Abstract
The number of tree-pollen-allergic patients showing allergic reactions to apples, various vegetables and nuts is increasing. In this paper the molecular characterization of the major apple allergen, Mal d 1, is reported. The cDNA coding for Mal d 1 was cloned and sequenced. Its open reading frame codes for a protein of 159 amino acids with a predicted molecular mass of 17.7 kDa and a predicted pI of 5.9. Sequence comparison to Bet v 1, the major birch pollen allergen, revealed 64.5% identity on the amino acid level and 55.6% identity on the nucleic acid level. Recombinant Mal d 1 was expressed in the plasmid pMW 175 in E. coli BL 21 (DE3) and its immunological properties were tested. Crossreactivity with Bet v 1 was shown by inhibition assays.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Allergens*
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Amino Acid Sequence
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Antigens, Plant
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Base Sequence
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Cloning, Molecular
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Cross Reactions
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DNA Primers
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DNA, Complementary
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DNA, Plant / chemistry
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DNA, Plant / metabolism
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Fruit
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Immunoblotting
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Molecular Sequence Data
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Molecular Weight
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Plant Proteins / biosynthesis*
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Plant Proteins / chemistry*
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Plant Proteins / immunology
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Polymerase Chain Reaction
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RNA, Messenger / biosynthesis
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RNA, Messenger / isolation & purification
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / immunology
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Sequence Homology, Amino Acid
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Trees
Substances
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Allergens
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Antigens, Plant
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DNA Primers
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DNA, Complementary
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DNA, Plant
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MALD1 protein, Malus domestica
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Plant Proteins
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RNA, Messenger
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Recombinant Proteins
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Bet v 1 allergen, Betula