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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1998-4-16
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pubmed:abstractText |
The interaction of free allergen with two (or more) IgE molecules bound to the high-affinity receptor for IgE (FcepsilonRI) on mast cells and basophilic granulocytes results in the release of inflammatory mediators. The role of allergen-specific IgG antibodies in the allergic reaction in human beings is less clear. We produced two chimeric IgE antibodies, hIgE-Dp2A and hIgE-Dp2B, directed to two nonoverlapping epitopes (A and B) of the house dust mite allergen Der p 2. Chimeric IgG1 and IgG4 variants of these antibodies were produced also. Basophil activation by the house dust mite allergen Der p 2 was induced after sensitization of basophils with a mixture of chimeric hIgE-Dp2A and hIgE-Dp2B antibodies but not after sensitization by the individual IgE antibodies alone. Basophil activation was also shown after sensitization with hIgE-Dp2A and stimulation with Der p 2 incubated with hIgG1-Dp2B or hIgG4-Dp2B antibodies. Both IgE and IgG antibodies directed to the other nonoverlapping epitope complemented the sensitization by the hIgE-Dp2A antibody. Nonsensitized basophils were not activated by the Der p 2/hIgG-Dp2 mixtures. These results indicate that allergen-specific IgG can complement an IgE-dependent reaction and therefore under certain conditions can act as an anaphylactic antibody.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Dermatophagoides,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Heavy Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0091-6749
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
101
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
404-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9525459-Anaphylaxis,
pubmed-meshheading:9525459-Animals,
pubmed-meshheading:9525459-Antibodies, Monoclonal,
pubmed-meshheading:9525459-Antigens, Dermatophagoides,
pubmed-meshheading:9525459-Basophils,
pubmed-meshheading:9525459-Cloning, Molecular,
pubmed-meshheading:9525459-Epitopes,
pubmed-meshheading:9525459-Glycoproteins,
pubmed-meshheading:9525459-Histamine Release,
pubmed-meshheading:9525459-Humans,
pubmed-meshheading:9525459-Immunoglobulin E,
pubmed-meshheading:9525459-Immunoglobulin G,
pubmed-meshheading:9525459-Immunoglobulin Heavy Chains,
pubmed-meshheading:9525459-Mice,
pubmed-meshheading:9525459-Mutagenesis, Insertional,
pubmed-meshheading:9525459-Polymerase Chain Reaction,
pubmed-meshheading:9525459-Recombinant Fusion Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
Complementation of Der P 2-induced histamine release from human basophils sensitized with monoclonal IgE: not only by IgE, but also by IgG antibodies directed to a nonoverlapping epitope of Der p 2.
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pubmed:affiliation |
Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, University of Amsterdam.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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