Pollen allergen Bet V 1

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Pollen allergen Bet v 1-A ( silver birch , Betula verrucosa )
Pollen allergen Bet v 1-A (silver birch, Betula verrucosa)
Band model of the monomer from two sides, according to PDB  1QMR

Existing structural data : 1BV1 , 1FSK , 1LLT , 1QMR

Mass / length primary structure 159 amino acids
Secondary to quaternary structure Homodimer
Identifier
Gene name (s) BETVIA; PR-10
External IDs
Occurrence
Parent taxon Vascular plants

Bet v 1 is the main allergen of the silver birch ( Betula pendula , Syn .: B. verrucosa ) and the cause of birch pollen allergy in humans. Bet v 1 belongs to the PR-10 protein family , the representatives of which are formed by many vascular plants in various tissue types in response to biotic and abiotic stress . The exact function of Bet v 1 for the plant is currently unknown. The results of the crystal structure analysis and binding studies suggest, however, that it could be a carrier for steroid hormones that plays a role in the defense against pathogens and in the development and growth of the plant. Several isoforms with different levels of allergenicity are known of Bet v 1 . The isoform composition of the Bet v 1 proteins found in pollen varies from tree to tree, which is why the strength of the allergenicity of the pollen is individual for each individual birch tree.

A subfamily of the PR-10 proteins combines all proteins homologous to Bet v 1 of the BetVI family; Members of this family are also widely dispersed in the plant kingdom and many are strong allergens. Since all members have the same epitope due to their homology , the reason for cross allergies is to be found here. Other members of the BetVI family include:

An indication of the exact function is a binding domain of the proteins, which can preferentially bind lipids such as cholesterol and lecithin . In cell culture, penetration of the protein into epithelial cells was observed only in allergy sufferers , possibly via lipid rafts in the cell membrane , while the immune system of healthy people prevents this process.

Individual evidence

  1. ↑ a b IPR000916 Bet v I allergen. In: InterPro 28.0. EBI, accessed October 6, 2010 .
  2. ↑ K. Hoffmann-Sommergruber: Plant Allergens and Pathogenesis-Related Proteins. What Do They Have in Common? In: International Archives of Allergy & Immunology. 2000, 122, pp. 155-166
  3. ↑ Z. Marković-Housley et al .: 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. In: Journal of Molecular Biology. 2003, 325 (1), pp. 123-33
  4. ↑ K. Hoffmann-Sommergruber, M. Vanek-Krebitz, C. Radauer, J. Wen, F. Ferreira, O. Scheiner, H. Breiteneder: Genomic characterization of members of the Bet v 1 family: genes coding for allergens and pathogenesis -related proteins share intron positions . In: Gene 1997, 197, pp. 91-100
  5. ↑ Schenk MF, Cordewener JH, America AH, Van't Westende WP, Smulders MJ, Gilissen LJ: Characterization of PR-10 genes from eight Betula species and detection of Bet v 1 isoforms in birch pollen . In: BMC Plant Biol . 9, 2009, p. 24. doi : 10.1186 / 1471-2229-9-24 . PMID 19257882 . PMC 2671506 (free full text).
  6. ↑ UniProt P15494
  7. ↑ Mattila K, Renkonen R: Modeling of Bet v 1 binding to lipids . In: Scand. J. Immunol. . 70, No. 2, August 2009, pp. 116-24. doi : 10.1111 / j.1365-3083.2009.02277.x . PMID 19630917 .
  8. ↑ Renkonen J, Mattila P, Lehti S, et al. : Birch pollen allergen Bet v 1 binds to and is transported through conjunctival epithelium in allergic patients . In: Allergy . 64, No. 6, June 2009, pp. 868-75. doi : 10.1111 / j.1398-9995.2008.01919.x . PMID 19154545 .
  9. ↑ Mattila P, Renkonen J, Toppila-Salmi S, et al. : Time-series nasal epithelial transcriptomics during natural pollen exposure in healthy subjects and allergic patients . In: Allergy . 65, No. 2, February 2010, pp. 175-83. doi : 10.1111 / j.1398-9995.2009.02181.x . PMID 19804444 .