Isolation and Characterization of Allergens
Cloning of the Patatin–Like Latex Allergen Hev b 7, Its Expression in the Yeast Pichia pastoris and Its Immunological CharacterizationBreiteneder H.a · Sowka S.a · Wagner S.a · Krebitz M.a · Hafner C.a · Kinaciyan T.b · Yeang H.Y.c · Scheiner O.a
aDepartment of General and Experimental Pathology, University of Vienna, bDivision of Immunology, Allergy and Infectious Diseases, Department of Dermatology, University Hospital, Vienna, Austria; cBiotechnology and Strategic Research Unit, Rubber Research Institute of Malaysia, Kuala Lumpur, Malaysia
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The 43–kD latex allergen Hev b 7 was purified from the latex of Hevea brasiliensis and identified by N–terminal and internal peptide sequences as highly homologous to patatins. Patatins are storage proteins encoded by a multigene family found in plants such as potato and tomato. We have obtained a cDNA clone coding for a cytoplasmic form of Hev b 7. The recombinant protein was expressed in the methylotrophic yeast Pichia pastoris at 10 mg/l culture supernatant. Both natural Hev b 7 and rHev b 7 were recognized by IgE in 11% of the latex–allergic patients. rHev b 7 inhibited binding to its counterpart in natural rubber latex extracts. Purified rHev b 7 used at concentrations of 10 μg/ml in skin prick tests produced wheal–and–flare reactions of sizes equal to those produced by nHev b 7. Furthermore, we were able to show that rHev b 7 possessed esterase activity. A plant expression system for the production of larger quantities of recombinant latex allergens as an alternative to the preparation from H. brasiliensis sap is discussed.
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