| pubmed-article:10224228 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10224228 | lifeskim:mentions | umls-concept:C0002092 | lld:lifeskim |
| pubmed-article:10224228 | lifeskim:mentions | umls-concept:C0440330 | lld:lifeskim |
| pubmed-article:10224228 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:10224228 | lifeskim:mentions | umls-concept:C0020846 | lld:lifeskim |
| pubmed-article:10224228 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:10224228 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:10224228 | pubmed:dateCreated | 1999-5-25 | lld:pubmed |
| pubmed-article:10224228 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10224228 | pubmed:abstractText | Type I allergy, an immunodisorder that affects almost 20% of the population worldwide, is based on the immunoglobulin E (IgE) recognition of per se innocuous antigens (allergens). Pollen from wind-pollinated plants belong to the most potent allergen sources. We report the isolation of a cDNA coding for a 8.6 kDa two EF-hand calcium binding allergen, Phl p 7, from a timothy grass (Phleum pratense) pollen expression cDNA library, using serum IgE from a grass pollen allergic patient. Sequence analysis identified Phl p 7 as a member of a recently discovered subfamily of pollen-specific calcium binding proteins. Recombinant Phl p 7 was expressed in Escherichia coli and purified to homogeneity as determined by mass spectroscopy. Approximately 10% of pollen allergic patients displayed IgE reactivity to rPhl p 7 and Phl p 7-homologous allergens present in pollens of monocotyledonic and dicotyledonic plants. Circular dichroism analysis of the calcium-bound and apo-rPhl p 7 indicated that differences in IgE recognition may be due to calcium-induced changes in the protein conformation. The fact that patients mount IgE antibodies against different protein conformations is interpreted as a footprint of a preferential sensitization against either form. The biological activity of rPhl p 7 was demonstrated by its ability to induce basophil histamine release and immediate type skin reactions in sensitized individuals. In conclusion, IgE binding to Phl p 7 represents an example for the conformation-dependent IgE recognition of an allergen. Recombinant Phl p 7 may be used for diagnosis and perhaps treatment of a group of patients who suffer from allergy to pollens of many unrelated plant species. | lld:pubmed |
| pubmed-article:10224228 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10224228 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10224228 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10224228 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10224228 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10224228 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10224228 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10224228 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10224228 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10224228 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10224228 | pubmed:month | May | lld:pubmed |
| pubmed-article:10224228 | pubmed:issn | 0892-6638 | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:KraftDD | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:HayesJJ | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:EhrenbergerKK | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:RumpoldHH | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:ValentPP | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:ValentaRR | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:SperrW RWR | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:VrtalaSS | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:SpitzauerSS | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:LafferSS | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:VangelistaLL | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:NiederbergerV... | lld:pubmed |
| pubmed-article:10224228 | pubmed:author | pubmed-author:TwardoszAA | lld:pubmed |
| pubmed-article:10224228 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10224228 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:10224228 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10224228 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10224228 | pubmed:pagination | 843-56 | lld:pubmed |
| pubmed-article:10224228 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10224228 | pubmed:meshHeading | pubmed-meshheading:10224228... | lld:pubmed |
| pubmed-article:10224228 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10224228 | pubmed:articleTitle | Calcium-dependent immunoglobulin E recognition of the apo- and calcium-bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7. | lld:pubmed |
| pubmed-article:10224228 | pubmed:affiliation | Department of Otorhinolaryngology, Institute of Medical and Chemical Laboratory Diagnostics, University of Vienna, Austria. | lld:pubmed |
| pubmed-article:10224228 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10224228 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:10224228 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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