Glycoform analysis of Japanese cedar [Cryptomeria japonica] pollen allergen, Cry j 1

In our previous study (Y. Kimura et al., Biosci. Biotechnol. Biochem., 69, 137-144 (2005)), we found that plant complex type N-glycans harboring Lewis a epitope are linked to the mountain cedar pollen allergen Jun a 1. Jun a 1 is a glycoprotein highly homologous with Japanese cedar pollen glycoaller...

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Veröffentlicht in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2005, Vol.69 (9), p.1700-1705
Hauptverfasser: Maeda, M.(Okayama Univ. (Japan)), Kamamoto, M, Hino, K, Yamamoto, S, Kimura, M, Okano, M, Kimura, Y
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container_end_page 1705
container_issue 9
container_start_page 1700
container_title Bioscience, biotechnology, and biochemistry
container_volume 69
creator Maeda, M.(Okayama Univ. (Japan))
Kamamoto, M
Hino, K
Yamamoto, S
Kimura, M
Okano, M
Kimura, Y
description In our previous study (Y. Kimura et al., Biosci. Biotechnol. Biochem., 69, 137-144 (2005)), we found that plant complex type N-glycans harboring Lewis a epitope are linked to the mountain cedar pollen allergen Jun a 1. Jun a 1 is a glycoprotein highly homologous with Japanese cedar pollen glycoallergen, Cry j 1. Although it has been found that some plant complex type N-glycans are linked to Cry j 1, the occurrence of Lewis a epitope in the N-glycan moiety has not been proved yet. Hence, we reinvestigated the glycoform of the pollen allergen to find whether the Lewis a epitope(s) occur in the N-glycan moiety of Cry j 1. From the cedar pollen glycoallergen, the N-glycans were liberated by hydrazinolysis and the resulting sugar chains were N-acetylated and then coupled with 2-aminopyridine. Three pyridylaminated sugar chains were purified by reversed-phase HPLC and size-fractionation HPLC. The structures were analyzed by a combination of exoand endo-glycosidase digestions, sugar chain mapping, and electrospray ionization mass spectrometry (ESIMS). Structural analysis clearly indicated that Lewis a epitope (Gal beta l-3(Fuc alpha l4) GlcNAc beta 1-), instead of the Gal beta l-4(Fuc alpha l-6) GlcNAc, occurs in the N-glycans of Cry j 1.
doi_str_mv 10.1271/bbb.69.1700
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From the cedar pollen glycoallergen, the N-glycans were liberated by hydrazinolysis and the resulting sugar chains were N-acetylated and then coupled with 2-aminopyridine. Three pyridylaminated sugar chains were purified by reversed-phase HPLC and size-fractionation HPLC. The structures were analyzed by a combination of exoand endo-glycosidase digestions, sugar chain mapping, and electrospray ionization mass spectrometry (ESIMS). 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(Japan))</creatorcontrib><creatorcontrib>Kamamoto, M</creatorcontrib><creatorcontrib>Hino, K</creatorcontrib><creatorcontrib>Yamamoto, S</creatorcontrib><creatorcontrib>Kimura, M</creatorcontrib><creatorcontrib>Okano, M</creatorcontrib><creatorcontrib>Kimura, Y</creatorcontrib><title>Glycoform analysis of Japanese cedar [Cryptomeria japonica] pollen allergen, Cry j 1</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>In our previous study (Y. Kimura et al., Biosci. Biotechnol. Biochem., 69, 137-144 (2005)), we found that plant complex type N-glycans harboring Lewis a epitope are linked to the mountain cedar pollen allergen Jun a 1. Jun a 1 is a glycoprotein highly homologous with Japanese cedar pollen glycoallergen, Cry j 1. Although it has been found that some plant complex type N-glycans are linked to Cry j 1, the occurrence of Lewis a epitope in the N-glycan moiety has not been proved yet. 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(Japan))</au><au>Kamamoto, M</au><au>Hino, K</au><au>Yamamoto, S</au><au>Kimura, M</au><au>Okano, M</au><au>Kimura, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glycoform analysis of Japanese cedar [Cryptomeria japonica] pollen allergen, Cry j 1</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2005</date><risdate>2005</risdate><volume>69</volume><issue>9</issue><spage>1700</spage><epage>1705</epage><pages>1700-1705</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>In our previous study (Y. Kimura et al., Biosci. Biotechnol. Biochem., 69, 137-144 (2005)), we found that plant complex type N-glycans harboring Lewis a epitope are linked to the mountain cedar pollen allergen Jun a 1. Jun a 1 is a glycoprotein highly homologous with Japanese cedar pollen glycoallergen, Cry j 1. Although it has been found that some plant complex type N-glycans are linked to Cry j 1, the occurrence of Lewis a epitope in the N-glycan moiety has not been proved yet. Hence, we reinvestigated the glycoform of the pollen allergen to find whether the Lewis a epitope(s) occur in the N-glycan moiety of Cry j 1. From the cedar pollen glycoallergen, the N-glycans were liberated by hydrazinolysis and the resulting sugar chains were N-acetylated and then coupled with 2-aminopyridine. Three pyridylaminated sugar chains were purified by reversed-phase HPLC and size-fractionation HPLC. The structures were analyzed by a combination of exoand endo-glycosidase digestions, sugar chain mapping, and electrospray ionization mass spectrometry (ESIMS). Structural analysis clearly indicated that Lewis a epitope (Gal beta l-3(Fuc alpha l4) GlcNAc beta 1-), instead of the Gal beta l-4(Fuc alpha l-6) GlcNAc, occurs in the N-glycans of Cry j 1.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>16195587</pmid><doi>10.1271/bbb.69.1700</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
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ispartof Bioscience, biotechnology, and biochemistry, 2005, Vol.69 (9), p.1700-1705
issn 0916-8451
1347-6947
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source J-STAGE Free; MEDLINE; Oxford University Press Journals All Titles (1996-Current); Open Access Titles of Japan; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry
subjects ALERGENOS
ALLERGENE
ALLERGENS
Allergens - analysis
Allergens - chemistry
Antigens, Plant
Biological and medical sciences
Carbohydrate Sequence
CHEMICAL STRUCTURE
Cry j 1
Cryptomeria
CRYPTOMERIA JAPONICA
Epitopes - analysis
Epitopes - chemistry
ESTRUCTURA QUIMICA
Fundamental and applied biological sciences. Psychology
Glycoside Hydrolases - metabolism
HYPERSENSITIVITY
Japanese cedar pollen
Lewis a epitope
Molecular Sequence Data
N-glycan
Plant Proteins - analysis
Plant Proteins - chemistry
POLEN
POLLEN
Pollen - chemistry
pollen allergen
Polysaccharides - chemistry
REACCIONES ALERGICAS
REACTION ALLERGIQUE
Spectrometry, Mass, Electrospray Ionization
STRUCTURE CHIMIQUE
title Glycoform analysis of Japanese cedar [Cryptomeria japonica] pollen allergen, Cry j 1
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