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Molecular and immunological characterization of profilin from mugwort pollen

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Wopfner, N., Willeroider, M., Hebenstreit, Daniel, Ree, R. van, Aalbers, M., Briza, P., Thalhamer, J., Ebner, C., Richter, K. and Ferreira, F. (2002) Molecular and immunological characterization of profilin from mugwort pollen. Biological Chemistry, Volume 383 (Number 11). pp. 1779-1789. doi:10.1515/BC.2002.199

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Official URL: http://dx.doi.org/10.1515/BC.2002.199

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Abstract

In late summer in Europe, pollen of mugwort is one of the major sources of atopic allergens. No information about the complete molecular structure of any mugwort allergen has been published so far. Here we report the isolation and characterization of mugwort pollen cDNA clones coding for two isoforms of the panallergen profilin. Thirtysix percent of the mugwort allergic patients tested displayed IgE antibodies against natural and recombinant profilin, and no significant differences were observed in the IgEbinding properties of the isoforms. One profilin isoform was purified to homogeneity and detailed structural analysis indicated that the protein exists in solution as dimers and tetramers stabilized by sulfydryl and/or ionic interactions. Profilin monomers were detectable only after exposure of multimers to harsh denaturing conditions. Dimers and tetramers did not significantly differ in their ability to bind serum IgE from mugwort pollenallergic patients. However, oligomeric forms might have a higher allergenic potential than monomers because larger molecules would have additional epitopes for IgEmediated histamine release. Profilin isolated from mugwort pollen also formed multimers. Thus, oligomerization is not an artifact resulting from the recombinant production of the allergen. Inhibition experiments showed extensive IgE crossreactivity of recombinant mugwort profilin and profilin from various pollen and food extracts.

Item Type: Journal Article
Subjects: Q Science > QR Microbiology
Divisions: Faculty of Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Allergens, Gene mapping, Molecular cloning, Oligomerization
Journal or Publication Title: Biological Chemistry
Publisher: Walter de Gruyter & Co
ISSN: 1431-6730
Official Date: June 2002
Dates:
DateEvent
June 2002Published
Volume: Volume 383
Number: Number 11
Page Range: pp. 1779-1789
DOI: 10.1515/BC.2002.199
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: Austria. Bundesministerium für Wissenschaft und Forschung [Federal Ministry of Education, Science and Culture], Österreichische Nationalbank
Grant number: S8802-MED (BWF), S8808-MED (BWF), S8811-MED (BWF), 6927 (ON)

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