TY - JOUR
TI - Comparison of natural and recombinant forms of the major fish allergen parvalbumin from cod and carp
AU - Ma, Y.
AU - Griesmeier, U.
AU - Susani, M.
AU - Radauer, C.
AU - Briza, P.
AU - Erler, A.
AU - Bublin, M.
AU - Alessandri, S.
AU - Himly, M.
AU - Vàzquez-Cortés, S.
AU - De Arellano, I.R.R.
AU - Vassilopoulou, E.
AU - Saxoni-Papageorgiou, P.
AU - Knulst, A.C.
AU - Fernández-Rivas, M.
AU - Hoffmann-Sommergruber, K.
AU - Breiteneder, H.
JO - Molecular Nutrition and Food Research
PY - 2008
VL - 52
TODO - SUPPL. 2
SP - S196-S207
PB - 
SN - null
TODO - 10.1002/mnfr.200700284
TODO - allergen;  calcium;  immunoglobulin E;  parvalbumin;  recombinant protein, amino acid sequence;  animal;  article;  carp;  chemistry;  circular dichroism;  comparative study;  cross reaction;  Gadiformes;  immunology;  isolation and purification;  mass spectrometry;  metabolism;  molecular cloning;  molecular genetics;  nuclear magnetic resonance spectroscopy;  pH, Allergens;  Amino Acid Sequence;  Animals;  Calcium;  Carps;  Circular Dichroism;  Cloning, Molecular;  Cross Reactions;  Gadiformes;  Hydrogen-Ion Concentration;  Immunoglobulin E;  Magnetic Resonance Spectroscopy;  Mass Spectrometry;  Molecular Sequence Data;  Parvalbumins;  Recombinant Proteins, Cyprinidae;  Cyprinus carpio;  Gadus morhua
TODO - Allergic reaction following fish consumption can trigger life-threatening reactions in predisposed individuals. Parvalbumins from different species have been identified as the major fish allergens. There are two distinct phylogenetic lineages of parvalbumins, alpha and beta. Most allergic reactions are caused by β-parvalbumins. We cloned and expressed cDNAs encoding cod (Gadus morhua) and carp (Cyprinus carpio) β-parvalbumins and purified natural cod β-parvalbumin. CD spectra of the purified proteins showed that their overall secondary structure contents were very similar. No differences in thermal stability were monitored in the calcium-bound or calcium-depleted form of natural cod parvalbumin. IgE reactivity was assessed using 26 sera of fish allergic patients from Spain, The Netherlands, and Greece in immunoblot and ELISA experiments. Twenty-five of the 26 patients with IgE reactivity to native and recombinant cod parvalbumin also reacted to the recombinant carp parvalbumin. IgE inhibition assays were performed using cod and carp extracts and purified recombinant parvalbumin of cod and carp. High crossreactivity among cod and carp parvalbumins was observed in immunoblots as well as in fluid phase assays. Natural and recombinant parvalbumins gave comparable results when performing various in vitro diagnostic assays. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
ER -