Ulrike Griesmeier

Publications (2)8.6 Total impact

• Article: Physicochemical properties and thermal stability of Lep w 1, the major allergen of whiff.

  Ulrike Griesmeier, Merima Bublin, Christian Radauer, Sonia Vázquez-Cortés, Yan Ma, Montserrat Fernández-Rivas, Heimo Breiteneder
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  ABSTRACT: Whiff (Lepidorhombus whiffiagonis) is a fish frequently consumed in Spain. Lep w 1, its major allergen, is a calcium-binding beta-parvalbumin. The resistance of Lep w 1 to heat denaturation and to digestion were studied by circular dichroism spectroscopy and by in vitro gastric digestion systems. Purified Lep w 1 was thermally stable up to 65 degrees C at neutral pH. Calcium depletion resulted in a change of its structure as determined by circular dichroism spectroscopy. A partial loss of structure was also observed at acidic pH; however, the allergen retained its full IgE-binding ability. The partially denatured Lep w 1 was easily digested by pepsin within 2 min. Further, the IgE reactivity of proteins extracted from cooked fish and their stability to proteolysis were analyzed. The extract revealed a higher number of IgE reactive bands than an extract from uncooked fish. IgE binding to these proteins could not be inhibited by an extract from uncooked fish. In contrast to a raw fish extract, the cooked extract showed higher resistance to pepsinolysis. The stability of Lep w 1 to thermal denaturation and digestion explains the high allergenicity of whiff.
  Molecular Nutrition & Food Research 11/2009; 54(6):861-9. · 4.30 Impact Factor
• Source

  Available from: Peter Briza

  Article: Comparison of natural and recombinant forms of the major fish allergen parvalbumin from cod and carp.

  Yan Ma, Ulrike Griesmeier, Markus Susani, Christian Radauer, Peter Briza, Anja Erler, Merima Bublin, Stefano Alessandri, Martin Himly, Sonia Vàzquez-Cortés, Isabel Reig Rincon de Arellano, Emilia Vassilopoulou, Photini Saxoni-Papageorgiou, André C Knulst, Montserrat Fernández-Rivas, Karin Hoffmann-Sommergruber, Heimo Breiteneder
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  ABSTRACT: 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 beta-parvalbumins. We cloned and expressed cDNAs encoding cod (Gadus morhua) and carp (Cyprinus carpio) beta-parvalbumins and purified natural cod beta-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.
  Molecular Nutrition & Food Research 06/2008; 52 Suppl 2:S196-207. · 4.30 Impact Factor