Molecular Characterisation of Group I Allergen Eur m I from House Dust Mite Euroglyphus mayneiKent N.A.a · Hill M.R.a · Keen J.N.b · Holland P.W.H.a · Hart B.J.a
Departments of aZoology, University of Oxford, Oxford, and bBiochemistry and Molecular Biology, University of Leeds, UK
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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.
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