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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1997-11-24
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pubmed:databankReference | |
pubmed:abstractText |
Birch pollen belongs to the most potent elicitors of Type I allergic reactions in early spring. Using serum IgE from a birch pollen allergic patient, two cDNA clones (clone 6 and clone 13) were isolated from a birch pollen expression cDNA library constructed in phage lambda gt11. Clone 6 encoded a 9.3 kD two EF-hand calcium-binding protein, designated Bet v 4, with significant end to end sequence homology to EF-hand calcium-binding allergens from weed and grass pollen. Recombinant Bet v 4, expressed as beta-galactosidase fusion protein, reacted with serum IgE from approximately 20% of pollen allergic individuals. Depletion of allergenbound calcium by EGTA treatment lead to a substantial reduction of IgE-binding to Bet v 4, indicating that protein-bound calcium is necessary for the maintenance of IgE-epitopes. The greatly reduced IgE-binding capacity of clone 13, a Bet v 4 fragment that lacked the 16 N-terminal amino acids, indicated that the N-terminus contributes significantly to the proteins IgE-binding capacity. By IgE-inhibition experiments it was demonstrated that recombinant Bet v 4 shared IgE-epitopes with natural Bet v 4 and a homologous timothy grass pollen allergen. Recombinant Bet v 4 may therefore be considered as a relevant crossreactive plant allergen, which may be used for diagnosis and treatment of patients suffering from multivalent plant allergies.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Anti-Idiotypic,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes, B-Lymphocyte,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/anti-IgE
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
239
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
197-204
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9345295-Allergens,
pubmed-meshheading:9345295-Amino Acid Sequence,
pubmed-meshheading:9345295-Antibodies, Anti-Idiotypic,
pubmed-meshheading:9345295-Antigens, Plant,
pubmed-meshheading:9345295-Base Sequence,
pubmed-meshheading:9345295-Brassica,
pubmed-meshheading:9345295-Calcium-Binding Proteins,
pubmed-meshheading:9345295-Cloning, Molecular,
pubmed-meshheading:9345295-DNA, Plant,
pubmed-meshheading:9345295-Epitopes, B-Lymphocyte,
pubmed-meshheading:9345295-Escherichia coli,
pubmed-meshheading:9345295-Molecular Sequence Data,
pubmed-meshheading:9345295-Plant Proteins,
pubmed-meshheading:9345295-Poaceae,
pubmed-meshheading:9345295-Protein Binding,
pubmed-meshheading:9345295-Recombinant Proteins,
pubmed-meshheading:9345295-Sequence Alignment,
pubmed-meshheading:9345295-Trees
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pubmed:year |
1997
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pubmed:articleTitle |
Molecular characterization, expression in Escherichia coli, and epitope analysis of a two EF-hand calcium-binding birch pollen allergen, Bet v 4.
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pubmed:affiliation |
Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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