Carbohydrate moieties can induce mediator release: a detailed characterization of two major timothy grass pollen allergens.

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Carbohydrate moieties can induce mediator release: a detailed characterization of two major timothy grass pollen allergens. / Wicklein, Daniel; Lindner, Buko; Moll, Hermann; Kolarich, Daniel; Altmann, Friedrich; Becker, Wolf-Meinhard; Petersen, Arnd.

In: BIOL CHEM, Vol. 385, No. 5, 5, 2004, p. 397-407.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

Harvard

Wicklein, D, Lindner, B, Moll, H, Kolarich, D, Altmann, F, Becker, W-M & Petersen, A 2004, 'Carbohydrate moieties can induce mediator release: a detailed characterization of two major timothy grass pollen allergens.', BIOL CHEM, vol. 385, no. 5, 5, pp. 397-407. <http://www.ncbi.nlm.nih.gov/pubmed/15195999?dopt=Citation>

APA

Wicklein, D., Lindner, B., Moll, H., Kolarich, D., Altmann, F., Becker, W-M., & Petersen, A. (2004). Carbohydrate moieties can induce mediator release: a detailed characterization of two major timothy grass pollen allergens. BIOL CHEM, 385(5), 397-407. [5]. http://www.ncbi.nlm.nih.gov/pubmed/15195999?dopt=Citation

Vancouver

Wicklein D, Lindner B, Moll H, Kolarich D, Altmann F, Becker W-M et al. Carbohydrate moieties can induce mediator release: a detailed characterization of two major timothy grass pollen allergens. BIOL CHEM. 2004;385(5):397-407. 5.

Bibtex

@article{1fff20048e854f4c87487578cb18be00,
title = "Carbohydrate moieties can induce mediator release: a detailed characterization of two major timothy grass pollen allergens.",
abstract = "Specific IgE binding to carbohydrate moieties of glycosylated allergens has been known for years, but the importance of these structures for the elicitation of allergic reactions is still a matter of debate. Because of their conserved carbohydrate structures, especially N-glycans have always been prime candidates for IgE cross-reactivity between allergens from unrelated species. The aim of our study was to determine whether carbohydrate structures on glycoproteins can by themselves elucidate allergic reactions. We characterized in detail the carbohydrate moieties of the major allergens Phl p 1 and Phl p 13 of timothy grass pollen (Phleum pratense L.) by performing tryptic digests followed by HPLC, N-terminal sequencing, sugar analysis, MALDI-TOF- and ESI-ICRFT-MS. Phl p 1 contains one N-glycan with one of the two glycoforms MMXF3 and M0XF3 and a single furanosidic arabinose, which is bound to a hydroxyproline residue in direct vicinity to the N-glycan. This O-glycosylation is probably due to an arabinosylation consensus sequence found in the N-terminal part of Phl p 1 and other group 1 allergens, but displayed no IgE-reactivity. Thus, Phl p 1 is monovalent with respect to its IgE-binding carbohydrate epitopes and showed no mediator release. In contrast, the carbohydrate moiety of Phl p 13, which carries four of the same N-glycans (like Phl p 1), can cross-link IgE-receptors via carbohydrate chains and elicits IL-4 release from basophils.",
keywords = "Humans, Amino Acid Sequence, Molecular Sequence Data, Fucose/chemistry/metabolism, Immunoglobulin E/*immunology, Allergens/*chemistry/immunology, Basophils/drug effects/immunology, Bromelains/pharmacology, Hypersensitivity/immunology, Interleukin-4/metabolism, Plant Proteins/*chemistry/immunology, Polysaccharides/chemistry/*immunology/metabolism, Humans, Amino Acid Sequence, Molecular Sequence Data, Fucose/chemistry/metabolism, Immunoglobulin E/*immunology, Allergens/*chemistry/immunology, Basophils/drug effects/immunology, Bromelains/pharmacology, Hypersensitivity/immunology, Interleukin-4/metabolism, Plant Proteins/*chemistry/immunology, Polysaccharides/chemistry/*immunology/metabolism",
author = "Daniel Wicklein and Buko Lindner and Hermann Moll and Daniel Kolarich and Friedrich Altmann and Wolf-Meinhard Becker and Arnd Petersen",
year = "2004",
language = "English",
volume = "385",
pages = "397--407",
journal = "BIOL CHEM",
issn = "1431-6730",
publisher = "Walter de Gruyter GmbH & Co. KG",
number = "5",

}

RIS

TY - JOUR

T1 - Carbohydrate moieties can induce mediator release: a detailed characterization of two major timothy grass pollen allergens.

