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bioRxiv · 10.1101/2021.07.26.453874

Understanding SARS-CoV-2 budding through molecular dynamics simulations of M and E protein complexes

Collins, L. T.·Elkholy, T.·Mubin, S.·Williams, R.·Ezike, K.·Singhal, A.
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Abstract

SARS-CoV-2 and other coronaviruses pose major threats to global health, yet computational efforts to understand them have largely overlooked the process of budding, a key part of the coronavirus life cycle. When expressed together, coronavirus M and E proteins are sufficient to facilitate budding into the ER-Golgi intermediate compartment (ERGIC). To help elucidate budding, we ran atomistic molecular dynamics (MD) simulations using the Feig laboratorys refined structural models of the SARS-CoV-2 M protein dimer and E protein pentamer. Our MD simulations consisted of M protein dimers and E protein pentamers in patches of membrane. By examining where these proteins induced membrane curvature in silico, we obtained insights around how the budding process may occur. Multiple M protein dimers acted together to induce global membrane curvature through protein-lipid interactions while E protein pentamers kept the membrane planar. These results could eventually help guide development of antiviral therapeutics which inhibit coronavirus budding.

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Collins, L. T., Elkholy, T., Mubin, S., Williams, R., Ezike, K., Singhal, A.. 2021-07-27. Understanding SARS-CoV-2 budding through molecular dynamics simulations of M and E protein complexes. https://doi.org/10.1101/2021.07.26.453874

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