Glycobiology, Vol 8, 651-661, Copyright © 1998 by Society for Glycobiology
IB Wilson, JE Harthill, NP Mullin, DA Ashford and F Altmann
Carbohydrates have been suggested to account for some IgE cross- reactions
between various plant, insect, and mollusk extracts, while some IgG
antibodies have been successfully raised against plant glycoproteins. A rat
monoclonal antibody raised against elderberry abscission tissue (YZ1/2.23)
and rabbit polyclonal antiserum against horseradish peroxidase were
screened for reactivity in enzyme-linked immunosorbent assay against a
range of plant glycoproteins and extracts as well as neoglycoproteins, bee
venom phospholipase, and several animal glycoproteins. Of the
oligosaccharides tested, Man3XylFucGlcNAc2(MMXF3) derived from horseradish
peroxidase was the most potent inhibitor of the reactivity of both YZ1/2.23
and anti- horseradish peroxidase to native horseradish peroxidase
glycoprotein. The reactivity of YZ1/2. 23 and anti-horseradish peroxidase
against Sophora japonica lectin was most inhibited by a neoglycoconjugate
of bromelain glycopeptide cross-linked to bovine serum albumin, while the
defucosylated form of this conjugate was inactive as an inhibitor. A wide
range of plant extracts was found to react against YZ1/2.23 and
anti-horseradish peroxidase, with particularly high reactivities recorded
for grass pollen and nut extracts. All these reactivities were inhibitable
with the bromelain glycopeptide/bovine serum albumin conjugate. Bee venom
phospholipase and whole bee venom reacted weakly with YZ1/2.23 but more
strongly with anti-horseradish peroxidase in a manner inhibitable with the
bromelain glycopeptide/bovine serum albumin conjugate, while hemocyanin
from Helix pomatia reacted poorly with YZ1/2.23 but did react with
anti-horseradish peroxidase. It is concluded that the alpha1, 3-fucose
residue linked to the chitobiose core of plant glycoproteins is the most
important residue in the epitope recognized by the two antibodies studied,
but that the polyclonal anti-horseradish peroxidase antiserum also contains
antibody populations that recognize the xylose linked to the core mannose
of many plant and gastropod N-linked oligosaccharides.
ORIGINAL ARTICLES
Core alpha1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant N-linked oligosaccharides and is present in a wide variety of plant extracts
Institut fur Chemie der Universitat fur Bodenkultur, Muthgasse 18, A- 1190, Wien, Austria.
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