AU - Wicklein, Daniel

AU - Lindner, Buko

AU - Moll, Hermann

AU - Kolarich, Daniel

AU - Altmann, Friedrich

AU - Becker, Wolf-Meinhard

AU - Petersen, Arnd

PY - 2004

Y1 - 2004

N2 - Specific IgE binding to carbohydrate moieties of glycosylated allergens has been known for years, but the importance of these structures for the elicitation of allergic reactions is still a matter of debate. Because of their conserved carbohydrate structures, especially N-glycans have always been prime candidates for IgE cross-reactivity between allergens from unrelated species. The aim of our study was to determine whether carbohydrate structures on glycoproteins can by themselves elucidate allergic reactions. We characterized in detail the carbohydrate moieties of the major allergens Phl p 1 and Phl p 13 of timothy grass pollen (Phleum pratense L.) by performing tryptic digests followed by HPLC, N-terminal sequencing, sugar analysis, MALDI-TOF- and ESI-ICRFT-MS. Phl p 1 contains one N-glycan with one of the two glycoforms MMXF3 and M0XF3 and a single furanosidic arabinose, which is bound to a hydroxyproline residue in direct vicinity to the N-glycan. This O-glycosylation is probably due to an arabinosylation consensus sequence found in the N-terminal part of Phl p 1 and other group 1 allergens, but displayed no IgE-reactivity. Thus, Phl p 1 is monovalent with respect to its IgE-binding carbohydrate epitopes and showed no mediator release. In contrast, the carbohydrate moiety of Phl p 13, which carries four of the same N-glycans (like Phl p 1), can cross-link IgE-receptors via carbohydrate chains and elicits IL-4 release from basophils.

AB - Specific IgE binding to carbohydrate moieties of glycosylated allergens has been known for years, but the importance of these structures for the elicitation of allergic reactions is still a matter of debate. Because of their conserved carbohydrate structures, especially N-glycans have always been prime candidates for IgE cross-reactivity between allergens from unrelated species. The aim of our study was to determine whether carbohydrate structures on glycoproteins can by themselves elucidate allergic reactions. We characterized in detail the carbohydrate moieties of the major allergens Phl p 1 and Phl p 13 of timothy grass pollen (Phleum pratense L.) by performing tryptic digests followed by HPLC, N-terminal sequencing, sugar analysis, MALDI-TOF- and ESI-ICRFT-MS. Phl p 1 contains one N-glycan with one of the two glycoforms MMXF3 and M0XF3 and a single furanosidic arabinose, which is bound to a hydroxyproline residue in direct vicinity to the N-glycan. This O-glycosylation is probably due to an arabinosylation consensus sequence found in the N-terminal part of Phl p 1 and other group 1 allergens, but displayed no IgE-reactivity. Thus, Phl p 1 is monovalent with respect to its IgE-binding carbohydrate epitopes and showed no mediator release. In contrast, the carbohydrate moiety of Phl p 13, which carries four of the same N-glycans (like Phl p 1), can cross-link IgE-receptors via carbohydrate chains and elicits IL-4 release from basophils.

KW - Humans

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Fucose/chemistry/metabolism

KW - Immunoglobulin E/immunology

KW - Allergens/chemistry/immunology

KW - Basophils/drug effects/immunology

KW - Bromelains/pharmacology

KW - Hypersensitivity/immunology

KW - Interleukin-4/metabolism

KW - Plant Proteins/chemistry/immunology

KW - Polysaccharides/chemistry/immunology/metabolism

KW - Humans

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Fucose/chemistry/metabolism

KW - Immunoglobulin E/immunology

KW - Allergens/chemistry/immunology

KW - Basophils/drug effects/immunology

KW - Bromelains/pharmacology

KW - Hypersensitivity/immunology

KW - Interleukin-4/metabolism

KW - Plant Proteins/chemistry/immunology

KW - Polysaccharides/chemistry/immunology/metabolism

M3 - SCORING: Journal article

VL - 385

SP - 397

EP - 407

JO - BIOL CHEM

JF - BIOL CHEM

SN - 1431-6730

IS - 5

M1 - 5

ER -