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Protease recognition sites in Bet v 1a are cryptic, explaining its slow processing relevant to its allergenicity

Freier, Regina ; Dall, Elfriede ; Brandstetter, Hans

Springer Science and Business Media LLC ; 2015

In: Scientific Reports Vol. 5, No. 1 ( 2015-08-03)

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In: Scientific Reports, Springer Science and Business Media LLC, Vol. 5, No. 1 ( 2015-08-03)

Abstract: Despite a high similarity with homologous protein families, only few proteins trigger an allergic immune response with characteristic T H 2 polarization. This puzzling observation is illustrated by the major birch pollen allergen Bet v 1a and its hypoallergenic protein isoforms, e.g., Bet v 1d. Given the key role of proteolytic processing in antigen presentation and T cell polarization, we investigated the recognition of Bet v 1 isoforms by the relevant protease cathepsin S. We found that at moderately acidic pH values Bet v 1a bound to cathepsin S with significantly lower affinity and was more slowly cleaved than its hypoallergenic isoform Bet v 1d. Only at pH values ≤4.5 the known proteolytic cleavage sites in Bet v 1a became accessible, resulting in a strong increase in affinity towards cathepsin S. Antigen processing and class II MHC loading occurs at moderately acidic compartments where processing of Bet v 1a and Bet v 1d differs distinctly. This difference translates into low and high density class II MHC loading and subsequently in T H 2 and T H 1 polarization, respectively.

Type of Medium: Online Resource

ISSN: 2045-2322

URL: Article

DOI: 10.1038/srep12707

Language: English

Publisher: Springer Science and Business Media LLC

Publication Date: 2015

detail.hit.zdb_id: 2615211-3

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Structures of the germline-specific Deadhead and thioredoxin T proteins from Drosophila melanogaster reveal unique features among thioredoxins

Freier, Regina ; Aragón, Eric ; Bagiński, Błażej ; [et al.]

International Union of Crystallography (IUCr) ; 2021

In: IUCrJ Vol. 8, No. 2 ( 2021-03-01), p. 281-294

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In: IUCrJ, International Union of Crystallography (IUCr), Vol. 8, No. 2 ( 2021-03-01), p. 281-294

Abstract: Thioredoxins (Trxs) are ubiquitous enzymes that regulate the redox state in cells. In Drosophila , there are two germline-specific Trxs, Deadhead (Dhd) and thioredoxin T (TrxT), that belong to the lethal(3)malignant brain tumor signature genes and to the `survival network' of genes that mediate the cellular response to DNA damage. Dhd is a maternal protein required for early embryogenesis that promotes protamine–histone exchange in fertilized eggs and midblastula transition. TrxT is testis-specific and associates with the lampbrush loops of the Y chromosome. Here, the first structures of Dhd and TrxT are presented, unveiling new features of these two thioredoxins. Dhd has positively charged patches on its surface, in contrast to the negatively charged surfaces commonly found in most Trxs. This distinctive charge distribution helps to define initial encounter complexes with DNA/RNA that will lead to final specific interactions with cofactors to promote chromatin remodeling. TrxT contains a C-terminal extension, which is mostly unstructured and highly flexible, that wraps the conserved core through a closed conformation. It is believed that these new structures can guide future work aimed at understanding embryo development and redox homeostasis in Drosophila . Moreover, due to their restricted presence in Schizophora (a section of the true flies), these structures can help in the design of small-molecular binders to modulate native redox homeostasis, thereby providing new applications for the control of plagues that cause human diseases and/or bring about economic losses by damaging crop production.

Type of Medium: Online Resource

ISSN: 2052-2525

URL: Article

DOI: 10.1107/S2052252521000221

DOI: 10.1107/S2052252521000221/jt5053sup1.pdf

Language: Unknown

Publisher: International Union of Crystallography (IUCr)

Publication Date: 2021

detail.hit.zdb_id: 2754953-7

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Carbon dioxide dissociation curve and buffer capacity of dog heart muscle

Benson, E. S. ; Freier, Esther F. ; Vijums, Regina

American Physiological Society ; 1965

In: American Journal of Physiology-Legacy Content Vol. 209, No. 5 ( 1965-11-01), p. 941-944

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In: American Journal of Physiology-Legacy Content, American Physiological Society, Vol. 209, No. 5 ( 1965-11-01), p. 941-944

Abstract: The carbon dioxide dissociation curve of dog heart muscle was found to be higher than of dog skeletal muscle. The slope of this dissociation curve in the range of Pco 2 20–55 and the buffer capacity of dog heart muscle with respect to Pco 2 appear to be approximately equal to those of dog skeletal muscle. Seemingly, in the dog, heart muscle is at least as well buffered against the pH-lowering effect of increasing CO 2 tension as is skeletal muscle and is more effectively buffered than has previously been realized.

Type of Medium: Online Resource

ISSN: 0002-9513

URL: Article

DOI: 10.1152/ajplegacy.1965.209.5.941

RVK:

WA 15000

RVK:

XA 20060

Language: English

Publisher: American Physiological Society

Publication Date: 1965

detail.hit.zdb_id: 1477334-X

detail.hit.zdb_id: 2065807-2

detail.hit.zdb_id: 1477287-5

detail.hit.zdb_id: 1477308-9

detail.hit.zdb_id: 1477297-8

detail.hit.zdb_id: 1477331-4

detail.hit.zdb_id: 1477300-4

detail.hit.zdb_id: 1477329-6

SSG: 12

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6th International Symposium on Molecular Allergology (ISMA)

Hilger, Christiane ; Swiontek, Kyra ; Fischer, Jörg ; [et al.]

