title: Characterization of high-molecular-mass allergens in oilseed rape pollen.
abstract: BACKGROUND
  Oilseed rape pollen allergies have been previously described as the result of cross-sensitization with various pollens. Recently, several proteins have been identified as oilseed rape allergens. The aim of the present work was the characterization of oilseed rape pollen allergens by two-dimensional (2-D) gel analysis and amino acid microsequencing.
  
  
  METHODS
  Water extractable proteins from oilseed rape pollen were separated by isoelectrofocusing and then transferred onto a nitrocellulose sheet. Twenty-one human sera from pollen- or mustard-allergic individuals were screened for their reactivity to oilseed rape proteins. Eleven sera possessed IgE which recognized oilseed rape pollen proteins and one serum was selected for further 2-D characterization and amino acid microsequencing of the allergens.
  
  
  RESULTS
  The results showed that three molecules from oilseed rape pollen were identified as oilseed rape allergens which have not yet been described. These three proteins were molecules of 70 kD with a pI >8, 40 kD with a pI around 10 and 80 kD with a pI around 5. These proteins displayed identities with the berberine bridge protein, a receptor-like protein kinase and the cobalamin-independent methionine synthetase from Arabidopsis thaliana, respectively. The genes encoding the putative Arabidopsis molecules are located on chromosome 1 (berberine bridge protein) and chromosomes 3 and 4 (receptor-like protein kinases).
  
  
  CONCLUSIONS
  These results show that certain high-molecular-mass proteins from oilseed rape pollen are allergens.
authors: Institut Pasteur, Unité d'Immuno-Allergie, Paris, France. hchardin@pasteur.fr
authors: H
authors: H
authors: Chardin
authors: C
authors: C
authors: Mayer
authors: H
authors: H
authors: Sénéchal
authors: M
authors: M
authors: Tepfer
authors: F X
authors: FX
authors: Desvaux
authors: G
authors: G
authors: Peltre
mesh_terms: D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D000485:Allergens / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics; D015153:Blotting, Western; D001937:Brassica / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D011058:Pollen / Q000737:chemistry* / Q000276:immunology; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D011852:Radioallergosorbent Test; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D000485:Allergens; D010940:Plant Proteins; D007073:Immunoglobulin E; D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase; D011494:Protein Kinases