Biophysical Society Conference | Tahoe 2024

Molecular Biophysics of Membranes

Poster Abstracts

5-POS Board 2 INVESTIGATION OF THE ASSEMBLY AND BUDDING MECHANISMS OF SARS COV-2 M PROTEIN Mandira Dutta 1 ; Gregory A Voth 1 ; 1 The University of Chicago, Department of Chemistry, Chicago, IL, USA The profound repercussions on both public health and the global economy resulting from the COVID-19 pandemic, instigated by the infection of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), have spurred unparalleled research efforts worldwide aimed at eradicating this virus. The SARS-CoV-2 virion is composed of four major structural proteins: Spike (S), Membrane (M), Envelope (E), and Nucleocapsid (N). The M protein is the most abundant structural protein in the virion surface. Its pivotal role lies in facilitating the assembly and budding processes of SARS-CoV-2. Our study investigates the intricate protein-protein and protein-lipid interactions of M protein within biologically relevant complex membrane models. We have performed atomistic molecular dynamics simulations based on recent experimental structures of M proteins; we have explored crucial lipid binding properties inherent to M proteins. These properties, we hypothesize, are critical for the assembly and budding processes of SARS-CoV-2. Additionally, we have scrutinized the conformational dynamics of distinct conformations of the M protein, elucidating how it orchestrates the curvature of the membrane through interactions with lipids. Our findings illuminate the mechanisms underpinning M protein-driven assembly and budding, thereby advancing our understanding of viral pathogenesis. Furthermore, this understanding aids in the advancement of novel antiviral therapeutics targeting viral budding processes.


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