Source:http://linkedlifedata.com/resource/pubmed/id/11054118
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
22
|
| pubmed:dateCreated |
2000-12-5
|
| pubmed:abstractText |
Der f 2 is the major group 2 allergen from house dust mite Dermatophagoides farinae and is composed of 129 amino-acid residues. Wild-type and six proline mutants of Der f 2 (P26A, P34A, P66A, P79A, P95A, and P99A) expressed in Escherichia coli were refolded and purified. Formations of intramolecular disulfide bonds in the purified proteins were confirmed correct. The apparent molecular masses analyzed by gel-filtration were 14-15 kDa. The IgE-binding capacity in the sera of seven mite-allergic patients, inhibitory activity for IgE-binding to immobilized wild-type Der f 2, and activity to stimulate peripheral blood basophils to release histamine in two volunteers were analyzed. P95A and P99A, which slightly differed from the wild-type Der f 2 in their CD spectrum, showed reduced IgE-binding, reduced inhibitory activity, and less histamine-releasing activity than the wild-type. P34A also showed reduced allergenicity. Considering that Pro95, Pro99 and Pro34 are closely located in loops at one end of the tertiary structure of Der f 2, we concluded that these loop regions included an IgE-binding site common to all tested patients. P66A showed reduced IgE-binding in two sera out of seven. P26A and P79A showed no reduced allergenicity. However, in immunoblot analysis after SDS/PAGE under reduced conditions, P79A showed no or markedly reduced IgE-binding while the other mutants showed IgE-binding corresponding to that in the assay using correctly refolded proteins. This suggests that Pro79 is involved in refolding of Der f 2. The findings in this study are important for the understanding of the antigenic structure of mite group 2 allergens and for manipulation of the allergens for specific immunotherapy.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Dermatophagoides,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0014-2956
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
267
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
6650-6
|
| pubmed:dateRevised |
2007-7-23
|
| pubmed:meshHeading |
pubmed-meshheading:11054118-Allergens,
pubmed-meshheading:11054118-Amino Acid Substitution,
pubmed-meshheading:11054118-Animals,
pubmed-meshheading:11054118-Antigens, Dermatophagoides,
pubmed-meshheading:11054118-Basophils,
pubmed-meshheading:11054118-Binding Sites,
pubmed-meshheading:11054118-Circular Dichroism,
pubmed-meshheading:11054118-Disulfides,
pubmed-meshheading:11054118-Glycoproteins,
pubmed-meshheading:11054118-Histamine Release,
pubmed-meshheading:11054118-Humans,
pubmed-meshheading:11054118-Immunoenzyme Techniques,
pubmed-meshheading:11054118-Immunoglobulin E,
pubmed-meshheading:11054118-Mites,
pubmed-meshheading:11054118-Models, Molecular,
pubmed-meshheading:11054118-Mutagenesis, Site-Directed,
pubmed-meshheading:11054118-Proline,
pubmed-meshheading:11054118-Protein Conformation,
pubmed-meshheading:11054118-Protein Structure, Secondary,
pubmed-meshheading:11054118-Recombinant Proteins
|
| pubmed:year |
2000
|
| pubmed:articleTitle |
Effects of proline mutations in the major house dust mite allergen Der f 2 on IgE-binding and histamine-releasing activity.
|
| pubmed:affiliation |
Bioscience Research and Development Laboratory, Asahi Breweries, Ltd, Ibaraki, Japan. toshiro.takai@asahibeer.co.jp
|
| pubmed:publicationType |
Journal Article
|