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- W2296072783 abstract "We report that N-linked oligosaccharide structures can be present on an asparagine residue not adhering to the consensus site motif NXS/T where X is not proline. Characterization of a recombinant human IgG2 antibody indicated that an Asn residue in the CH1 sequence TVSWN162SGAL was glycosylated. This highly atypical modification has also been observed in IgG1 antibodies derived from human donors. Site directed mutagenesis of the CH1 domain sequence in a recombinant-human IgG1 antibody resulted in an increase in non-consensus glycosylation to 3.15%, a greater than four fold increase over the level observed in the wild-type, by changing the -1 and +1 amino acids relative to the Asn residue at position 162. Following these results, we developed enrichment techniques to isolate molecules with non-consensus N-glycans based on selective endo- and exoglycosidase digestion followed by lectin chromatography. By applying our enrichment techniques, we subsequently discovered additional occurrences of non-consensus glycosylation that are present on amino acid sequences not previously described. Modeling of these residues from crystal structures provided valuable information of structural characteristics shared by these sites. These new findings shed light on the sequence requirements necessary for N-glycosylation when there is not a Ser or Thr residue present in the +2 position with respect to the glycosylated Asn. We believe that further understanding of the phenomenon of non-consensus glycosylation can be used to gain fundamental insights into the fidelity of the cellular glycosylation machinery." @default.
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- W2296072783 date "2010-04-01" @default.
- W2296072783 modified "2023-09-23" @default.
- W2296072783 title "Asparagine Linked Oligosaccharides Present on a Non‐Consensus Amino Acid Sequence in the CH1 Domain of Human Antibodies" @default.
- W2296072783 doi "https://doi.org/10.1096/fasebj.24.1_supplement.480.11" @default.
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