NDLI: Reduction in the IgE reactivity of Pacific mackerel parvalbumin by mutations at Ca$^{2+}$-binding sites

Content Provider	Springer Nature Link
Author	Tomura, Satoko Ishizaki, Shoichiro Nagashima, Yuji Shiomi, Kazuo
Copyright Year	2008
Abstract	Parvalbumin is a sarcoplasmic Ca$^{2+}$-binding protein of 12 kDa and represents the major fish allergen. Several peptide segments are identified as immunoglobulin E (lgE)-binding epitopes of cod parvalbumin. However, carp parvalbumin (Cyp c 1) shows a markedly reduced IgE-binding ability upon depletion of Ca$^{2+}$, suggesting the importance of conformational epitopes associated with Ca$^{2+}$-chelating. In this study, the IgE reactivity of Pacific mackerel Scomber japonicus parvalbumin (Sco j 1) was demonstrated to be markedly reduced (60–100% reduction) by Ca$^{2+}$-depletion, similar to Cyp c 1. Three Sco j 1 mutants (D51A, D90A, D51/90A), with modifications in either one or both of the two Ca$^{2+}$-binding sites, were then constructed by site-directed mutagenesis, followed by expression in Escherichia coli, and evaluated for their IgE reactivity. Interestingly, the double mutant (D51/90A), probably devoid of Ca$^{2+}$-binding capacity, exhibited a significantly reduced IgE reactivity (equivalent to 0.0–7.5% of the IgE reactivity of natural Sco j 1). The results suggest that the IgE-binding ability of Sco j 1 largely depends on the solid conformation mediated by Ca$^{2+}$-chelating, and that the hypoallergenic D51/90A will be a useful tool for the specific immunotherapy of fish allergy.
Starting Page	411
Ending Page	417
Page Count	7
File Format	PDF
ISSN	09199268
Journal	Fisheries Science
Volume Number	74
Issue Number	2
e-ISSN	14442906
Language	English
Publisher	Springer-Verlag
Publisher Date	2008-01-01
Publisher Place	Tokyo
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Ca$^{2+}$-binding IgE reactivity mutant Pacific mackerel parvalbumin Fish & Wildlife Biology & Management Freshwater & Marine Ecology Food Science
Content Type	Text
Resource Type	Article
Subject	Aquatic Science

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