Abstract
The pollen of oil palm (Elaeis guineensis Jacq.) is a strong allergen and causes severe pollinosis in Malaysia and Singapore. In the previous study (Biosci. Biotechnol. Biochem., 64, 820-827 (2002)), from the oil palm pollens, we purified an antigenic glycoprotein (Ela g Bd 31 K), which is recognized by IgE from palm pollinosis patients. In this report, we describe the structural analysis of sugar chains linked to palm pollen glycoproteins to confirm the ubiquitous occurrence of antigenic N-glycans in the allergenic pollen. N-Glycans liberated from the pollen glycoprotein mixture by hydrazinolysis were labeled with 2-aminopyridine followed by purification with a combination of size-fractionation HPLC and reversed-phase HPLC. The structures of the PA-sugar chains were analyzed by a combination of two-dimensional sugar chain mapping, electrospray ionization mass spectrometry (ESI-MS), and tandem MS analysis, as well as exoglycosidase digestions. The antigenic N-glycan bearing α1-3 fucose and/or β1-2 xylose residues accounts for 36.9% of total N-glycans: GlcNAc2Man3Xyl1Fuc1GlcNAc 2 (24.6%), GlcNAc2Man3Xyl 1GlcNAc2 (4.4%), Man3Xyl1Fuc 1GlcNAc2 (1.1%), GlcNAc1Man3Xyl 1Fuc1GlcNAc2 (5.6%), and GlcNAc 1Man3Xyl1GlcNAc2 (1.2%). The remaining 63.1% of the total N-glycans belong to the high-mannose type structure: Man9GlcNAc2 (5.8%), Man8GlcNAc2 (32.1%), Man7GlcNAc2 (19.9%), Man6GlcNAc2 (5.3%).
| Original language | English |
|---|---|
| Pages (from-to) | 2232-2239 |
| Number of pages | 8 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 67 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - Oct 2003 |
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Keywords
- Antigenic N-glycan
- Elaeis guineensis Jacq
- Oil palm pollen
- Plant glycoprotein
- Pollen allergy
ASJC Scopus subject areas
- Food Science
- Applied Microbiology and Biotechnology
- Chemistry (miscellaneous)
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biotechnology
- Bioengineering
Cite this
Structural features of N-glycans linked to glycoproteins from oil palm pollen, an allergenic pollen. / Kimura, Yoshinobu; Yoshiie, Takeo; Kit, Woo Kwan; Maeda, Megumi; Kimura, Mariko; Tan, Siang Hee.
In: Bioscience, Biotechnology and Biochemistry, Vol. 67, No. 10, 10.2003, p. 2232-2239.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structural features of N-glycans linked to glycoproteins from oil palm pollen, an allergenic pollen
AU - Kimura, Yoshinobu
AU - Yoshiie, Takeo
AU - Kit, Woo Kwan
AU - Maeda, Megumi
AU - Kimura, Mariko
AU - Tan, Siang Hee
PY - 2003/10
Y1 - 2003/10
N2 - The pollen of oil palm (Elaeis guineensis Jacq.) is a strong allergen and causes severe pollinosis in Malaysia and Singapore. In the previous study (Biosci. Biotechnol. Biochem., 64, 820-827 (2002)), from the oil palm pollens, we purified an antigenic glycoprotein (Ela g Bd 31 K), which is recognized by IgE from palm pollinosis patients. In this report, we describe the structural analysis of sugar chains linked to palm pollen glycoproteins to confirm the ubiquitous occurrence of antigenic N-glycans in the allergenic pollen. N-Glycans liberated from the pollen glycoprotein mixture by hydrazinolysis were labeled with 2-aminopyridine followed by purification with a combination of size-fractionation HPLC and reversed-phase HPLC. The structures of the PA-sugar chains were analyzed by a combination of two-dimensional sugar chain mapping, electrospray ionization mass spectrometry (ESI-MS), and tandem MS analysis, as well as exoglycosidase digestions. The antigenic N-glycan bearing α1-3 fucose and/or β1-2 xylose residues accounts for 36.9% of total N-glycans: GlcNAc2Man3Xyl1Fuc1GlcNAc 2 (24.6%), GlcNAc2Man3Xyl 1GlcNAc2 (4.4%), Man3Xyl1Fuc 1GlcNAc2 (1.1%), GlcNAc1Man3Xyl 1Fuc1GlcNAc2 (5.6%), and GlcNAc 1Man3Xyl1GlcNAc2 (1.2%). The remaining 63.1% of the total N-glycans belong to the high-mannose type structure: Man9GlcNAc2 (5.8%), Man8GlcNAc2 (32.1%), Man7GlcNAc2 (19.9%), Man6GlcNAc2 (5.3%).
AB - The pollen of oil palm (Elaeis guineensis Jacq.) is a strong allergen and causes severe pollinosis in Malaysia and Singapore. In the previous study (Biosci. Biotechnol. Biochem., 64, 820-827 (2002)), from the oil palm pollens, we purified an antigenic glycoprotein (Ela g Bd 31 K), which is recognized by IgE from palm pollinosis patients. In this report, we describe the structural analysis of sugar chains linked to palm pollen glycoproteins to confirm the ubiquitous occurrence of antigenic N-glycans in the allergenic pollen. N-Glycans liberated from the pollen glycoprotein mixture by hydrazinolysis were labeled with 2-aminopyridine followed by purification with a combination of size-fractionation HPLC and reversed-phase HPLC. The structures of the PA-sugar chains were analyzed by a combination of two-dimensional sugar chain mapping, electrospray ionization mass spectrometry (ESI-MS), and tandem MS analysis, as well as exoglycosidase digestions. The antigenic N-glycan bearing α1-3 fucose and/or β1-2 xylose residues accounts for 36.9% of total N-glycans: GlcNAc2Man3Xyl1Fuc1GlcNAc 2 (24.6%), GlcNAc2Man3Xyl 1GlcNAc2 (4.4%), Man3Xyl1Fuc 1GlcNAc2 (1.1%), GlcNAc1Man3Xyl 1Fuc1GlcNAc2 (5.6%), and GlcNAc 1Man3Xyl1GlcNAc2 (1.2%). The remaining 63.1% of the total N-glycans belong to the high-mannose type structure: Man9GlcNAc2 (5.8%), Man8GlcNAc2 (32.1%), Man7GlcNAc2 (19.9%), Man6GlcNAc2 (5.3%).
KW - Antigenic N-glycan
KW - Elaeis guineensis Jacq
KW - Oil palm pollen
KW - Plant glycoprotein
KW - Pollen allergy
UR - http://www.scopus.com/inward/record.url?scp=3142758915&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=3142758915&partnerID=8YFLogxK
U2 - 10.1271/bbb.67.2232
DO - 10.1271/bbb.67.2232
M3 - Article
C2 - 14586113
AN - SCOPUS:3142758915
VL - 67
SP - 2232
EP - 2239
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 10
ER -