Abstract
Methods Recombinant Pla l 1.0101 was heterologously expressed in the E. coli strain Rosetta-gami B pLysS and purified using cation exchange and size exclusion chromatography. Natural Pla l 1 was obtained by pollen extraction and cation exchange chromatography. Physico-chemical properties of the purified proteins were analyzed in gel electrophoresis, mass spectrometry and circular dichroism. Using sera from Austrian ribwort pollen allergic patients (n=20) the IgE-binding activity of natural and recombinant Pla l 1 was investigated in ELISA.
Highlights
ObjectivesThe aim of the study was to express a non-glycosylated Pla l 1 and compare to the natural allergen
Pollen of Plantago lanceolata (English plantain) represent a frequent cause of allergic reactions in patients in the temperate regions of Europe, Australia and North America
Recombinant Pla l 1.0101 was heterologously expressed in the E. coli strain Rosetta-gami B pLysS and purified using cation exchange and size exclusion chromatography
Summary
The aim of the study was to express a non-glycosylated Pla l 1 and compare to the natural allergen
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