Journal
SCIENTIFIC REPORTS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-019-53052-1
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Funding
- AMED [JP19ae0101026, JP19ae0101027]
- Japan Society for the Promotion of Science [KAKENHI] [21390018, 25293011, 26670023]
- JSPS Core-to-Core programs entitled International Core Research Center for Phototheranostics
- Grants-in-Aid for Scientific Research [21390018, 26670023, 25293011] Funding Source: KAKEN
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Anti-mucinl (MUC1) antibodies have long been used clinically in cancer diagnosis and therapy and specific bindings of some of them are known to be dependent on the differential glycosylation of MUC1. However, a systematic comparison of the binding specificities of anti-MUC1 antibodies was not previously conducted. Here, a total of 20 glycopeptides including the tandem repeat unit of MUC1, APPAHGVTSAPDTRPAPGSTAPPAHGV with GalNAc (Tn-antigen), Gal beta 1-3GalNAc (T-antigen), NeuAc alpha 2-3Gal beta 1-3GalNAc (sialyl-T-antigen), or NeuAc alpha 2-6GalNAc (sialyl-Tn-antigen) at each threonine or serine residue were prepared by a combination of chemical glycopeptide synthesis and enzymatic extension of carbohydrate chains. These glycopeptides were tested by the enzyme-linked immunosorbent assay (ELISA) for their capacity to bind 13 monoclonal antibodies (mAbs) known to be specific for MUC1. The results indicated that anti-MUC1 mAbs have diverse specificities but can be classified into a few characteristic groups based on their binding pattern toward glycopeptides in some cases having a specific glycan at unique glycosylation sites. Because the clinical significance of some of these antibodies was already established, the structural features identified by these antibodies as revealed in the present study should provide useful information relevant to their further clinical use and the biological understanding of MUC1.
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