¹H, ¹³C and ¹⁵N resonance assignments and second structure information of Gad m 1: a β-parvalbumin allergen from Atlantic cod (Gadus morhua)

Biomol NMR Assign. 2013 Oct;7(2):133-6. doi: 10.1007/s12104-012-9393-y. Epub 2012 May 15.

Abstract

Gad m 1 is the major allergen from Atlantic cod. It belongs to β-parvalbumin protein family and is characterized by the presence of two calcium-binding sites so called EF-hand motifs. β-Parvalbumins such as Gad m 1 are the most important fish allergens and their high cross-reactivity is the cause of the observed polysensitization to various fish species in allergic patients. Despite extensive efforts, the complete elucidation of β-parvalbumin-IgE complexes has not been achieved yet. Allergen structural studies are essential for the development of novel immunotherapy strategies, including vaccination with hypoallergenic derivatives and chimeric molecules. Here, we report for the first time the NMR study of a β-parvalbumin: Gad m 1. This report includes: (1)H, (13)C and (15)N resonance assignments of Gad m 1 as well as the second structure information based on the (13)C chemical shifts.

MeSH terms

  • Allergens / chemistry*
  • Animals
  • Carbon Isotopes
  • Fish Proteins / chemistry*
  • Gadus morhua / metabolism*
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular*
  • Parvalbumins / chemistry*
  • Protein Structure, Secondary
  • Protons*

Substances

  • Allergens
  • Carbon Isotopes
  • Fish Proteins
  • Nitrogen Isotopes
  • Parvalbumins
  • Protons