Hi,

Protein glycosylation can occur on asparagine (N-linked) or on serine/threonine (O-linked). There is a multitude of approaches involving enzymatic (either proteolytic or glycolytic) treatments, liquid chromatography and mass spectrometry that can provide insight into changes (i.e. increase) in the mass of your protein and whether this is the result of glycosylation in your CDR (complementarity-determining regions).

You could for example digest your antibody with IdEs and separate the generated species (Fc and Fab) to see whether your Fab domains (that contain the CDRs) exhibits a mass increase upon exposure of the antibody to pathogen.

If this is the case, you could proceed by using an additional protease to perform peptide mapping, which will allow you to determine the site(s) of glycosylation.

Hope this helps: good luck!

You might find these helpful.

Thank you, Eef it does help.

Thank you for the links, Vincent.