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. 2017 Jul 27;7:6713. doi: 10.1038/s41598-017-07220-w

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Structure and membrane nanoscale organization of DC-SIGN. (A) DC-SIGN is type-II C-type lectin (N-terminus is intracellular) that has an extracellular Carbohydrate Recognition Domain (CRD), a region of 7.5 amino acid repeats, preceded by a site for N-glycosylation (amino acid N80), a transmembrane region and a short cytoplasmic tail. In this study, besides the wild-type, several mutants of DC-SIGN were used: DC-SIGN-ΔCRD, which lacks the ligand binding domain; DC-SIGN-N80A, which carries a point mutation that abolish N-glycosylation; and DC-SIGN-ΔRep, which only lacks the repeat region²⁵. (B) Except for DC-SIGN-ΔRep, all the other variants can form tetramers and organize in small nanoclusters within the plasma membrane¹⁰.