Molecular characterisation of group I allergen Eur m I from house dust mite Euroglyphus maynei.
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.
Kent
N A
NA
Department of Zoology, University of Oxford, UK.
Hill
M R
MR
Keen
J N
JN
Holland
P W
PW
Hart
B J
BJ
D000485:Allergens / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D039741:Antigens, Dermatophagoides; D060829:Arthropod Proteins; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis; D007301:Insect Hormones / Q000235:genetics* / Q000302:isolation & purification; D019476:Insect Proteins; D008925:Mites / Q000235:genetics*; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid
D000485:Allergens; D039741:Antigens, Dermatophagoides; D060829:Arthropod Proteins; C079269:Eur m I protein, Euroglyphus maynei; D007301:Insect Hormones; D019476:Insect Proteins; D004247:DNA