IgG2 dominancy and carbohydrate recognition specificity of C3H/He mouse antibodies directed to cross-reactive carbohydrate determinants (CCDs) bearing beta-(1,2)-xylose and alpha-(1,3)-fucose.
Few common carbohydrate epitopes consisting of terminal beta-(1,2)-xylose and/or alpha-(1,3)-fucose residues are shared by a variety of glycoproteins from plants, insects and parasitic worms, termed cross-reactive carbohydrate determinant (CCD), and frequently recognized by IgE antibodies of patients with food and/or respiratory allergy, though clinical relevancy of such CCD-specific IgE is still controversial. Attention has also been focused on CCDs from the undesired post-translational modification of recombinant therapeutic proteins produced by transgenic plants and insects. In the present study, to clarify immunogenic potentials of CCD-bearing glycoproteins, the antibody response to a model plant glycoprotein, horseradish peroxidase (HRP) was investigated in a mouse model. C3H/He mice were immunized with HRP plus Al(OH)(3) or Freund's adjuvant, and IgG and IgE responses to CCDs in addition to HRP were analyzed by ELISA using some distinct glycoproteins with known N-glycan structures. IgE response to HRP was induced remarkably, whereas that to CCD was weaker and delayed. Moreover, apparent ratio of the CCD-specific antibodies to HRP-specific ones tended to be higher in IgG2a and IgG2b isotypes than IgG1, IgG3 and IgE. In contrast to rabbit antibodies, the CCD-specific antibodies from the mice gave poor reactivity with bromelain and honeybee phospholipase A2, suggesting the critical role of both beta-(1,2)-xylose and alpha-(1,3)-mannose in the CCD-recognition by the mouse antibodies. Moreover, the mouse antibodies showed weaker cross-reactivity to pollen- and insect-derived glycoproteins than the rabbit ones. Thus, in this mouse model, not only IgE but also IgG2 antibody responses to CCDs were induced by immunizing with a CCD-bearing glycoprotein, suggesting that CCDs affected not only Th2-type but also Th1-type antibody response at least in C3H/He mice.
Hino
Shingo
S
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan.
Umeda
Fumiko
F
Inumaru
Shigeki
S
Aoki
Naohito
N
Sato
Chihiro
C
Okajima
Tetsuya
T
Nadano
Daita
D
Matsuda
Tsukasa
T
D000818:Animals; D002478:Cells, Cultured; D003429:Cross Reactions / Q000276:immunology*; D018604:Epitope Mapping; D005260:Female; D005643:Fucose / Q000031:analogs & derivatives / Q000737:chemistry; D006735:Horseradish Peroxidase / Q000276:immunology* / Q000378:metabolism; D056724:Immunity, Humoral; D007117:Immunization, Secondary; D016056:Immunodominant Epitopes / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D007073:Immunoglobulin E / Q000097:blood / Q000276:immunology / Q000378:metabolism*; D007074:Immunoglobulin G / Q000097:blood / Q000276:immunology / Q000378:metabolism*; D019476:Insect Proteins / Q000276:immunology; D051379:Mice; D008809:Mice, Inbred C3H; D011817:Rabbits; D013045:Species Specificity; D014994:Xylose / Q000031:analogs & derivatives / Q000737:chemistry
D016056:Immunodominant Epitopes; D007074:Immunoglobulin G; D019476:Insect Proteins; D005643:Fucose; D007073:Immunoglobulin E; D014994:Xylose; D006735:Horseradish Peroxidase