Solution structure of Der f 2, the major mite allergen for atopic diseases

J Biol Chem. 1998 Jan 2;273(1):356-60. doi: 10.1074/jbc.273.1.356.

Abstract

House dust mites cause heavy atopic diseases such as asthma and dermatitis. Among allergens from Dermatophagoides farinae, Der f 2 shows the highest positive rate for atopic patients, but its biological function in mites has been perfectly unknown, as well as the functions of its homologs in human and other animals. We have determined the tertiary structure of Der f 2 by multidimensional nuclear magnetic resonance spectroscopy. Der f 2 was found to be a single-domain protein of immunoglobulin fold, and its structure was the most similar to those of the two regulatory domains of transglutaminase. This fact, binding to the bacterial surface, and other small pieces of information hinted that Der f 2 is related to the innate antibacterial defense system in mites. The immunoglobulin E epitopes are also discussed on the basis of the tertiary structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / chemistry*
  • Allergens / immunology
  • Amino Acid Sequence
  • Animals
  • Antigens, Dermatophagoides
  • Dermatitis, Atopic / immunology*
  • Epitopes / chemistry
  • Epitopes / immunology
  • Glycoproteins / chemistry*
  • Glycoproteins / immunology
  • Humans
  • Immunoglobulin E / immunology
  • Mites / immunology*
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Sequence Homology, Amino Acid
  • Solutions

Substances

  • Allergens
  • Antigens, Dermatophagoides
  • Epitopes
  • Glycoproteins
  • Solutions
  • Immunoglobulin E

Associated data

  • PDB/1AHK
  • PDB/1AHM
  • PDB/R1AHKMR