Immunoreactivity in mammals of two typical plant glyco-epitopes, core α(1,3)-fucose and core xylose

The presence of nonmammalian core α(1,3)-fucose and core xylose glyco-epitopes on glycans N-linked to therapeutic glycoproteins produced in plants has raised the question of their immunogenicity in human therapy. We address this question by studying the distribution of these N-glycans in pea, rice,...

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Published in:Glycobiology (Oxford) 2003-06, Vol.13 (6), p.427-434
Main Authors: Bardor, Muriel, Faveeuw, Christelle, Fitchette, Anne-Catherine, Gilbert, Danièle, Galas, Ludovic, Trottein, François, Faye, Loïc, Lerouge, Patrice
Format: Article
Language:English
Subjects:
Animals
Antibodies - immunology
antibody
Carbohydrate Sequence
CID
collision-induced dissociation
ELISA
enzyme-linked immunosorbent assay
Epitopes - chemistry
Epitopes - immunology
Female
Fucose - immunology
Glycoproteins - immunology
Glycoproteins - therapeutic use
horseradish peroxidase
Horseradish Peroxidase - immunology
HRP
Humans
Immune Sera - immunology
immunogenicity
MALDI-TOF
Mammals - immunology
mass spectrometry
matrix-assisted laser desorption ionization time-of-flight
Mice
Mice, Inbred C57BL
Molecular Sequence Data
N-glycans
Oryza - chemistry
Oryza - immunology
PBS
phosphate buffered saline
phospholipase A2
Pisum sativum - chemistry
Pisum sativum - immunology
PLA2
Plants - chemistry
Plants - immunology
post source decay
PSD
Rats
Rats, Wistar
recombinant proteins
transgenic plants
Xylose - immunology
Zea mays - chemistry
Zea mays - immunology
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container_end_page 434
container_issue 6
container_start_page 427
container_title Glycobiology (Oxford)
container_volume 13
creator Bardor, Muriel
Faveeuw, Christelle
Fitchette, Anne-Catherine
Gilbert, Danièle
Galas, Ludovic
Trottein, François
Faye, Loïc
Lerouge, Patrice
description The presence of nonmammalian core α(1,3)-fucose and core xylose glyco-epitopes on glycans N-linked to therapeutic glycoproteins produced in plants has raised the question of their immunogenicity in human therapy. We address this question by studying the distribution of these N-glycans in pea, rice, and maize (which are the crops intended for the production of therapeutic proteins) and by reinvestigating their immunogenicity in rodents. We found that immunization with a model glycoprotein, horseradish peroxidase, elicits in C57BL/6 mice and rats the production of antibodies (Abs) specific for core α(1,3)-fucose and core xylose epitopes. Furthermore, we demonstrated that about 50% of nonallergic blood donors contains in their sera Abs specific for core xylose, whereas 25% have Abs against core α(1,3)-fucose. These Abs probably result from sensitization to environmental antigens. Although the immunological significance of these data is too speculative at the moment, the presence of such Abs might introduce some limitations to the use of plant-derived biopharmaceutical glycoproteins, such as an accelerated clearance during human therapy.
doi_str_mv 10.1093/glycob/cwg024
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e-mail: plerouge@crihan.fr</notes><notes>istex:F855E5A9BEE9593FE69D99094C78F2D3966D6F70</notes><notes>ark:/67375/HXZ-JV88BW5H-1</notes><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>The presence of nonmammalian core α(1,3)-fucose and core xylose glyco-epitopes on glycans N-linked to therapeutic glycoproteins produced in plants has raised the question of their immunogenicity in human therapy. We address this question by studying the distribution of these N-glycans in pea, rice, and maize (which are the crops intended for the production of therapeutic proteins) and by reinvestigating their immunogenicity in rodents. We found that immunization with a model glycoprotein, horseradish peroxidase, elicits in C57BL/6 mice and rats the production of antibodies (Abs) specific for core α(1,3)-fucose and core xylose epitopes. Furthermore, we demonstrated that about 50% of nonallergic blood donors contains in their sera Abs specific for core xylose, whereas 25% have Abs against core α(1,3)-fucose. These Abs probably result from sensitization to environmental antigens. Although the immunological significance of these data is too speculative at the moment, the presence of such Abs might introduce some limitations to the use of plant-derived biopharmaceutical glycoproteins, such as an accelerated clearance during human therapy.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>12626420</pmid><doi>10.1093/glycob/cwg024</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record>
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source Oxford Academic Journals (OUP)
subjects Animals
Antibodies - immunology
antibody
Carbohydrate Sequence
CID
collision-induced dissociation
ELISA
enzyme-linked immunosorbent assay
Epitopes - chemistry
Epitopes - immunology
Female
Fucose - immunology
Glycoproteins - immunology
Glycoproteins - therapeutic use
horseradish peroxidase
Horseradish Peroxidase - immunology
HRP
Humans
Immune Sera - immunology
immunogenicity
MALDI-TOF
Mammals - immunology
mass spectrometry
matrix-assisted laser desorption ionization time-of-flight
Mice
Mice, Inbred C57BL
Molecular Sequence Data
N-glycans
Oryza - chemistry
Oryza - immunology
PBS
phosphate buffered saline
phospholipase A2
Pisum sativum - chemistry
Pisum sativum - immunology
PLA2
Plants - chemistry
Plants - immunology
post source decay
PSD
Rats
Rats, Wistar
recombinant proteins
transgenic plants
Xylose - immunology
Zea mays - chemistry
Zea mays - immunology
title Immunoreactivity in mammals of two typical plant glyco-epitopes, core α(1,3)-fucose and core xylose
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