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a Institute of Medical
and Chemical Laboratory Diagnostics, AKH, University of Vienna, Austria, b Institute of Medical Physics and
Biophysics, University of Münster, Germany, c European Molecular Biology Laboratory
(EMBL), Heidelberg, Germany, d Department
of Internal Medicine I, Division of Haematology, AKH, University of
Vienna, Austria, e Molecular Structure Division, National Institute
for Medical Research, London, UK, f Department of Pathophysiology, AKH, University
of Vienna, Austria
Correspondence to: Dr R Valenta, Molecular Immunopathology Group, Department of Pathophysiology, Vienna General Hospital, University of Vienna, Währinger Gürtel 18-20, A-1090 Vienna, Austria
Accepted for publication 3 November 1999
BACKGROUND
Almost 4%
of the population suffer from food allergy which is an adverse reaction
to food with an underlying immunological mechanism.
AIMSTo characterise
one of the most frequent IgE defined food allergens, fish parvalbumin.
METHODSTissue and
subcellular distribution of carp parvalbumin was analysed by immunogold
electron microscopy and cell fractionation. Parvalbumin was purified to
homogeneity, analysed by mass spectrometry and circular dichroism (CD)
spectroscopy, and its allergenic activity was analysed by IgE binding
and basophil histamine release tests.
RESULTSThe
isoelectric point (pI) 4.7 form of carp parvalbumin, a three EF-hand
calcium-binding protein, was purified to homogeneity. CD analysis
revealed a remarkable stability and refolding capacity of calcium-bound
parvalbumin. This may explain why parvalbumin, despite cooking and
exposure to the gastrointestinal tract, can sensitise patients.
Purified parvalbumin reacted with IgE of more than 95% of individuals
allergic to fish, induced dose-dependent basophil histamine release and
contained, on average, 83% of the IgE epitopes present in other fish
species. Calcium depletion reduced the IgE binding capacity of
parvalbumin which, according to CD analysis, may be due to
conformation-dependent IgE recognition.
CONCLUSIONSPurified
carp parvalbumin represents an important cross reactive food allergen.
It can be used for in vitro and in vivo diagnosis of fish-induced food
allergy. Our finding that the apo-form of parvalbumin had a greatly
reduced IgE binding capacity indicates that this form may be a
candidate for safe immunotherapy of fish-related food allergy.
This article has been cited by other articles:
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  I. Swoboda, A. Bugajska-Schretter, B. Linhart, P. Verdino, W. Keller, U. Schulmeister, W. R. Sperr, P. Valent, G. Peltre, S. Quirce, et al. A Recombinant Hypoallergenic Parvalbumin Mutant for Immunotherapy of IgE-Mediated Fish Allergy J. Immunol., May 15, 2007; 178(10): 6290 - 6296. [Abstract] [Full Text] [PDF]
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I. Swoboda, A. Bugajska-Schretter, P. Verdino, W. Keller, W. R. Sperr, P. Valent, R. Valenta, and S. Spitzauer Recombinant Carp Parvalbumin, the Major Cross-Reactive Fish Allergen: A Tool for Diagnosis and Therapy of Fish Allergy J. Immunol., May 1, 2002; 168(9): 4576 - 4584. [Abstract] [Full Text] [PDF]
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S. Flicker, S. Vrtala, P. Steinberger, L. Vangelista, A. Bufe, A. Petersen, M. Ghannadan, W. R. Sperr, P. Valent, L. Norderhaug, et al. A Human Monoclonal IgE Antibody Defines a Highly Allergenic Fragment of the Major Timothy Grass Pollen Allergen, Phl p 5: Molecular, Immunological, and Structural Characterization of the Epitope-Containing Domain J. Immunol., October 1, 2000; 165(7): 3849 - 3859. [Abstract] [Full Text] [PDF]
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