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. 2021 May 24;12:3038. doi: 10.1038/s41467-021-23400-9

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© The Author(s) 2021

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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Fig. 4 — A E1 (N141) and E2 (N262) N-glycosylation sites. B On the left, zoom at the E2 N262 glycosylation with the carbohydrate monomers modelled. Polar residues under hydrogen bond distances are shown in sticks and labelled. On the right, detail of the E1 N141 site with the carbohydrates modelled. C Equivalent asparagine residues regions found in EEEV (cyan), VEEV (orange), SINDV (yellow) and CHIKV (grey) cryo-EM structures are shown superposed to the MAYV structure. MAYV density map is in mesh representation. D Base peak chromatogram derived from UPLC-MS/MS analyses of N-glycans released from E1/E2 glycoproteins of MAYV. Nine peaks were integrated (#1 to #9), being further characterized based on the MS1 isotopic and MS2 fragmentation patterns as N-glycans composed by combinations of N-acetyl-hexosamine (HexNAc); hexoses (Hex) or fucose (Fuc) as indicated. GlcNAc (NAG) and Man (MAN) were assigned as the hexosamine and hexose monomers based on enzyme PNGase F and EndoH specificity and cryo-EM density map interpretation.