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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1996-12-27
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pubmed:databankReference |
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pubmed:abstractText |
Bet v 1 and homologous proteins represent major cross-reactive allergens for more than 95% of tree pollen-, fruit-, and vegetable-allergic individuals. To study the interaction of Bet v 1 and the immune system, we characterized a Bet v 1-specific mAb, Bip 1. Soluble rBip 1 Fabs were expressed in Escherichia coli and purified by affinity chromatography using immobilized Bet v 1. Bip 1 Fabs displayed a cross-reactivity to homologous allergens comparable with that of IgE Abs from allergic patients. Preincubation of Bet v 1 with Bip 1 led to an up to fivefold increase of allergic patients' IgE binding to Bet v 1. This enhancement in IgE binding may be interpreted as stabilization of a Bet v 1 state, in which certain IgE epitopes are better applicable. It also shows that allergic patients possess IgE Abs directed against different Bet v 1 conformations. The modulation of Ab binding to a given Ag by other Abs was observed also for human Bet v 1-specific IgG Abs, and may represent a novel mechanism for the regulation of specific humoral immune responses in a complex network.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Bet v 1 allergen, Betula,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Fab Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
157
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4953-62
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pubmed:dateRevised |
2011-6-21
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pubmed:meshHeading |
pubmed-meshheading:8943401-Allergens,
pubmed-meshheading:8943401-Amino Acid Sequence,
pubmed-meshheading:8943401-Antibodies, Monoclonal,
pubmed-meshheading:8943401-Antigens, Plant,
pubmed-meshheading:8943401-Base Sequence,
pubmed-meshheading:8943401-Cloning, Molecular,
pubmed-meshheading:8943401-Cross Reactions,
pubmed-meshheading:8943401-DNA, Complementary,
pubmed-meshheading:8943401-Escherichia coli,
pubmed-meshheading:8943401-Humans,
pubmed-meshheading:8943401-Immunoglobulin E,
pubmed-meshheading:8943401-Immunoglobulin Fab Fragments,
pubmed-meshheading:8943401-Molecular Sequence Data,
pubmed-meshheading:8943401-Molecular Structure,
pubmed-meshheading:8943401-Plant Proteins,
pubmed-meshheading:8943401-Pollen,
pubmed-meshheading:8943401-Protein Folding,
pubmed-meshheading:8943401-Recombinant Proteins,
pubmed-meshheading:8943401-Rhinitis, Allergic, Seasonal,
pubmed-meshheading:8943401-Sequence Homology, Amino Acid,
pubmed-meshheading:8943401-Solubility
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pubmed:year |
1996
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pubmed:articleTitle |
Molecular characterization of Bip 1, a monoclonal antibody that modulates IgE binding to birch pollen allergen, Bet v 1.
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pubmed:affiliation |
Institute of General and Experimental Pathology, Vienna General Hospital (AKH), University of Vienna, Austria.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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