tailieunhanh - Báo cáo khoa học: Gain of structure and IgE epitopes by eukaryotic expression of the major Timothy grass pollen allergen, Phl p 1

Approximately 400 million allergic patients are sensitized against group 1 grass pollen allergens, a family of highly cross-reactive allergens present in all grass species. We report the eukaryotic expression of the group 1 aller-gen from Timothy grass, Phl p 1, in baculovirus-infected insect cells. Domain elucidation by limited proteolysis and mass spectrometry of the purified recombinant glycoprotein indicates that the C-terminal 40% of Phl p 1, a major IgE-reactive segment, represents a stable domain | ềFEBS Journal Gain of structure and IgE epitopes by eukaryotic expression of the major Timothy grass pollen allergen Phl p 1 Tanja Ball1 2 William Edstrom2 Ludwig Mauch3 Jacky Schmitt3 Bernd Leistler3 Helmut Fiebig4 Wolfgang R. Sperr5 Alexander W. Hauswirth5 Peter Valent5 Dietrich Kraft1 Steven C. Almo2 and Rudolf Valenta1 1 Department of Pathophysiology Center for Physiology and Pathophysiology MedicalUniversity of Vienna Austria 2 Albert Einstein College of Medicine Department of Biochemistry NY USA 3 Pharmacia Diagnostics Freiburg Germany 4 Allergopharma KG Reinbek Germany 5 Division of Hematology Department of InternalMedicine I MedicalUniversity of Vienna Austria Keywords allergen allergy epitope eukaryotic expression Phlp 1 Correspondence R. Valenta Division of Immunopathology Department of Pathophysiology Center for Physiology and Pathophysiology Medical University of Vienna Waehringer Guertel 18-20 A-1090 Vienna Austria Fax 43 1 40 400 5130 Tel 43 1 40 400 5108 E-mail Received 6 August 2004 revised 21 September 2004 accepted 22 September 2004 doi Approximately 400 million allergic patients are sensitized against group 1 grass pollen allergens a family of highly cross-reactive allergens present in all grass species. We report the eukaryotic expression of the group 1 allergen from Timothy grass Phl p 1 in baculovirus-infected insect cells. Domain elucidation by limited proteolysis and mass spectrometry of the purified recombinant glycoprotein indicates that the C-terminal 40 of Phl p 1 a major IgE-reactive segment represents a stable domain. This domain also exhibits a significant sequence identity of 43 with the family of immunoglobulin domain-like group 2 3 grass pollen allergens. Circular dichroism analysis demonstrates that insect cell-expressed rPhl p 1 is a folded species with significant secondary structure. This material is well behaved and is adequate for the growth of crystals that .

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