Experimental and theoretical occupancy of TfR N-glycosylation sites.

1Based on the predicted amino acid sequences for ESAG6 (GenBank: CAQ57442.1) and ESAG7 (GenBank: CAQ57441.1) minus their predicted 17-residue N-terminal signal peptides.2Predicted isoelectric point of the glycosylation sequon ±5 amino acid residues, as shown, calculated using ExPASy Compute pI/MW.3Experimentally determined (E) or theoretically predicted (P) sensitivity (+) or resistance (−) of the N-glycan to Endo H at the glycosylation site.4The major triantennary Endo H sensitive oligomannose Man5GlcNac2 structure is Manα1-3(Manα1-3(Manα1-6-Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAc and the major biantennary Endo H resistant paucimannose Man4GlcNac2 structure is Manα1-2Manα1-3(Manα1-6Manβ1-4GlcNAcβ1-4GlcNAc.