Publication Date:
1991-08-02
Description:
A complementary DNA encoding a pollen allergen from white birch (Betula verrucosa) that was isolated from a pollen complementary DNA library with serum immunoglobulin E from a birch pollen-allergic individual revealed significant sequence homology to profilins. The recombinant protein showed high affinity to poly-L-proline. Immunoglobulin E antibodies from allergic individuals bound to natural and recombinant birch profilin and also to human profilin. In addition, birch and human profilin induced histamine release from blood basophils of profilin-allergic individuals, but not of individuals sensitized to other plant allergens. The structural similarity of conserved proteins might therefore be responsible for maintaining immunoglobulin E antibody titers in type I allergy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valenta, R -- Duchene, M -- Pettenburger, K -- Sillaber, C -- Valent, P -- Bettelheim, P -- Breitenbach, M -- Rumpold, H -- Kraft, D -- Scheiner, O -- New York, N.Y. -- Science. 1991 Aug 2;253(5019):557-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of General and Experimental Pathology, University of Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1857985" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Contractile Proteins/immunology
;
Gene Library
;
Humans
;
*Hypersensitivity
;
Immunoblotting
;
Immunoglobulin E/*immunology
;
Microfilament Proteins/genetics/*immunology
;
Molecular Sequence Data
;
Pollen/*immunology
;
Profilins
;
Recombinant Proteins/immunology
;
Saccharomyces cerevisiae/genetics
;
Sequence Homology, Nucleic Acid
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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