Solution and high-pressure NMR studies of the structure, dynamics, and stability of the cross-reactive allergenic cod parvalbumin Gad m 1.
Beta-parvalbumins from different fish species have been identified as the main elicitors of IgE-mediated reactions in fish-allergic individuals. Here, we report for the first time the NMR determination of the structure and dynamics of the major Atlantic cod (Gadus morhua) allergen Gad m 1 and compare them with other known parvalbumins. Although the Gad m 1 structure and accessibility of putative IgE epitopes are similar to parvalbumins in mackerel and carp, the charge distribution at the putative epitopes is different. The determination of the Gad m 1 structure contributes to a better understanding of cross-reactivity among fish parvalbumins. In addition, the high-pressure NMR and temperature variation experiments revealed the important contribution of the AB motif and other regions to the protein folding. This structural information could assist the future identification of hot spots for targeted mutations to develop hypoallergenic Ca(2+) -free forms for potential use in immunotherapy.
['Moraes|Adolfo H|AH|', 'Ackerbauer|Daniela|D|', 'Kostadinova|Maria|M|', 'Bublin|Merima|M|', 'de Oliveira|Guilherme Augusto|GA|', 'Ferreira|Fátima|F|', 'Almeida|Fabio C L|FC|', 'Breiteneder|Heimo|H|', 'Valente|Ana Paula|AP|']
D000485:Allergens D000595:Amino Acid Sequence D000818:Animals D001665:Binding Sites D002118:Calcium D003429:Cross Reactions D029941:Fish Proteins D048389:Gadus morhua D008958:Models, Molecular D008969:Molecular Sequence Data D019906:Nuclear Magnetic Resonance, Biomolecular D010320:Parvalbumins D011312:Pressure D011487:Protein Conformation D055550:Protein Stability D012996:Solutions D040681:Structural Homology, Protein D013696:Temperature
high-pressure NMR cross-reactivity allergenicity protein structure β-parvalbumin