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* Institute of Medical and Chemical Laboratory Diagnostics,
Department of Internal Medicine I, Division of Hematology, and
Department of Pathophysiology, Vienna General Hospital, University of Vienna, Vienna, Austria; and
Division of Structural Biology, Institute for Chemistry, University of Graz, Graz, Austria
IgE-mediated reactions to fish allergens represent one of the most
frequent causes of food allergy. We have constructed an expression cDNA
library from carp (Cyprinus carpio) muscle in phage
gt11 and used serum IgE from a fish allergic patient to isolate 33
cDNA clones that coded for two parvalbumin isoforms (Cyp c 1.01 and Cyp
c 1.02) with comparable IgE binding capacities. Both isoforms
represented calcium-binding proteins that belonged to the 
-lineage
of parvalbumins. The Cyp c 1.01 cDNA was overexpressed in
Escherichia coli, and rCyp c 1.01 was purified to
homogeneity. Circular dichroism analysis and mass spectroscopy showed
that rCyp c 1.01 represented a folded protein with mainly 
-helical
secondary structure and a molecular mass of 11,416 Da,
respectively. rCyp c 1.01 reacted with IgE from all fish-allergic
patients tested (n = 60), induced specific and
dose-dependent basophil histamine release, and contained most of the
IgE epitopes (70%) present in natural allergen extracts from cod,
tuna, and salmon. Therefore, it may be used to identify patients
suffering from IgE-mediated fish allergy. The therapeutic potential of
rCyp c 1.01 is indicated by our findings that rabbit Abs raised against
rCyp c 1.01 inhibited the binding of IgE (n = 25)
in fish-allergic patients to rCyp c 1.01 between 35 and 97% (84% mean
inhibition) and that depletion of calcium strongly reduced IgE
recognition of rCyp c 1.01. The latter results suggest that it will be
possible to develop strategies for immunotherapy for fish allergy that
are based on calcium-free hypoallergenic rCyp c 1.01
derivatives.
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