Calorimetric analysis of the interplay between synthetic Tn antigen-presenting MUC1 glycopeptides and human macrophage galactose-type lectin
Human macrophage galactose-type lectin (hMGL, HML, CD301, CLEC10A), a C-type lectin expressed by dendritic cells and macrophages, is a receptor for N-acetylgalactosamine alpha-linked to serine/threonine residues (Tn antigen, CD175) and its alpha 2,6-sialylated derivative (sTn, CD175s). Because these...
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| Main Authors: | , , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
February 9, 2021
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| In: |
Biochemistry
Year: 2021, Volume: 60, Issue: 7, Pages: 547-588 |
| ISSN: | 1520-4995 |
| DOI: | 10.1021/acs.biochem.0c00942 |
| Online Access: | Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1021/acs.biochem.0c00942
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| Author Notes: | Donella M. Beckwith, Forrest G. FitzGerald, Maria C. Rodriguez Benavente, Elizabeth R. Mercer, Anna-Kristin Ludwig, Malwina Michalak, Herbert Kaltner, Jürgen Kopitz, Hans-Joachim Gabius, and Maré Cudic |
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| 520 | |a Human macrophage galactose-type lectin (hMGL, HML, CD301, CLEC10A), a C-type lectin expressed by dendritic cells and macrophages, is a receptor for N-acetylgalactosamine alpha-linked to serine/threonine residues (Tn antigen, CD175) and its alpha 2,6-sialylated derivative (sTn, CD175s). Because these two epitopes are among malignant cell glycan displays, particularly when presented by mucin-1 (MUC1), assessing the influence of the site and frequency of glycosylation on lectin recognition will identify determinants governing this interplay. Thus, chemical synthesis of the tandem-repeat O-glycan acceptor region of MUC1 and site-specific threonine glycosylation in all permutations were carried out. Isothermal titration calorimetry (ITC) analysis of the binding of hMGL to this library of MUC1 glycopeptides revealed an enthalpy-driven process and an affinity enhancement of an order of magnitude with an increasing glycan count from 6-8 mu M for monoglycosylated peptides to 0.6 mu M for triglycosylated peptide. ITC measurements performed in D2O permitted further exploration of the solvation dynamics during binding. A shift in enthalpy-entropy compensation and contact position-specific effects with the likely involvement of the peptide surroundings were detected. KinITC analysis revealed a prolonged lifetime of the lectin-glycan complex with increasing glycan valency and with a change in the solvent to D2O. | ||
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| 700 | 1 | |a Rodriguez Benavente, Maria C. |e VerfasserIn |4 aut | |
| 700 | 1 | |a Mercer, Elizabeth R. |e VerfasserIn |4 aut | |
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