Fig. 4: N-Glycosylation sites observed in the E1–E2 ectodomain of the MAYV cryo-EM structure. | Nature Communications

Fig. 4: N-Glycosylation sites observed in the E1–E2 ectodomain of the MAYV cryo-EM structure.

From: Cryo-EM structure of the mature and infective Mayaro virus at 4.4 Å resolution reveals features of arthritogenic alphaviruses

Fig. 4: N-Glycosylation sites observed in the E1–E2 ectodomain of the MAYV cryo-EM structure.The alternative text for this image may have been generated using AI.

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.

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