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.

Type

Journal article

Journal

Int Arch Allergy Immunol

Publication Date

1992

Volume

99

Pages

150 - 152

Keywords

Allergens, Amino Acid Sequence, Animals, Antigens, Dermatophagoides, Arthropod Proteins, Base Sequence, Cloning, Molecular, DNA, Insect Hormones, Insect Proteins, Mites, Molecular Sequence Data, Polymerase Chain Reaction, Sequence Homology, Amino Acid