Source:http://linkedlifedata.com/resource/pubmed/id/12581204
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2003-2-12
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pubmed:abstractText |
We have previously cloned, expressed and characterized two variants of the major allergen Lep d 2 from cultured Lepidoglyphus destructor mites. These variants, Lep d 2.0101 and Lep d 2.0201, differ at 13 amino acid positions. In this study we investigated Lep d 2 sequence diversity between wild and cultured mites. PCR, Southern blot and DNA sequence analysis revealed the presence of two different Lep d 2 genes, one with and one without an intron. In addition, two new variants of Lep d 2, Lep d 2.0102 and Lep d 2.0202, were found at different frequencies in wild and cultured mites. When we expressed the Lep d 2 variants and compared their IgE binding properties by ELISA inhibition, we found that Lep d 2.0102 was a more potent inhibitor than Lep d 2.0101, and to a lesser extent Lep d 2.0202 was more potent than Lep d 2.0201. Long-term cultures of peripheral blood mononuclear cells were used to assess the ability of the expressed Lep d 2 variants to induce cytokine release. Although cells from different individuals released different amounts of interferon-gamma and interleukin-5, no consistent cytokine release pattern could be linked to any specific Lep d 2 variant. In conclusion, we show that both cultured and wild Lepidoglyphus destructor mites contain the same pattern of polymorphism. Furthermore, this Lep d 2 sequence diversity seems not to have any significant impact on the allergens IgE binding or its ability to induce T cell cytokine release.
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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/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-5,
http://linkedlifedata.com/resource/pubmed/chemical/Lep d I allergen,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
646-53
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12581204-Allergens,
pubmed-meshheading:12581204-Amino Acid Sequence,
pubmed-meshheading:12581204-Animals,
pubmed-meshheading:12581204-Blotting, Southern,
pubmed-meshheading:12581204-Cloning, Molecular,
pubmed-meshheading:12581204-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:12581204-Immunoblotting,
pubmed-meshheading:12581204-Immunoglobulin E,
pubmed-meshheading:12581204-Interferon-gamma,
pubmed-meshheading:12581204-Interleukin-5,
pubmed-meshheading:12581204-Mites,
pubmed-meshheading:12581204-Molecular Sequence Data,
pubmed-meshheading:12581204-Mutagenesis, Site-Directed,
pubmed-meshheading:12581204-Polymerase Chain Reaction,
pubmed-meshheading:12581204-Polymorphism, Genetic,
pubmed-meshheading:12581204-Proteins,
pubmed-meshheading:12581204-Sequence Homology, Amino Acid,
pubmed-meshheading:12581204-T-Lymphocytes
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pubmed:year |
2003
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pubmed:articleTitle |
Lep d 2 polymorphisms in wild and cultured Lepidoglyphus destructor mites.
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pubmed:affiliation |
Department of Medicine, Unit of Clinical Immunology and Allergy, Karolinska Hospital and Institute, Stockholm, Sweden. liselotte.kaiser@ks.se
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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