1996
DOI: 10.1007/bf00731443
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Structures and contribution to the antigenicity of oligosaccharides of Japanese cedar (Cryptomeria japonica) pollen allergenCry j I: relationship between the structures and antigenic epitopes of plantN-linked complex-type glycans

Abstract: The oligosaccharide structures of Cry j I, a major allergenic glycoprotein of Cryptomeria japonica (Japanese cedar, sugi), were analysed by 400 MHz 1H-NMR and two-dimensional sugar mapping analyses. The four major fractions comprised a series of biantennary complex type N-linked oligosaccharides that share a fucose/xylose-containing core and glucosamine branches including a novel structure with a nongalactosylated fucosylglucosamine branch. Rabbit polyclonal anti-Cry j I IgG antibodies cross-reacted with three… Show more

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Cited by 61 publications
(53 citation statements)
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“…Biantennary complex-type N-glycans, called in the past "laccase-type N-glycans" and now renamed "Le acontaining N-glycans" after examination of their structure, have been so far described in only a few secreted glycoproteins (Takahashi et al, 1986(Takahashi et al, , 1990Ogawa et al, 1996). We showed in a previous study that a large number of higher plant glycoproteins are glycosylated with Le acontaining N-glycans .…”
Section: Discussionmentioning
confidence: 93%
“…Biantennary complex-type N-glycans, called in the past "laccase-type N-glycans" and now renamed "Le acontaining N-glycans" after examination of their structure, have been so far described in only a few secreted glycoproteins (Takahashi et al, 1986(Takahashi et al, , 1990Ogawa et al, 1996). We showed in a previous study that a large number of higher plant glycoproteins are glycosylated with Le acontaining N-glycans .…”
Section: Discussionmentioning
confidence: 93%
“…9) However, inhibition assay revealed that the carbohydrates on Cry j 1 were not always necessary for the binding of specific IgE in humans. 11) Though conformational epitopes of Cry j 1 play major roles in allergy, information of linear epitopes seems to be useful for the evaluation of cross-reactivity of IgE antibodies, and linear epitopes are suggested to be stable. Furthermore, information of B-cell linear epitopes is needed for future safety immunotherapy using allergenicity-decreased proteins.…”
Section: Fig 2 Results Of Spots Assaymentioning
confidence: 99%
“…and Ogawa et al 12) have reported that the plant complex type N-glycans on Cry j I themselves are not essentially involved in the binding to allergic human IgE but contribute partially to build up a relevant epitope conformation with the peptides portion, since they found that an allergic human IgE that recognizes Cry j I could not recognize other plant glycoproteins bearing the plant complex type N-glycans.…”
Section: )mentioning
confidence: 99%
“…It has been reported that allergens puriˆed from plant materials are often glycoproteins, to which the plant complex type N-glycans bearing b 1-2 xylose and W or a1-3 fucose residue(s) are bound. [3][4][5][6][7][8][9][10][11][12][13][14][15][16] Several groups (Garcia-Casado et al, 7) Ohsuga et al, 8) F äotisch et al, 9) van Ree et al 10) ) have reported that b 1-2 xylose and W or a1-3 fucose residues are essential in the recognition of the allergenic glycoproteins by allergic human IgE, postulating that the plant complex type N-glycans could be an important epitope in the allergenic response. On the other hand, Hijikata et al…”
mentioning
confidence: 99%