Medizinische Universit├Ąt Graz - Research portal

Logo MUG Resarch Portal

Selected Publication:

SHR Neuro Cancer Cardio Lipid

Ball, T; Edstrom, W; Mauch, L; Schmitt, J; Leistler, B; Fiebig, H; Sperr, WR; Hauswirth, AW; Valent, P; Kraft, D; Almo, SC; Valenta, R.
Gain of structure and IgE epitopes by eukaryotic expression of the major Timothy grass pollen allergen, Phl p 1.
FEBS J. 2005; 272(1): 217-227. [OPEN ACCESS]
Web of Science PubMed FullText FullText_MUG

 

Authors Med Uni Graz:
Ball Tanja
Altmetrics:

Dimensions Citations:

Plum Analytics:
Abstract:
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 diffract to 2.9 A resolution. The importance of conformational epitopes for IgE recognition of Phl p 1 is demonstrated by the superior IgE recognition of insect-cell expressed Phl p 1 compared to Escherichia coli-expressed Phl p 1. Moreover, insect cell-expressed Phl p 1 induces potent histamine release and leads to strong up-regulation of CD203c in basophils from grass pollen allergic patients. Deglycosylated Phl p 1 frequently exhibits higher IgE binding capacity than the recombinant glycoprotein suggesting that rather the intact protein structure than carbohydrate moieties themselves are important for IgE recognition of Phl p 1. This study emphasizes the important contribution of conformational epitopes for the IgE recognition of respiratory allergens and provides a paradigmatic tool for the structural analysis of the IgE allergen interaction.
Find related publications in this database (using NLM MeSH Indexing)
Allergens - genetics Allergens - immunology
Animals -
Cell Line -
Epitopes - chemistry
Humans -
Immunoglobulin E - immunology
Mass Spectrometry -
Phylogeny -
Plant Proteins - genetics Plant Proteins - immunology
Recombinant Proteins - genetics Recombinant Proteins - immunology
Spodoptera -

Find related publications in this database (Keywords)
allergen
allergy
epitope
eukaryotic expression
Phl p 1
© Meduni GrazImprint