| Autor: |
Breiteneder, Heimo, Sowka, Slawomir, Wagner, Stefan, Krebitz, Monika, Hafner, Christine, Kinaciyan, Tamar, Yeang, Hong Yeet, Scheiner, Otto |
| Předmět: |
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| Zdroj: |
International Archives of Allergy & Immunology; 1999, Vol. 118 Issue 2-4, p309-310, 2p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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