Linked Life Data

10224228

Source:http://linkedlifedata.com/resource/pubmed/id/10224228

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1999-5-25
pubmed:databankReference
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0892-6638
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
843-56
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10224228-Allergens, pubmed-meshheading:10224228-Amino Acid Sequence, pubmed-meshheading:10224228-Animals, pubmed-meshheading:10224228-Apoproteins, pubmed-meshheading:10224228-Base Sequence, pubmed-meshheading:10224228-Calcium, pubmed-meshheading:10224228-Cross Reactions, pubmed-meshheading:10224228-DNA, Complementary, pubmed-meshheading:10224228-DNA, Plant, pubmed-meshheading:10224228-DNA Primers, pubmed-meshheading:10224228-Escherichia coli, pubmed-meshheading:10224228-Histamine Release, pubmed-meshheading:10224228-Humans, pubmed-meshheading:10224228-Hypersensitivity, Immediate, pubmed-meshheading:10224228-Immunoglobulin E, pubmed-meshheading:10224228-Models, Molecular, pubmed-meshheading:10224228-Molecular Sequence Data, pubmed-meshheading:10224228-Plant Proteins, pubmed-meshheading:10224228-Poaceae, pubmed-meshheading:10224228-Pollen, pubmed-meshheading:10224228-Protein Conformation, pubmed-meshheading:10224228-Rabbits, pubmed-meshheading:10224228-Recombinant Proteins, pubmed-meshheading:10224228-Sequence Homology, Amino Acid
pubmed:year
1999
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.
pubmed:affiliation
Department of Otorhinolaryngology, Institute of Medical and Chemical Laboratory Diagnostics, University of Vienna, Austria.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't