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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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Author

  • M Gajhede
  • Peter Osmark
  • F M Poulsen
  • H Ipsen
  • J N Larsen
  • R J Joost van Neerven
  • C Schou
  • H Lowenstein
  • M D Spangfort

Summary, in English

The three-dimensional structure of the major birch pollen allergen, the 17,500 M(r) acidic protein Bet v 1 (from the birch, Betula verrucosa), is presented as determined both in the crystalline state by X-ray diffraction and in solution by nuclear magnetic resonance (NMR) spectroscopy. This is the first experimentally determined structure of a clinically important inhalant major allergen, estimated to cause allergy in 5-10 million individuals worldwide. The structure shows three regions on the molecular surface predicted to harbour cross-reactive B-cell epitopes which provide a structural basis for the allergic symptoms that birch pollen allergic patients show when they encounter pollens from related trees such as hazel, alder and hornbeam. The structure also shows an unusual feature, a 30 A-long forked cavity that penetrates the entire protein.

Publishing year

1996

Language

English

Pages

1040-1045

Publication/Series

Nature Structural Biology

Volume

3

Issue

12

Document type

Journal article

Publisher

Nature Publishing Group

Topic

  • Endocrinology and Diabetes

Status

Published

ISBN/ISSN/Other

  • ISSN: 1072-8368