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A single C-terminal residue controls SARS-CoV-2 spike trafficking and incorporation into VLPs
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A single C-terminal residue controls SARS-CoV-2 spike trafficking and incorporation into VLPs
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Journal Article
A single C-terminal residue controls SARS-CoV-2 spike trafficking and incorporation into VLPs
2023
Overview
The spike (S) protein of SARS-CoV-2 is delivered to the virion assembly site in the ER-Golgi Intermediate Compartment (ERGIC) from both the ER and cis-Golgi in infected cells. However, the relevance and modulatory mechanism of this bidirectional trafficking are unclear. Here, using structure-function analyses, we show that S incorporation into virus-like particles (VLP) and VLP fusogenicity are determined by coatomer-dependent S delivery from the cis-Golgi and restricted by S-coatomer dissociation. Although S mimicry of the host coatomer-binding dibasic motif ensures retrograde trafficking to the ERGIC, avoidance of the host-like C-terminal acidic residue is critical for S-coatomer dissociation and therefore incorporation into virions or export for cell-cell fusion. Because this C-terminal residue is the key determinant of SARS-CoV-2 assembly and fusogenicity, our work provides a framework for the export of S protein encoded in genetic vaccines for surface display and immune activation.
Dey et al. use structure-function methods to show that partial mimicry of the coatomer-binding motif in the SARS-CoV-2 spike is crucial for its release post coatomer-dependent delivery, thus ensuring optimal spike fusogenicity and VLP incorporation.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Assembly
/ Binding
/ COVID-19
/ Golgi
/ Golgi Apparatus - metabolism
/ Humanities and Social Sciences
/ Humans
/ Mimicry
/ Proteins
/ Residues
/ Science
/ Science & Technology - Other Topics
/ Severe acute respiratory syndrome coronavirus 2
/ Spike Glycoprotein, Coronavirus - genetics
/ Spike Glycoprotein, Coronavirus - metabolism
/ Structure-function relationships
/ Virions
