Journal
PROTEIN & CELL
Volume 2, Issue 1, Pages 41-47Publisher
SPRINGEROPEN
DOI: 10.1007/s13238-011-1007-4
Keywords
BY2 cells; N-glycosylation; glycosyltransferase; RNA interference
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Funding
- National Natural Science Foundation of China [31030047]
- European Commission [SP22-CT-2004-511060]
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Plants are known to be efficient hosts for the production of mammalian therapeutic proteins. However, plants produce complex N-glycans bearing beta 1,2-xylose and core alpha 1,3-fucose residues, which are absent in mammals. The immunogenicity and allergenicity of plant-specific N-glycans is a key concern in mammalian therapy. In this study, we amplified the sequences of 2 plant-specific glycosyltransferases from Nicotiana tabacum L. cv Bright Yellow 2 (BY2), which is a well-established cell line widely used for the expression of therapeutic proteins. The expression of the endogenous xylosyltranferase (XylT) and fucosyltransferase (FucT) was down-regulated by using RNA interference (RNAi) strategy. The xylosylated and core fucosylated N-glycans were significantly, but not completely, reduced in the glyco-engineered lines. However, these RNAi-treated cell lines were stable and viable and did not exhibit any obvious phenotype. Therefore, this study may provide an effective and promising strategy to produce recombinant glycoproteins in BY2 cells with humanized N-glycoforms to avoid potential immunogenicity.
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