| Isolation and immunological characterization of a novel Cladosporium herbarum allergen structurally homologous to the alpha/beta hydrolase fold superfamily. | |
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MedLine Citation:
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PMID: 20022636 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Because the ascomycete Cladosporium herbarum embodies one of the most important, world-wide occurring fungal species responsible for eliciting typical IgE-mediated hypersensitivity reactions ranging from rhinitis and ocular symptoms to severe involvement of the lower respiratory tract, a more comprehensive definition of its detailed allergen repertoire is unquestionably of critical medical as well as therapeutic significance. By screening a C. herbarum cDNA library with IgE antibodies pooled from 3 mold-reactive sera, we were able to identify, clone and affinity-purify a novel allergen candidate (29.9 kDa) exhibiting considerable (three-dimensional) homology to the alpha/beta hydrolase fold superfamily. The latter covers a collection of hydrolytic enzymes of widely differing phylogenetic origin as well as catalytic activity (operating in countless biological contexts) that in general exhibit only little sequence similarity yet show a remarkable conservation of structural topology. Our present study (i) characterizes recombinant non-fusion C. herbarum hydrolase as a natively folded, minor mold allergen that displays a prevalence of IgE reactivity of approximately 17% in our in vitro immunoblot experiments, (ii) proposes the existence of several putative (speculatively cross-reactive) ascomycete orthologues as determined via genome-wide in silico predictions, and (iii) finally implies that C. herbarum hydrolase could be included in forthcoming minimal testing sets when fungal allergy is suspected. |
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Authors:
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Raphaela Rid; Kamil Onder; Thomas Hawranek; Martin Laimer; Johann W Bauer; Claudia Holler; Birgit Simon-Nobbe; Michael Breitenbach |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2009-12-22 |
Journal Detail:
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Title: Molecular immunology Volume: 47 ISSN: 1872-9142 ISO Abbreviation: Mol. Immunol. Publication Date: 2010 Mar |
Date Detail:
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Created Date: 2010-03-01 Completed Date: 2010-03-23 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7905289 Medline TA: Mol Immunol Country: England |
Other Details:
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Languages: eng Pagination: 1366-77 Citation Subset: IM |
Copyright Information:
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Copyright 2009 Elsevier Ltd. All rights reserved. |
Affiliation:
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Department of Cell Biology, Division of Genetics, University of Salzburg, Salzburg, Austria. Raphaela.Rid@sbg.ac.at |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/DQ159861 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Allergens
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chemistry,
genetics,
immunology*,
isolation & purification* Amino Acid Sequence Base Sequence Cladosporium / enzymology*, immunology* Humans Hydrolases / chemistry, genetics, immunology*, isolation & purification* Immunoblotting Immunoglobulin E / immunology Models, Molecular Molecular Sequence Data Multigene Family Protein Renaturation Recombinant Proteins / immunology Sequence Alignment Structural Homology, Protein* |
| Chemical | |
Reg. No./Substance:
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0/Allergens; 0/Recombinant Proteins; 37341-29-0/Immunoglobulin E; EC 3.-/Hydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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