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. Author manuscript; available in PMC: 2022 Oct 15.
Published in final edited form as: J Immunol. 2021 Sep 20;207(8):2005–2014. doi: 10.4049/jimmunol.2100225

Figure 3. Mass spectrometry analysis of N-glycan occupancy in MuSK- and AChR-specific human monoclonal antibodies.

Figure 3.

Validation of N-glycan variable region occupancy in three patient-derived monoclonal anti-MuSK antibodies (MUSK1A, MUSK1B, MUSK3-28) and one patient-derived monoclonal anti-AChR antibody (monoclonal antibody 637). Schematic of variable regions for anti-MuSK antibodies indicating regions (CDR or FWR) and localization of putative N-linked glycosylation amino acid motifs alongside deconvoluted mass spectra of the associated constructs (labels). This is shown for MUSK1A (A), MUSK1B (B), MUSK3-28 (C) and mAb 637 (D).