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N-Glycosylation of an IgG antibody secreted by Nicotiana tabacum BY-2 cells can be modulated through co-expression of human β-1, 4-galactosyltransferase.

Transgenic Res.. 2017-06; 
Navarre C,Smargiasso N,Duvivier L,Nader J,Far J,De Pauw E,Boutry M.
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Codon Optimization ... 2009), except that residue 377 is Gly (instead of Val) in their construct and that their Flag-tag was extended with ID. The nucleotide sequence was plant codon-optimized (GenScript) and flanked by the KpnI and SacI restriction sites. … Get A Quote

摘要

Nicotiana tabacum BY-2 suspension cells have several advantages that make them suitable for the production of full-size monoclonal antibodies which can be purified directly from the culture medium. Carbohydrate characterization of an antibody (Lo-BM2) expressed in N. tabacum BY-2 cells showed that the purified Lo-BM2 displays N-glycan homogeneity with a high proportion (>70%) of the complex GnGnXF glycoform. The stable co-expression of a human β-1,4-galactosyltransferase targeted to different Golgi sub-compartments altered Lo-BM2N-glycosylation and resulted in the production of an antibody that exhibited either hybrid structures containing a low abundance of the plant epitopes (α-1,3-fucose and β-1,2-xylose)... More

关键词

Antibody; N-Glycosylation; Plant suspension cells; β-1,4-Galactosyltransferase
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