Wiley ; 2016

In: Clinical and Translational Allergy Vol. 6, No. S2 ( 2016-10)

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In: Clinical and Translational Allergy, Wiley, Vol. 6, No. S2 ( 2016-10)

Type of Medium: Online Resource

ISSN: 2045-7022

URL: Article

DOI: 10.1186/s13601-016-0123-x

Language: English

Publisher: Wiley

Publication Date: 2016

detail.hit.zdb_id: 2630865-4

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Crystal structure of the human odorant binding protein, OBP IIa : X-Ray Structure of OBP IIa

Schiefner, André ; Freier, Regina ; Eichinger, Andreas ; [et al.]

Wiley ; 2015

In: Proteins: Structure, Function, and Bioinformatics Vol. 83, No. 6 ( 2015-06), p. 1180-1184

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In: Proteins: Structure, Function, and Bioinformatics, Wiley, Vol. 83, No. 6 ( 2015-06), p. 1180-1184

Type of Medium: Online Resource

ISSN: 0887-3585

URL: Issue

URL: Article

DOI: 10.1002/prot.v83.6

DOI: 10.1002/prot.24797

RVK:

WA 15000

Language: English

Publisher: Wiley

Publication Date: 2015

detail.hit.zdb_id: 1475032-6

SSG: 12

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Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen

Machado, Yoan ; Freier, Regina ; Scheiblhofer, Sandra ; [et al.]

Elsevier BV ; 2016

In: Journal of Allergy and Clinical Immunology Vol. 137, No. 5 ( 2016-05), p. 1525-1534

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In: Journal of Allergy and Clinical Immunology, Elsevier BV, Vol. 137, No. 5 ( 2016-05), p. 1525-1534

Type of Medium: Online Resource

ISSN: 0091-6749

URL: Article

DOI: 10.1016/j.jaci.2015.09.026

RVK:

XA 52000

Language: English

Publisher: Elsevier BV

Publication Date: 2016

detail.hit.zdb_id: 2006613-2

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Structural basis for genome wide recognition of 5-bp GC motifs by SMAD transcription factors

Martin-Malpartida, Pau ; Batet, Marta ; Kaczmarska, Zuzanna ; [et al.]

Springer Science and Business Media LLC ; 2017

In: Nature Communications Vol. 8, No. 1 ( 2017-12-12)

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In: Nature Communications, Springer Science and Business Media LLC, Vol. 8, No. 1 ( 2017-12-12)

Abstract: Smad transcription factors activated by TGF-β or by BMP receptors form trimeric complexes with Smad4 to target specific genes for cell fate regulation. The CAGAC motif has been considered as the main binding element for Smad2/3/4, whereas Smad1/5/8 have been thought to preferentially bind GC-rich elements. However, chromatin immunoprecipitation analysis in embryonic stem cells showed extensive binding of Smad2/3/4 to GC-rich cis -regulatory elements. Here, we present the structural basis for specific binding of Smad3 and Smad4 to GC-rich motifs in the goosecoid promoter, a nodal-regulated differentiation gene. The structures revealed a 5-bp consensus sequence GGC(GC)|(CG) as the binding site for both TGF-β and BMP-activated Smads and for Smad4. These 5GC motifs are highly represented as clusters in Smad-bound regions genome-wide. Our results provide a basis for understanding the functional adaptability of Smads in different cellular contexts, and their dependence on lineage-determining transcription factors to target specific genes in TGF-β and BMP pathways.

Type of Medium: Online Resource

ISSN: 2041-1723

URL: Article

DOI: 10.1038/s41467-017-02054-6

Language: English

Publisher: Springer Science and Business Media LLC

Publication Date: 2017

detail.hit.zdb_id: 2553671-0

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Crystal structure of Pla l 1 reveals both structural similarity and allergenic divergence within the Ole e 1–like protein family

Stemeseder, Teresa ; Freier, Regina ; Wildner, Sabrina ; [et al.]

Elsevier BV ; 2017

In: Journal of Allergy and Clinical Immunology Vol. 140, No. 1 ( 2017-07), p. 277-280

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In: Journal of Allergy and Clinical Immunology, Elsevier BV, Vol. 140, No. 1 ( 2017-07), p. 277-280

Type of Medium: Online Resource

ISSN: 0091-6749

URL: Article

DOI: 10.1016/j.jaci.2016.10.035

RVK:

XA 52000

Language: English

Publisher: Elsevier BV

Publication Date: 2017

detail.hit.zdb_id: 2006613-2

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Unveiling the dimer/monomer propensities of Smad MH1-DNA complexes

Ruiz, Lidia ; Kaczmarska, Zuzanna ; Gomes, Tiago ; [et al.]

Elsevier BV ; 2021

In: Computational and Structural Biotechnology Journal Vol. 19 ( 2021), p. 632-646

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In: Computational and Structural Biotechnology Journal, Elsevier BV, Vol. 19 ( 2021), p. 632-646

Type of Medium: Online Resource

ISSN: 2001-0370

URL: Article

DOI: 10.1016/j.csbj.2020.12.044

Language: English

Publisher: Elsevier BV

Publication Date: 2021

detail.hit.zdb_id: 2694435-2

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Ligand Binding Modulates the Structural Dynamics and Compactness of the Major Birch Pollen Allergen

Grutsch, Sarina ; Fuchs, Julian E. ; Freier, Regina ; [et al.]

Elsevier BV ; 2014

In: Biophysical Journal Vol. 107, No. 12 ( 2014-12), p. 2972-2981

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In: Biophysical Journal, Elsevier BV, Vol. 107, No. 12 ( 2014-12), p. 2972-2981

Type of Medium: Online Resource

ISSN: 0006-3495

URL: Article

DOI: 10.1016/j.bpj.2014.10.062

Language: English

Publisher: Elsevier BV

Publication Date: 2014

detail.hit.zdb_id: 1477214-0

SSG: 12

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