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. 2019 Oct 4;7:650. doi: 10.3389/fchem.2019.00650

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Copyright © 2019 Li, Hogervorst, Achilli, Bruijns, Arnoldus, Vivès, Wong, Thépaut, Meeuwenoord, van den Elst, Overkleeft, van der Marel, Filippov, van Vliet, Fieschi, Codée and van Kooyk.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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DC-SIGN has the highest affinity for α1,2-di-mannoside in a hexavalent configuration on multiple interaction levels. (A) Surface plasmon resonance (SPR) analysis demonstrates increase of affinity for DC-SIGN with increasing multivalence (n = 1 > 2 > 3 > 6). Clusters presenting the α1,2-di-mannoside 5 (B series) have the highest affinity in comparison to the other mannosides in this array. (B) Binding of the biotinylated mannoside library to DC-SIGN on moDC was measured by flow cytometry. Normalized to the unbound control, the clusters displayed increased binding with increasing multivalence. (C) Overall binding profile of the library, normalized to A1, indicating that the highest affinity binders are the B6, C6, D6, E3, and E6 clusters. *p < 0.05 and **p < 0.01.