AllFam - Database of allergen families Department of Pathophysiology and Allergy Research Medical University of Vienna

AF069: Bet v 1-related protein

Pfam domains
PF00407: Pathogenesis-related protein Bet v I family

Biochemical properties

Bet v 1-related protein are widely distributed among vascular plants. The family was classyfied by sequence similarity into three subfamilies [1]. The largest of them contains the pathogenesis-related protein family PR-10 [2]. The expression of these proteins is either induced by pathogen attack or abiotic stress or developmentally regulated. PR-10 proteins are expressed in high concentrations in reproductive tissues such as pollen, seeds and fruits. The biological function of these proteins is still unclear. X-ray crystallography and ligand-binding studies suggest a role as steroid hormone carriers [3]. Other studies point to a ribonuclease activity [4]. The other two subfamilies are a group of major latex proteins and ripening-related proteins first described in the latex of opium poppy [5] and a small family of proteins containing members with S-norcoclaurin synthase activity, enzymes involved in alkaloid biosynthesis [6].

Allergological significance

The major birch pollen allergen, Bet v 1, is a member of the PR-10 family. Closely-related, cross-reactive allergens were found in the pollen of other trees from the order Fagales such as hazel, alder, and chestnut. Many birch pollen-allergic patients show allergic reactions to various fruits and vegetables, which are caused by IgE cross-reactivity between Bet v 1 and homologous allergens from plant foods [7]. Most Bet v 1-related food allergens were found in members of certain plant families: Rosaceae (apple, pear, stone fruits), Apiaceae (celery, carrot), and Fabaceae (soybean, peanut).

References

  1. Liscombe DK, MacLeod BP, Loukanina N, Nandi OI, Facchini PJ.
    Evidence for the monophyletic evolution of benzylisoquinoline alkaloid biosynthesis in angiosperms.
    Phytochemistry 2005, 66, 2501-20. [PubMed]
  2. Wen J, Vanek-Krebitz M, Hoffmann-Sommergruber K, Scheiner O, Breiteneder H.
    The potential of Betv1 homologues, a nuclear multigene family, as phylogenetic markers in flowering plants.
    Mol Phylogenet Evol 1997, 8, 317-33. [PubMed]
  3. Markovic-Housley Z, Degano M, Lamba D, von Roepenack-Lahaye E, Clemens S, Susani M, Ferreira F, Scheiner O, Breiteneder H.
    Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier.
    J Mol Biol 2003, 325, 123-33. [PubMed]
  4. Park CJ, Kim KJ, Shin R, Park JM, Shin YC, Paek KH.
    Pathogenesis-related protein 10 isolated from hot pepper functions as a ribonuclease in an antiviral pathway.
    Plant J 2004, 37, 186-98. [PubMed]
  5. Osmark P, Boyle B, Brisson N.
    Sequential and structural homology between intracellular pathogenesis-related proteins and a group of latex proteins.
    Plant Mol Biol 1998, 38, 1243-6. [PubMed]
  6. Samanani N, Liscombe DK, Facchini PJ.
    Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis.
    Plant J 2004, 40, 302-13. [PubMed]
  7. Vieths S, Scheurer S, Ballmer-Weber B.
    Current understanding of cross-reactivity of food allergens and pollen.
    Ann N Y Acad Sci 2002, 964, 47-68. [PubMed]

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