LAUSR

BACKGROUND Parvalbumin (PV) could be subdivided into two phylogenetic lineages, αPV and βPV. The bony fish βPV was considered as major fish allergen. However, there is no available report on the immunological property and epitope mapping of bony fish αPV. RESULTS To characterize the allergenic property of bony fish αPV and investigate the difference in allergenic property of bony fish αPV and βPV, turbot (Scophthalmus maximus) αPV and βPV were identified by mass spectrometry and were expressed in E. coli system in this study. Spectra analysis and 3D modeling showed the similar structure between αPV and βPV. αPV exhibited lower IgE/IgG binding capacity than βPV. Three identified βPV epitopes possessed higher IgE reactivity and more hydrophobic residues than three identified αPV epitopes. In addition, less similarity in sequence homology of αPV epitopes was observed with allergen sequences in database. CONCLUSION These finding expanded information on fish PV epitopes and substantiated the difference in allergenicity and epitope mapping between fish αPV and βPV, which will improve the epitope-based detection tools of parvalbumin and diagnostic of parvalbumin induced fish allergy. This article is protected by copyright. All rights reserved.