Kraft, D., & Valenta, R. (1998). Molecular and immunologic characterization of a highly cross-reactive two EF-hand calcium-binding alder pollen allergen, Aln g 4: structural basis for calcium-modulated IgE recognition. Journal of Immunology (Baltimore, Md. : 1950), 161(12), 7031-9.
Hayek B, et al. Molecular and Immunologic Characterization of a Highly Cross-reactive Two EF-hand Calcium-binding Alder Pollen Allergen, Aln G 4: Structural Basis for Calcium-modulated IgE Recognition. J Immunol. 1998 Dec 15;161(12):7031-9. PubMed PMID: 9862740.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular and immunologic characterization of a highly cross-reactive two EF-hand calcium-binding alder pollen allergen, Aln g 4: structural basis for calcium-modulated IgE recognition. AU - Hayek,B, AU - Vangelista,L, AU - Pastore,A, AU - Sperr,W R, AU - Valent,P, AU - Vrtala,S, AU - Niederberger,V, AU - Twardosz,A, AU - Kraft,D, AU - Valenta,R, PY - 1998/12/23/pubmed PY - 1998/12/23/medline PY - 1998/12/23/entrez SP - 7031 EP - 9 JF - Journal of immunology (Baltimore, Md. : 1950) JO - J. Immunol. VL - 161 IS - 12 N2 - Serum IgE was used to isolate a cDNA coding for a 9.4-kDa two EF-hand calcium-binding allergen, Aln g 4, from a lambda gt11 expression cDNA library constructed from alder (Alnus glutinosa) pollen. rAln g 4 was overexpressed in Escherichia coli and purified to homogeneity. It reacted with serum IgE from 18% of pollen-allergic patients (n = 122); shared IgE epitopes with homologous allergens present in tree, grass, and weed pollens; and thus belongs to a family of highly cross-reactive pollen allergens. Exposure of two E. coli-expressed rAln g 4 fragments comprising amino acids 1-41 and 42-85 to patients' IgE Abs, as well as to a rabbit antiserum raised against purified rAln g 4, indicated that most of the B cell epitopes reside in the N-terminal portion of the protein. IgE recognition of Aln g 4 was strongly modulated by the presence or absence of calcium. Circular dichroism analysis of rAln g 4 revealed that the protein consisted mostly of alpha helical secondary structure and possessed a remarkable thermal stability and refolding capacity, a property that was greatly reduced after calcium depletion. Circular dichroism analysis of the calcium-bound and apo form of rAln g 4 indicated that calcium-induced modulation of IgE binding could be due to changes in the protein conformation. Purified rAln g 4 elicited dose-dependent basophil histamine release and immediate type skin reactions in sensitized patients. It may hence be useful for allergy diagnosis and for specific immunotherapy. SN - 0022-1767 UR - https://www.unboundmedicine.com/medline/citation/9862740/Molecular_and_immunologic_characterization_of_a_highly_cross_reactive_two_EF_hand_calcium_binding_alder_pollen_allergen_Aln_g_4:_structural_basis_for_calcium_modulated_IgE_recognition_ L2 - http://www.jimmunol.org/cgi/pmidlookup?view=long&pmid=9862740 DB - PRIME DP - Unbound Medicine ER -