Figure 3
From: A novel glycosylated anti-CD20 monoclonal antibody from transgenic cattle
Characterization of the N-glycosylation patterns and crystal structures of the recombinant anti-CD20 mAb and Rituxan. (a) Comparison of the LC-MS peptide-mapping results of the recombinant mAb and Rituxan. The upper panel with red peaks represents the peptide peak assignment of the recombinant mAb, while the bottom panel with green peaks represents those of Rituxan. (b,c) Comparison of the oligosaccharide profiles of Rituxan (b) and the recombinant mAb (c), as analysed by MS. The major peaks in the spectra are labelled with the oligosaccharide structure assignments. (d) Overall structure of the recombinant mAb Fc fragment. The glycosylated glycan is shown in stick representation. (e) Structural superimposition between the recombinant mAb Fc fragment (green) and Rituxan Fc fragment (PDB: 1L6X). (f) The “omit” electron density map of the glycosylation site at Asn 297 in the recombinant mAb Fc fragment, contoured at 1.0 σ.
