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A Remote Secondary Binding Pocket Promotes Heteromultivalent Targeting of DC-SIGN

Robert Wawrzinek, Eike‐Christian Wamhoff, Jonathan Lefèbre, Mareike Rentzsch, Gunnar Bachem, Gary Domeniconi, Jessica Schulze, Felix F. Fuchsberger, Hengxi Zhang, Carlos P. Modenutti, Lennart Schnirch, Marcelo A. Martí, Oliver Schwardt, Maria Bräutigam, Mónica Guberman, Dirk Hauck, Peter H. Seeberger, Oliver Seitz, Alexander Titz, Beat Ernst, Christoph Rademacher

2021Journal of the American Chemical Society32 citationsDOIOpen Access PDF

Abstract

cell lines. Mechanistic investigations combining NMR spectroscopy with molecular docking and molecular dynamics simulations led to the identification of a secondary binding pocket for the glycomimetics. This pocket, located remotely of DC-SIGN's carbohydrate bindings site, can be leveraged by heteromultivalent avidity enhancement. We further present preliminary evidence that the aglycone allosterically activates glycan recognition and thereby contributes to DC-SIGN-specific cell targeting. Our findings have important implications for both translational and basic glycoscience, showcasing heteromultivalent targeting of DCs to improve specificity and supporting potential allosteric regulation of DC-SIGN and CLRs in general.

Topics & Concepts

DC-SIGNChemistryLangerinGlycanAllosteric regulationGlycobiologyAvidityDocking (animal)Molecular recognitionComputational biologyCell biologyDendritic cellBiochemistryReceptorAntigenGlycoproteinImmunologyBiologyNursingOrganic chemistryMedicineMoleculeImmunotherapy and Immune ResponsesGlycosylation and Glycoproteins ResearchRNA Interference and Gene Delivery
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