Secondary Structure and Tertiary Fold of the Birch Pollen Allergen Bet v 1 in Solution

Faber, Cornelius; Lindemann, Almut; Sticht, Heinrich; Ejchart, Andrzej; Kungl, Andreas J.; Susani, Markus; Frank, Rainer; Breitenbach, Michael; Rösch, Paul

doi:10.1074/jbc.271.32.19243

Cited by 28 publications

(16 citation statements)

References 36 publications

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“…The CD spectra of the two fragments show features characteristic of a random coil structure which remains unchanged even after prolonged coincubation of equimolar mixtures of the fragments. This result agrees with what is expected on the basis of the secondary structure as determined by nuclear magnetic resonance (38). The fold of Bet v 1 is mainly stabilized by two antiparallel ␤ sheets and three helices.…”

Section: Discussionsupporting

confidence: 82%

Conversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapy.

Vrtala¹,

Hirtenlehner²,

Vangelista³

et al. 1997

J. Clin. Invest.

199

230

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Section: Discussionsupporting

confidence: 82%

Conversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapy.

Vrtala¹,

Hirtenlehner²,

Vangelista³

et al. 1997

J. Clin. Invest.

199

230

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show abstract

“…2B). Further NMR analysis confirmed earlier predictions of IgEbinding epitopes of BetV I and revealed a protein structure composed of six antiparallel b-strands and three a-helices (Faber et al, 1996;Markovic-Housley et al, 2003;Spangfort et al, 2003), which defines a hydrophobic cavity involved in the binding of lipid molecules (Radauer et al, 2008).…”

Section: Discussionsupporting

confidence: 61%

The Nuclear Interactor PYL8/RCAR3 ofFagus sylvaticaFsPP2C1 Is a Positive Regulator of Abscisic Acid Signaling in Seeds and Stress

et al. 2009

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The functional protein phosphatase type 2C from beechnut (Fagus sylvatica; FsPP2C1) was a negative regulator of abscisic acid (ABA) signaling in seeds. In this report, to get deeper insight on FsPP2C1 function, we aim to identify PP2C-interacting partners. Two closely related members (PYL8/RCAR3 and PYL7/RCAR2) of the Arabidopsis (Arabidopsis thaliana) BetV I family were shown to bind FsPP2C1 in a yeast two-hybrid screening and in an ABA-independent manner. By transient expression of FsPP2C1 and PYL8/RCAR3 in epidermal onion (Allium cepa) cells and agroinfiltration in tobacco (Nicotiana benthamiana) as green fluorescent protein fusion proteins, we obtained evidence supporting the subcellular localization of both proteins mainly in the nucleus and in both the cytosol and the nucleus, respectively. The in planta interaction of both proteins in tobacco cells by bimolecular fluorescence complementation assays resulted in a specific nuclear colocalization of this interaction. Constitutive overexpression of PYL8/RCAR3 confers ABA hypersensitivity in Arabidopsis seeds and, consequently, an enhanced degree of seed dormancy. Additionally, transgenic 35S:PYL8/RCAR3 plants are unable to germinate under low concentrations of mannitol, NaCl, or paclobutrazol, which are not inhibiting conditions to the wild type. In vegetative tissues, Arabidopsis PYL8/RCAR3 transgenic plants show ABA-resistant drought response and a strong inhibition of early root growth. These phenotypes are strengthened at the molecular level with the enhanced induction of several ABA response genes. Both seed and vegetative phenotypes of Arabidopsis 35S:PYL8/RCAR3 plants are opposite those of 35S: FsPP2C1 plants. Finally, double transgenic plants confirm the role of PYL8/RCAR3 by antagonizing FsPP2C1 function and demonstrating that PYL8/RCAR3 positively regulates ABA signaling during germination and abiotic stress responses.

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“…Results are expressed as the mean residue ellipticity (y-axis) at a given wavelength (x-axis). previously described to be a monomer (54). Interestingly, the dimer of Bet v 1, like the monomer, has been shown to possess RNase activity (55).…”

Section: Discussionmentioning

confidence: 99%

Dimerization of the Major Birch Pollen Allergen Bet v 1 Is Important for its In Vivo IgE-Cross-Linking Potential in Mice

Schöll¹,

Kalkura

Shedziankova

et al. 2005

The Journal of Immunology

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In type I allergy, the cross-linking of membrane IgE on B lymphocytes and of cytophilic IgE on effector cells by their respective allergens are key events. For cross-linking two IgE molecules, allergens need at least two epitopes. On large molecules, these could be different epitopes in a multivalent, or identical epitopes in a symmetrical, fashion. However, the availability of epitopes may be limited on small allergens such as Bet v 1, the major birch pollen allergen. The present work analyzes whether dimerization is required for the cross-linking capacity of this allergen. In immunoblots, murine monoclonal and polyclonal human Bet v 1-specific Abs detected, besides a Bet v 1 monomer of 17 kDa, a dimer of 34 kDa. In dynamic light scattering, Bet v 1 appeared as dimers and even multimers, but a single condition could be defined where it behaved exclusively monomerically. Small-angle x-ray scattering of the monomeric and dimeric samples resulted in diagrams agreeing with the calculated models. Circular dichroism measurements indicated that the structure of Bet v 1 was preserved under monomeric conditions. Skin tests in Bet v 1-allergic mice were positive with Bet v 1 dimer, but remained negative using the monomer. Furthermore, in contrast to dimeric Bet v 1, the monomer was less capable of activating murine memory B cells for IgE production in vivo. Our data indicate that the presentation of two identical epitopes by dimerized allergens is a precondition for cross-linking of IgE on mast cells and B lymphocytes.

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Secondary Structure and Tertiary Fold of the Birch Pollen Allergen Bet v 1 in Solution

Cited by 28 publications

References 36 publications

Conversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapy.

Conversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapy.

The Nuclear Interactor PYL8/RCAR3 ofFagus sylvaticaFsPP2C1 Is a Positive Regulator of Abscisic Acid Signaling in Seeds and Stress

Dimerization of the Major Birch Pollen Allergen Bet v 1 Is Important for its In Vivo IgE-Cross-Linking Potential in Mice

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