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J Biol Chem, Vol. 273, Issue 43, 28091-28097, October 23, 1998

Identification and Cloning of Prs a 1, a 32-kDa Endochitinase and Major Allergen of Avocado, and Its Expression in the Yeast Pichia pastoris

Slawomir Sowka, Li-Shan Hsieh, Monika Krebitz, Akira Akasawa^§, Brian M. Martin^¶, David Starrett, Clemens K. Peterbauer, Otto Scheiner, and Heimo Breiteneder

From the Department of General and Experimental Pathology, University of Vienna, AKH-EBO-3Q, Waehringer Guertel 18-20, A-1090 Vienna, Austria, the  Division of Oncology Drug Products, DNDC 1, CDER HFD-150, Rockville, Maryland 20852, the ^§ Department of Allergy, National Children's Hospital, 3-35-31, Taishido, Setagaya-Ku, Tokyo, 154 Japan, the ^¶ Unit of Molecular Structures, Clinical Neuroscience Branch, National Institute of Mental Health, Bethesda, Maryland 20892, and  Biology Department, Southeast Missouri State University, Cape Girardeau, Missouri 63701

Avocado, the fruit of the tropical tree Persea americana, is a source of allergens that can elicit diverse IgE-mediated reactions including anaphylaxis in sensitized individuals. We characterized a 32-kDa major avocado allergen, Prs a 1, which is recognized by 15 out of 20 avocado- and/or latex-allergic patients. Natural Prs a 1 was purified, and its N-terminal and two tryptic peptide sequences were determined. We isolated the Prs a 1 encoding cDNA by PCR using degenerate primers and 5'-rapid amplification of cDNA ends. The Prs a 1 cDNA coded for an endochitinase of 326 amino acids with a leader peptide of 25 amino acids. We expressed Prs a 1 in the yeast Pichia pastoris at 50 mg/liter of culture medium. The recombinant Prs a 1 showed endochitinase activity, inhibited growth and branching of Fusarium oxysporum hyphae, and possessed IgE binding capacity. IgE cross-reactivity with latex proteins including a 20-kDa allergen, most likely prohevein, was demonstrated, providing an explanation for the commonly observed cross-sensitization between avocado and latex proteins. Sequence comparison showed that Prs a 1 and prohevein had 70% similarity in their chitin-binding domains. Characterization of chitinases as allergens has implications for engineering transgenic crops with increased levels of chitinases.

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