Glycoform analysis of Japanese cedar pollen allergen, Cry j 1

Megumi Maeda, Maiko Kamamoto, Katsuhiko Hino, Shigeto Yamamoto, Manko Kimura, Mitsuhiro Okano, Yoshinobu Kimura

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)


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 exo-and endo-glycosidase digestions, sugar chain mapping, and electrospray ionization mass spectrometry (ESI-MS). Structural analysis clearly indicated that Lewis a epitope (Galβ1-3(Fucα1-4)GlcNAcβ1-), instead of the Galβ1-4(Fucα1-6)GlcNAc, occurs in the N-glycans of Cry j 1.

Original languageEnglish
Pages (from-to)1700-1705
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Issue number9
Publication statusPublished - 2005


  • Cry j 1
  • Japanese cedar pollen
  • Lewis a epitope
  • N-glycan
  • Pollen allergen

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


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