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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-11-24
pubmed:databankReference
pubmed:abstractText
Birch pollen belongs to the most potent elicitors of Type I allergic reactions in early spring. Using serum IgE from a birch pollen allergic patient, two cDNA clones (clone 6 and clone 13) were isolated from a birch pollen expression cDNA library constructed in phage lambda gt11. Clone 6 encoded a 9.3 kD two EF-hand calcium-binding protein, designated Bet v 4, with significant end to end sequence homology to EF-hand calcium-binding allergens from weed and grass pollen. Recombinant Bet v 4, expressed as beta-galactosidase fusion protein, reacted with serum IgE from approximately 20% of pollen allergic individuals. Depletion of allergenbound calcium by EGTA treatment lead to a substantial reduction of IgE-binding to Bet v 4, indicating that protein-bound calcium is necessary for the maintenance of IgE-epitopes. The greatly reduced IgE-binding capacity of clone 13, a Bet v 4 fragment that lacked the 16 N-terminal amino acids, indicated that the N-terminus contributes significantly to the proteins IgE-binding capacity. By IgE-inhibition experiments it was demonstrated that recombinant Bet v 4 shared IgE-epitopes with natural Bet v 4 and a homologous timothy grass pollen allergen. Recombinant Bet v 4 may therefore be considered as a relevant crossreactive plant allergen, which may be used for diagnosis and treatment of patients suffering from multivalent plant allergies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
239
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
197-204
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:9345295-Allergens, pubmed-meshheading:9345295-Amino Acid Sequence, pubmed-meshheading:9345295-Antibodies, Anti-Idiotypic, pubmed-meshheading:9345295-Antigens, Plant, pubmed-meshheading:9345295-Base Sequence, pubmed-meshheading:9345295-Brassica, pubmed-meshheading:9345295-Calcium-Binding Proteins, pubmed-meshheading:9345295-Cloning, Molecular, pubmed-meshheading:9345295-DNA, Plant, pubmed-meshheading:9345295-Epitopes, B-Lymphocyte, pubmed-meshheading:9345295-Escherichia coli, pubmed-meshheading:9345295-Molecular Sequence Data, pubmed-meshheading:9345295-Plant Proteins, pubmed-meshheading:9345295-Poaceae, pubmed-meshheading:9345295-Protein Binding, pubmed-meshheading:9345295-Recombinant Proteins, pubmed-meshheading:9345295-Sequence Alignment, pubmed-meshheading:9345295-Trees
pubmed:year
1997
pubmed:articleTitle
Molecular characterization, expression in Escherichia coli, and epitope analysis of a two EF-hand calcium-binding birch pollen allergen, Bet v 4.
pubmed:affiliation
Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't