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. 2021 Sep 9;12:5333. doi: 10.1038/s41467-021-25589-1

Fig. 2. The tail of SARS-CoV-2 S protein binds directly to moesin, WIPI3, SNX27, and to VPS26 via SNX27.

Fig. 2

a Coomassie-stained gel and immunoblot against His6 to test the binding from bacterial cell lysates of the β-propellor of the β’-COP subunit of COPI (residues 1–304 with an MBP-His6 tag) to beads coated with GST fusions to the tail of S. Experiment representative of three repeats with either His6-MBP-tag (as here) or with His6-tag. Input is 1/50 of that applied to beads. b Coomassie gel showing that the residues 1238ThrSerCys1240 of the tail of S are required for binding to SNX27. As in (a) except that the lysate was from cells overexpressing SNX27-His6. The experiment repeated three times, input 1/40 that applied to beads. c Coomassie gel showing that VPS26 requires SNX27 to bind to the tail of S protein. Same experiment as in (a) except that beads coated with the GST-fusions were incubated with bacterial lysate from cells overexpressing either SNX27-His6, His6-VPS26 or both. The experiment repeated twice. d Coomassie-stained gel and immunoblot against His6 to test the binding of the FERM domain of moesin (residues 1–300, expressed in bacterial lysate) to GST fusions to the tail of S. Experiment repeated twice, input is 1/40 (Coomassie) or 1/160 (immunoblot) of that applied to beads. e As in (d), except beads coated with the indicated GST-fusions were incubated with lysates from bacteria overexpressing WIPI3-His6. The experiment repeated twice, input is 1/14 (Coomassie) or 1/160 (immunoblot) of that applied to beads.