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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
- 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] - 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] - 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] - 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] - 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] - 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] - 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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