SARS-CoV-2 membrane protein biogenesis
Ortiz Mateu, J.; Pearson, G. J.; Rius-Salvador, M.; Sedighian, S.; Pavlova, A.; Alonso-Romero, J.; Acosta-Caceres, J. M.; Metola, A.; Garcia-Murria, M. J.; Skehel, J. M.; Gumbart, J. C.; Carlton, J. C.; von Heijne, G.; Sanchez-del Pino, M. M.; Martinez-Gil, L.; Mingarro, I.
Show abstract
Viral protein biogenesis underpins every viral life cycle stage, and elucidating these processes could reveal fundamental principles of virus-host interaction, and vulnerabilities amenable to therapeutic targeting. Here we apply biophysical, molecular, and cell biology techniques to investigate the insertion, folding, and oligomerization of the SARS-CoV-2 M protein. We describe the sequential co-translational insertion of the hydrophobic core, and demonstrate that the cytosolic C-terminal domain undergoes slower adoption of its tertiary structure. Additionally, we characterize how the transmembrane domain bundle facilitates M-protein oligomerization. Our results reveal a hydrophobic residue cluster that is essential for protein folding and co-translational dimerization. Additionally, we identify the cellular machinery responsible for targeting and inserting the M protein into the ER membrane, and chaperones and cofactors that may contribute to proper folding.
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