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Daniel Otzen

The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands

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Standard

The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. / Mogensen, Jesper E.; Wimmer, Reinhard; Larsen, Jørgen N.; Spangfort, Michael D.; Otzen, Daniel E.

In: Journal of Biological Chemistry, Vol. 277, No. 26, 28.06.2002, p. 23684-23692.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Mogensen, JE, Wimmer, R, Larsen, JN, Spangfort, MD & Otzen, DE 2002, 'The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands', Journal of Biological Chemistry, vol. 277, no. 26, pp. 23684-23692. https://doi.org/10.1074/jbc.M202065200

APA

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, 277(26), 23684-23692. https://doi.org/10.1074/jbc.M202065200

CBE

Mogensen JE, Wimmer R, Larsen JN, Spangfort MD, Otzen DE. 2002. The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. Journal of Biological Chemistry. 277(26):23684-23692. https://doi.org/10.1074/jbc.M202065200

MLA

Mogensen, Jesper E. et al. "The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands". Journal of Biological Chemistry. 2002, 277(26). 23684-23692. https://doi.org/10.1074/jbc.M202065200

Vancouver

Mogensen JE, Wimmer R, Larsen JN, Spangfort MD, Otzen DE. The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. Journal of Biological Chemistry. 2002 Jun 28;277(26):23684-23692. https://doi.org/10.1074/jbc.M202065200

Author

Mogensen, Jesper E. ; Wimmer, Reinhard ; Larsen, Jørgen N. ; Spangfort, Michael D. ; Otzen, Daniel E. / The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. In: Journal of Biological Chemistry. 2002 ; Vol. 277, No. 26. pp. 23684-23692.

Bibtex

@article{f498b6baf1714611addf65caa9924471,
title = "The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands",
abstract = "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.",
author = "Mogensen, {Jesper E.} and Reinhard Wimmer and Larsen, {J{\o}rgen N.} and Spangfort, {Michael D.} and Otzen, {Daniel E.}",
year = "2002",
month = jun,
day = "28",
doi = "10.1074/jbc.M202065200",
language = "English",
volume = "277",
pages = "23684--23692",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "26",

}

RIS

TY - JOUR

T1 - The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands

AU - Mogensen, Jesper E.

AU - Wimmer, Reinhard

AU - Larsen, Jørgen N.

AU - Spangfort, Michael D.

AU - Otzen, Daniel E.

PY - 2002/6/28

Y1 - 2002/6/28

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0037189581&partnerID=8YFLogxK

U2 - 10.1074/jbc.M202065200

DO - 10.1074/jbc.M202065200

M3 - Journal article

C2 - 11953433

AN - SCOPUS:0037189581

VL - 277

SP - 23684

EP - 23692

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 26

ER -