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Expression of Zm13, a pollen specific maize protein, in Escherichia coli reveals IgE‐binding capacity and allergenic potential
Author(s) -
Heiss Susanne,
Flicker Sabine,
Hamilton Douglas A.,
Kraft Dietrich,
Mascarenhas Joseph P.,
Valenta Rudolf
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00108-1
Subject(s) - escherichia coli , pollen , protein expression , biology , chemistry , biochemistry , botany , gene
Plant proteins belong to the most frequent elicitors of type I allergic symptoms in industrialized countries. Several relevant plant allergens have been found to be either specifically expressed or highly upregulated in mature pollen. The cDNA coding for a pollen specific maize protein, Zm13, shows significant sequence homology with a number of pollen or anther specific proteins from monocot and dicot plants as well as with recently described allergens from olive and rye grass. To test whether the Zm13 protein might possess IgE‐binding capacity, Zm13 was expressed in E coli . The coding region of Zm13 was PCR amplified from a genomic clone and expressed as as a glutathione‐ S ‐transferase fusion protein. The recombinant Zm13 fusion protein bound a Zm13 specific rabbit antiserum and reacted with serum IgE from grass pollen allergic patients indicating that Zm13 and homologous proteins represent a family of conserved plant allergens.