Tell us about yourself?
I work as a Research Associate in Mass Spectrometry Core Facility at the Johns Hopkins University. My interest is in O-linked glycosylation and I have developed a series of glycoproteomic methods to study protein N- and O-linked glycosylation.
What is new with the ExoO method you have developed?
Using EXoO, scientists can start to gain new insight into their biological systems regarding O-linked glycoproteins. The EXoO method identifies a large number of O-linked glycosylation sites in the sample that may be easily identified by using other methods such as various enrichments coupled with ETD-MS/MS.
What are the benefits of applying Operator in the workflow?
The OpeRATOR enzyme is a key component in the workflow. The high specificity of OpeRATOR enabled release of site-specific O-linked glycopeptides from solid phase support. Therefore, the resulting glycopeptides are relatively pure for improved identification.
How did you perform the analysis prior to this method?
We tried to released O-glycopeptides using beta-elimination to study site of protein O-linked glycosylation and ETD-MS/MS for O-linked glycopeptide analysis but the number of identification is lower than the use of the current method using EXoO to release the O-glycopeptides.
How would you describe the impact of OpeRATOR on the O-glycan field?
The discovery of OpeRATOR changes of the game in the field of O-linked glycoproteomics. It makes the analysis of large-scale and site-specific O-linked glycoproteome in clinical samples feasible.
What are your thoughts on the future of O-glycan analysis?
EXoO and OpeRATOR provide unique research tools to identify the site of O-linked glycosylation. So far, the evidence supports that core 1 Gal-GalNAc structure can be studied by the use of OpeRATOR. In the future, the structures of O-linked glycans on the specific sites on the proteins can be revealed in a single workflow.
