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

Abstract

The cytosolic tail of β-coronavirus spike proteins contains dibasic motifs that must be able to bind to the host’s coatomer protein-I (COPI) for trafficking and be released for viral assembly in the ER-Golgi intermediate compartment. The critical residues in both the spike cytosolic tail and COPI are identified that modulate the association-dissociation kinetics.