Extended Data Fig. 6: Contact residues involved in filovirus GP binding to human NPC1. | Nature

Extended Data Fig. 6: Contact residues involved in filovirus GP binding to human NPC1.

From: Structures of Marburgvirus glycoprotein and its complex with NPC1 receptor

Extended Data Fig. 6: Contact residues involved in filovirus GP binding to human NPC1.

(a) Sequence alignment of the RBS in RAVV, two MARV strains (Musoke and Angola), and EBOV. Asterisks indicate fully conserved residues, colons indicate strongly conserved residues, and periods indicate weakly conserved residues. Receptor-binding residues are highlighted in magenta and grouped into three regions: RBS1, RBS2, and RBS3. These residues are fully conserved within the MBV genus (RAVV and MARV). Receptor-binding residues in EBOV RBS that differ from those in MBV RBS are highlighted in red. (b) List of NPC1-C residues that directly contact the RBS of RAVV or EBOV. These residues are located on three loops that interact with RAVV RBS and two loops that interact with EBOV RBS.

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