cDNA cloning and characterization of a cross-reactive birch pollen allergen: Identification as a pectin esterase

International Archives of Allergy and Immunology

Volumn 124, Issue 1-3, 2001, Pages 64-66

  Mahler, V ^a,b   Fischer, S ^a   Heiss, S ^a   Duchene M ^a   Kraft, D ^a   Valenta, Rudolf ^a,c  

^a UNIVERSITY OF VIENNA   (Austria)

^b UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

^c UNIVERSITY OF VIENNA   (Austria)

Author keywords

Birch pollen allergen; cDNA cloning; Cross reactivity; Pectin esterase

Indexed keywords

COMPLEMENTARY DNA; ESTERASE; PECTIN; POLLEN ANTIGEN;

ALLERGY; AMINO ACID SEQUENCE; CONFERENCE PAPER; CONTROLLED STUDY; CROSS REACTION; DNA LIBRARY; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; MOLECULAR CLONING; PRIORITY JOURNAL; SEQUENCE HOMOLOGY;

ALLERGENS; CARBOXYLIC ESTER HYDROLASES; CLONING, MOLECULAR; CROSS REACTIONS; DNA, COMPLEMENTARY; HUMANS; IMMUNOGLOBULIN E; PLANT PROTEINS; POLLEN; SEQUENCE HOMOLOGY, AMINO ACID; TREES;

EID: 0035051462     PISSN: 10182438     EISSN: None     Source Type: Journal    
DOI: 10.1159/000053670     Document Type: Conference Paper

References (12)

1. The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene
2. Identification of profilin as a novel pollen allergen; IgE autoreactivity in sensitized individuals
3. Profilins constitute a novel family of functional plant pan-allergens
4. Characterization of a birch pollen allergen, Bet v III, representing a novel class of Ca(2+)binding proteins: Specific expression in mature pollen and dependence of patients' IgE binding on protein-bound Ca(2+)
5. Molecular characterization, expression in Escherichia coli, and epitope analysis of a two EF-hand calcium-binding birch pollen allergen, Bet v 4
6. Molecular cloning and characterization of a birch pollen minor allergen, Bet v 5, belonging to a family of isoflavone reductase-related proteins
7. Purification and characterization of an 18-kd allergen of birch(Betula verrucosa)pollen: Identification as a cyclophilin
8. Recombinant birch pollen allergens (rBet v 1 and rBet v 2) contain most of the IgE epitopes present in birch, alder, hornbeam, hazel, and oak pollen: A quantitative IgE inhibition study with sera from different populations
9. Quantitative IgE inhibition experiments with purified recombinant allergens indicate pollen-derived allergens as the sensitizing agents responsible for many forms of plant food allergy
10. Plant and animal profilins are functionally equivalent and stabilize microfilaments in living animal cells
11. Comparison of recombinant timothy grass pollen allergens with natural extract for diagnosis of grass pollen allergy in different populations
12. Sense and antisense inactivation of fruit ripening genes in tomato