Molecular characterisation of group I allergen Eur m I from house dust mite Euroglyphus maynei

Int Arch Allergy Immunol. 1992;99(1):150-2. doi: 10.1159/000236349.

Abstract

Using the polymerase chain reaction (PCR) we have amplified and cloned genomic DNA encoding the secreted group I allergen proteins from the house dust mite species Euroglyphus maynei, Dermatophagoides pteronyssinus and D. farinae. Affinity chromatography using a monoclonal antibody to the allergen Der p I was used to purify the group I protein from E. maynei. We present the deduced amino acid sequence of a new member of the group I house dust mite allergen family Eur m I. The three proteins show a high level of primary structure similarity: Eur m I and Der p I show 85% amino acid identity, and the three allergen amino acid sequences taken together show 78% identity. A potential N-glycosylation site and residues of the cysteine protease active site are also conserved between the three proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / genetics*
  • Amino Acid Sequence
  • Animals
  • Antigens, Dermatophagoides
  • Arthropod Proteins
  • Base Sequence
  • Cloning, Molecular
  • DNA / analysis
  • Insect Hormones / genetics*
  • Insect Hormones / isolation & purification
  • Insect Proteins*
  • Mites / genetics*
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Sequence Homology, Amino Acid

Substances

  • Allergens
  • Antigens, Dermatophagoides
  • Arthropod Proteins
  • Eur m I protein, Euroglyphus maynei
  • Insect Hormones
  • Insect Proteins
  • DNA

Associated data

  • GENBANK/X60073
  • GENBANK/X65196
  • GENBANK/X65197