Open AccessProduction of non‐glycosylated recombinant Pla l 1, the main allergen of Plantago lanceolata
Author(s) -
Stemeseder Teresa,
Eichhorn Stephanie,
Schuller Sabrina,
Lang Roland,
Briza Peter,
Hawranek Thomas,
Ferreira Fatima,
Gadermaier Gabriele
Publication year - 2014
Publication title -
clinical and translational allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.979
H-Index - 37
ISSN - 2045-7022
DOI - 10.1186/2045-7022-4-s2-p15
Subject(s) - medicine , recombinant dna , allergen , allergy , plantaginaceae , plantago , traditional medicine , immunology , botany , biochemistry , biology , gene
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.