Fig. 2: Direct binding interaction of sarbecovirus spike hepta-peptide with αCOPI-WD40. | Communications Biology

Fig. 2: Direct binding interaction of sarbecovirus spike hepta-peptide with αCOPI-WD40.

From: An extended motif in the SARS-CoV-2 spike modulates binding and release of host coatomer in retrograde trafficking

Fig. 2

a Structural conservation of αCOPI-WD40 domain determined in the present investigation (yellow) and a previous structure (magenta). Arrow highlights main chain differences between these two αCOPI-WD40 structures in Gly168-Ala188. b–h BLI assay of N-biotinylated spike hepta-peptide with COPI-WD40 domain. One representative experiment of three is shown in panels (b–h). Color code for concentrations is given at the bottom of the figure. The equilibrium KD is provided with each sensorgram for comparison. b The spike wild-type peptide sequence demonstrates dose-dependent binding to αCOPI-WD40 domain. c Scrambling of the hepta-peptide sequence abolishes binding suggesting sequence-specific interaction. d β’COPI-WD40 demonstrates no interaction with the immobilized hepta-peptide. The mutant peptide, Gly-Val-Lys-Leu-Lys-Tyr-Thr, shows dose-dependent binding to (e) αCOPI-WD40 but not (f) β’COPI-WD40. g Acidification enhances binding between the wild-type spike hepta-peptide and αCOPI-WD40 domain. h β’COPI-WD40 shows weakly enhanced binding to the spike hepta-peptide upon acidification. “n.d.” implies not determined for weak interactions.

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