Fig. 6: Location of protein receptor- and HS-binding residues on the EEEV E2 trimer. | Nature Communications

Fig. 6: Location of protein receptor- and HS-binding residues on the EEEV E2 trimer.

From: Three positively charged binding sites on the eastern equine encephalitis virus E2 glycoprotein coordinate heparan sulfate- and protein receptor-dependent infection

Fig. 6

A ribbon model of the structure of EEEV E2 proteins as they appear in the E1/E2 trimeric spike. Side chains are displayed for residues involved in HS-binding (blue), residues identified in structural analysis as being involved in binding to one VLDLR molecule11,12,13 (red), and residues that are involved in both HS-binding and are direct contacts for VLDLR-binding (purple). Side chains for residues mutated during in vitro passage are lime green (K562-VLDLR) or cyan (BHK-21). A Top view. B Side view. Figures were made using UCSF ChimeraX53,54.

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