Elucidation of SARS-Cov-2 Budding Mechanisms through Molecular Dynamics Simulations of M and E Protein Complexes.
J Phys Chem Lett
; 12(51): 12249-12255, 2021 Dec 30.
Article
in English
| MEDLINE | ID: covidwho-1586057
Preprint
This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
See preprint
This scientific journal article is probably based on a previously available preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
See preprint
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.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Viral Matrix Proteins
/
Molecular Dynamics Simulation
/
Coronavirus Envelope Proteins
/
SARS-CoV-2
Limits:
Humans
Language:
English
Journal:
J Phys Chem Lett
Year:
2021
Document Type:
Article
Affiliation country:
Acs.jpclett.1c02955
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