tetano
Editor, Senior Moderator
J Phys Chem Lett
. 2021 Dec 20;12249-12255.
doi: 10.1021/acs.jpclett.1c02955. Online ahead of print.
Elucidation of SARS-Cov-2 Budding Mechanisms through Molecular Dynamics Simulations of M and E Protein Complexes
Logan Thrasher Collins[SUP] 1 2 [/SUP], Tamer Elkholy[SUP] 1 3 [/SUP], Shafat Mubin[SUP] 1 4 [/SUP], David Hill[SUP] 1 5 [/SUP], Ricky Williams[SUP] 1 6 [/SUP], Kayode Ezike[SUP] 1 7 [/SUP], Ankush Singhal[SUP] 1 8 [/SUP]
Affiliations
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 laboratory's 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 that inhibit coronavirus budding.
. 2021 Dec 20;12249-12255.
doi: 10.1021/acs.jpclett.1c02955. Online ahead of print.
Elucidation of SARS-Cov-2 Budding Mechanisms through Molecular Dynamics Simulations of M and E Protein Complexes
Logan Thrasher Collins[SUP] 1 2 [/SUP], Tamer Elkholy[SUP] 1 3 [/SUP], Shafat Mubin[SUP] 1 4 [/SUP], David Hill[SUP] 1 5 [/SUP], Ricky Williams[SUP] 1 6 [/SUP], Kayode Ezike[SUP] 1 7 [/SUP], Ankush Singhal[SUP] 1 8 [/SUP]
Affiliations
- PMID: 34928612
- DOI: 10.1021/acs.jpclett.1c02955
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 laboratory's 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 that inhibit coronavirus budding.