The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
The Major Birch Allergen, Bet v 1, Shows Affinity for a Broad Spectrum of Physiological Ligands
Open accessAbstract
Bet v 1 is a 17-kDa protein abundantly present in the pollen of the White birch tree and is the primary cause of birch pollen allergy in humans. Its three-dimensional structure is remarkable in that a solvent-accessible cavity traverses the core of the molecule. The biological function of Bet v 1 is unknown, although it is homologous to a family of pathogenesis-related proteins in plants. In this study we first show that Bet v 1 in the native state is able to bind the fluorescent probe 8-anilino-1-naphthalenesulfonic acid (ANS). ANS binds to Bet v 1 with 1:1 stoichiometry, and NMR data indicate that binding takes place in the cavity. Using an ANS displacement assay, we then identify a range of physiologically relevant ligands, including fatty acids, flavonoids, and cytokinins, which generally bind with low micromolar affinity. The ability of these ligands to displace ANS suggests that they also bind in the cavity, although the exact binding sites seem to vary among different ligands. The cytokinins, for example, seem to bind at a separate site close to ANS, because they increase the fluorescence of the ANS. Bet v 1 complex. Also, the fluorescent sterol dehydroergosterol binds to Bet v 1 as demonstrated by direct titrations. This study provides the first qualitative and quantitative data on the ligand binding properties of this important pollen allergen. Our findings indicate that ligand binding is important for the biological function of Bet v 1.
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A classification of plant food allergens
Breiteneder, H., & Radauer, C. (2004) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2004.01.779 · Cited by 553
EAACI Molecular Allergology User's Guide 2.0
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Allergic cross‐reactivity: from gene to the clinic
Ferreira, F., Hawranek, T., Gruber, P., Wopfner, N., & Mari, A. (2004) · Allergy · doi:10.1046/j.1398-9995.2003.00407.x · Cited by 194
Pollen Food Allergy Syndrome (PFAS): A Review of Current Available Literature
Carlson, G., & Coop, C. (2019) · Annals of Allergy, Asthma & Immunology · doi:10.1016/j.anai.2019.07.022 · Cited by 171
Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family
Aglas, L., Soh, W. T., Kraiem, A., Wenger, M., Brandstetter, H., & Ferreira, F. (2020) · Current Allergy and Asthma Reports · doi:10.1007/s11882-020-00918-4 · Cited by 56
Metadata
- Authors
- Mogensen, J. E., Wimmer, R., Larsen, J. N., Spangfort, M. D., & Otzen, D. E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-06
- Volume
- 277
- Issue
- 26
- Pages
- 23684-23692
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2028846971
- Cited by
- 254
- References
- 54
- FWCI
- 4.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Mogensen, J. E., Wimmer, R., Larsen, J. N., Spangfort, M. D., & Otzen, D. E. (2002). The Major Birch Allergen, Bet v 1, Shows Affinity for a Broad Spectrum of Physiological Ligands. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m202065200
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