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http://purl.uniprot.org/citations/12653800http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12653800http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12653800http://www.w3.org/2000/01/rdf-schema#comment"

Background

Class I chitinase in natural rubber latex (NRL) has been assumed to be an important allergen, especially concerning its cross-reactivity with fruits like avocado and banana.

Objectives

The present study aimed to produce a recombinant latex class I chitinase from Hevea brasiliensis leaves and to study its immunoglobulin (Ig)E-binding reactivity.

Methods

A class I chitinase-specific complementary DNA from H. brasiliensis leaves was synthesized, subcloned, sequenced and overexpressed in fusion with the maltose-binding protein (MBP) in Escherichia coli. The IgE-binding reactivity of this protein was studied by the Pharmacia CAP System and by immunoblot experiments using sera from latex-allergic patients.

Results

The rHev b 11.0102 was found to have a length of 295 amino acid residues and contains an N-terminal hevein-like domain with a 56% homology to hevein. Analysis by the CAP method revealed the presence of rHev b 11.0102-specific IgE antibodies in 17 of 58 sera (29%) of IgE-mediated latex-allergic subjects tested. Immunoblot analysis of the MBP-rHev b 11.0102 fusion protein and the MBP carrier protein as a negative control confirmed the IgE-reactivity of rHev b 11.0102.

Conclusion

Due to its IgE-reactivity rHev b 11.0102 represents an allergen of intermediate prevalence in NRL. Its property to cross-react with certain fruits makes it an important supplement in the diagnostic panel of recombinant NRL allergens."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.org/dc/terms/identifier"doi:10.1034/j.1398-9995.2003.00058.x"xsd:string
http://purl.uniprot.org/citations/12653800http://purl.org/dc/terms/identifier"doi:10.1034/j.1398-9995.2003.00058.x"xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Bruening T."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Bruening T."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Cremer R."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Cremer R."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Dumont B."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Dumont B."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Lundberg M."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Lundberg M."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Raulf-Heimsoth M."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Raulf-Heimsoth M."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Rihs H.P."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Rihs H.P."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Rozynek P."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/author"Rozynek P."xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/name"Allergy"xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/name"Allergy"xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/pages"246-251"xsd:string
http://purl.uniprot.org/citations/12653800http://purl.uniprot.org/core/pages"246-251"xsd:string
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