title: Relevance of the recombinant lipid transfer protein of Hevea brasiliensis: IgE-binding reactivity in fruit-allergic adults.
abstract: BACKGROUND
  Lipid transfer proteins (LTPs) are relevant allergens in certain plants. The role of the LTP of Hevea brasiliensis in the latex-fruit syndrome is widely unknown.
  
  
  OBJECTIVE
  To study IgE reactivity with recombinant Hevea LTP in sera of fruit-allergic adults with and without natural rubber latex (NRL) allergy.
  
  
  METHODS
  An LTP-specific complementary DNA of H brasiliensis leaves was amplified, subcloned into the pMAL expression system, and analyzed. The recombinant protein was coupled to ImmunoCAP, and the IgE-binding properties were studied in sera of 10 NRL-allergic patients without symptoms to fruit and 48 atopic patients with fruit allergy. Eleven of these 48 patients were also allergic to NRL, 14 displayed sensitization to NRL without symptoms on NRL exposure so far, and 23 had neither symptoms nor IgE antibodies to NRL.
  
  
  RESULTS
  After expression in Escherichia coli, a soluble maltose-binding protein-rHev b 12 fusion protein was isolated and coupled to ImmunoCAP to determine rHev b 12 specific IgE reactivity. rHev b 12 specific IgE binding was found in 3 fruit-allergic patients with NRL sensitization (0.68, 0.88, and 0.96 kU/L) and in 3 fruit-allergic patients without NRL sensitization (1.58, 2.25, and 2.27 kU/L). The remaining 52 serum samples and all maltose-binding protein control test results were negative (< 0.35 kU/L).
  
  
  CONCLUSIONS
  In these patients, rHev b 12 specific IgE reactivity seems to result from common cross-reactive epitopes with some of the fruit LTPs tested and underscores only an involvement in co-recognition. No clinical relevance of IgE binding to the LTP of H brasiliensis in association with NRL allergy was detected.
authors.affiliation: Abteilung Molekulare Genetik, Berufsgenossenschaftliches Forschungsin-Institut für Arbeitsmedizin (BGFA), Institut der Ruhr-Universität Bochum, Bochum, Germany. rihs@bgfa.de
authors.forename: Hans-Peter
authors.initials: HP
authors.lastname: Rihs
authors.forename: Franziska
authors.initials: F
authors.lastname: Ruëff
authors.forename: Maria
authors.initials: M
authors.lastname: Lundberg
authors.forename: Peter
authors.initials: P
authors.lastname: Rozynek
authors.forename: Domingo
authors.initials: D
authors.lastname: Barber
authors.forename: Stephan
authors.initials: S
authors.lastname: Scheurer
authors.forename: Anna
authors.initials: A
authors.lastname: Cisteró-Bahima
authors.forename: Thomas
authors.initials: T
authors.lastname: Brüning
authors.forename: Monika
authors.initials: M
authors.lastname: Raulf-Heimsoth
mesh_terms: D000293:Adolescent; D000328:Adult; D000368:Aged; D000485:Allergens / Q000096:biosynthesis / Q000276:immunology*; D000937:Antigen-Antibody Reactions / Q000276:immunology; D052179:Antigens, Plant / Q000096:biosynthesis / Q000276:immunology*; D001667:Binding, Competitive / Q000276:immunology; D002352:Carrier Proteins / Q000096:biosynthesis / Q000276:immunology*; D002648:Child; D003429:Cross Reactions / Q000276:immunology; D005260:Female; D005512:Food Hypersensitivity / Q000276:immunology*; D005638:Fruit / Q000276:immunology*; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology*; D020315:Latex Hypersensitivity / Q000276:immunology; D008297:Male; D008875:Middle Aged; D010940:Plant Proteins / Q000096:biosynthesis / Q000276:immunology*; D011993:Recombinant Fusion Proteins / Q000276:immunology
chemical_list: D000485:Allergens; D052179:Antigens, Plant; D002352:Carrier Proteins; C502833:Hev b 12 protein, Hevea brasiliensis; D010940:Plant Proteins; C514372:Pru av 3 allergen, Prunus avium; D011993:Recombinant Fusion Proteins; C511920:lipid transfer proteins, plant; D007073:Immunoglobulin E