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. 2018 Mar 13;8:4407. doi: 10.1038/s41598-018-22729-4

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© The Author(s) 2018

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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Characterization of the SNAP-mGlu₅-∆856 N-glycosylation profile in HEK293 cells. (A) The five mGlu₅ N-linked glycosylation sites are highlighted as surface spheres (red) and the sugar moieties in green on the cartoon structure (grey) of the VFT (code pdb 3LMK). Atoms in the glutamate molecules bound to the VFT are represented as blue spheres. (B) SDS-PAGE gel migration of monomeric SNAP-mGlu₅-Δ856 and different N-glycosylation mutants. Samples were treated with reducing agent (DTT). (C) Cell surface expression of the fluorescently labeled SNAP-mGlu₅-Δ856 and different N-glycosylation mutants using SNAP-Lumi4Tb. Gel is representative of one experiment repeated at least two time. Expression profiles are representative of at least three separate experiments. Dunnett’s test as part of one-way ANOVA was used for comparison with hmGlu₅-Δ856 set as reference level.