Fig. 4: Glycosylation analysis of the PEDV PT52 S. | Nature Communications

Fig. 4: Glycosylation analysis of the PEDV PT52 S.

From: In situ structure and dynamics of an alphacoronavirus spike protein by cryo-ET and cryo-EM

Fig. 4: Glycosylation analysis of the PEDV PT52 S.

The cryo-EM maps of PEDV PT52 S in all D0-down (D0DDD) arrangements (a) and only one D0-up (D0UDD) arrangement (b). c, d The EM maps were displayed at a low threshold with the D0 and protruding glycan densities highlighted in hot pink and blue, respectively. The respective S protein cryo-EM maps were low-pass filtered, and shown as transparent isosurfaces superimposed with their respective atomic models. e Cryo-EM densities of representative glycans and their modeled atomic coordinates. f EM map and atomic model of the N-glycan on Asn216. g N-glycan on Asn324 of the S2 subunit that makes extensive contact with D0 in the D0-up conformation. h Protein-glycan interactions between the D0 and S2 subunit in the D0-down conformation. i The representative glycoforms of the recombinant PEDV PT52 S expressed in IPEC-J2 cells. The individual glycans are depicted in symbols following the standard Symbol Nomenclature For Glycans (SNFG)88, as indicated on the right. Note that the complex type N-glycans of PT52 S produced in IPEC-J2 cells carried extra hexoses (open circle) attributable to terminal Galα1-3Gal-GlcNAc, in addition to Neu5Ac (magenta diamond)-sialylated Gal-GlcNAc antenna, at Asn62, Asn118, Asn216, Asn300, Asn344, Asn351, Asn556, and Asn667.

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