Title : Identification of protein O-glycosylation
site and corresponding glycans using liquid chromatography-tandem mass spectrometry via mapping accurate mass and retention time shift
Abstract :
- We reported an improved combinatorial approach for identifying site-specific O-glycosylation using both glycan cleaved and non-cleaved methods
- In this approach, a non-reducing β-elimination kit coupled with non-specific enzymes performed efficient digestion, O-glycan cleavage, and partial dephosphorylation without significant side reactions, thus enabling an automatic database search for the cleaved O-glycosylation or serine/threonine (S/T) phosphorylation sites
- From the same sample concurrently prepared without β-elimination, the corresponding intact O-glycopeptides were mapped by accurate precursor ion mass using an in-house glycan database majorly composed of GalNAc (mucin-type) core and the retention-time shift (ΔRt)
- Each glycopeptide assignment was verified by the detection of glycan-specific fragments using collision-induced dissociation (CID) to estimate False Discovery Rate (FDR)
- Using fetuin as a model, all identified S/T elimination sites were matched to multiple intact glycopeptides with a 31% FDR
- This considerably reduced to 0% FDR by ΔRt filtering
- This approach was then applied to a protein mixture composed of therapeutic Factor IX and Enbrel(®) mixed with fetuin and kappa-casein
- A total of 26 glycosylation sites each of which corresponds to 1-4 glycans were positively mapped and confirmed
- The FDR decreased from 33% to 3.3% by ΔRt filtering and exclusion of repeated peptide tags that covered the same glycosylation sites
- Moreover, the phosphorylation and O-glycosylation on the same site such as T159 of Factor IX and T170 of kappa-casein were able to be unambiguously differentiated
- Thus, our approach is useful for in-depth characterization of site-specific O-glycosylation of a simple mixture such as protein-based therapeutics
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. O-glycosylation, , -, -, site
- 10. O-glycosylation, , -, -, site
- 3. O-glycopeptides, , -, -, O-glycopeptides
- 4. glycopeptide, , -, -, glycopeptide
- 5. glycopeptides, , -, -, glycopeptides
- 8. glycosylation, , -, -, sites
- 9. glycosylation, , -, -, sites
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):