(19−22) Here, we extend this work by analyzing the lipids around 10 different classes of plasma membrane proteins. The recent modeling of a complex plasma membrane mixture containing more than 60 different lipids, however, has opened the way to probe lipid–protein interplay in a more realistic membrane environment. (17,18) So far, most computational studies have been restricted to model membrane systems with a few lipid types. (13−16) In particular the use of coarse-grain (CG) models allows simulation of reversible binding and unbinding events and identify both strong and weakly binding lipids. Our results provide a molecular glimpse of the complexity of lipid–protein interactions, with potentially far-reaching implications for our understanding of the overall organization of real cell membranes.Ĭomputational approaches on the other hand, such as molecular dynamics (MD) simulations, can provide such details and have been extensively used to study lipid–protein interplay. The simulations detail how each protein modulates its local lipid environment in a unique way, through enrichment or depletion of specific lipid components, resulting in thickness and curvature gradients.
To provide a realistic lipid environment, the proteins are embedded in a model plasma membrane, where more than 60 lipid species are represented, asymmetrically distributed between the leaflets. Here, we use molecular dynamics simulations to characterize the lipid environment of 10 different membrane proteins. Our current understanding of the detailed organization of cell membranes remains rather elusive, because of the challenge to study fluctuating nanoscale assemblies of lipids and proteins with the required spatiotemporal resolution. Future Virology.Cell membranes contain hundreds of different proteins and lipids in an asymmetric arrangement. Membrane binding proteins of coronaviruses. The Proteins of Severe Acute Respiratory Syndrome Coronavirus-2 (SARS CoV-2 or n-COV19), the Cause of COVID-19. Properties of Coronavirus and SARS-CoV-2. The membrane protein binding with the nucleocapsid protein is responsible for nucleocapsid stabilization and viral assembly (1). The membrane-spike protein interaction is required for maintaining the spike protein within the ER-Golgi intermediate compartment (1). Additional functions show a role in inducing apoptosis as well as interactions with the spike and nucleocapsid proteins (1,2). The main functions of the membrane protein are for viral assembly and contributing to the shape and structural integrity of the viral envelope (1,2). The membrane protein exists as a dimer and is either in long or compact conformation, which contributes to the curvature of the viral membrane (2,4). Structurally, the membrane protein is a type III transmembrane glycoprotein containing a glycosylated N-terminal ectodomain, three transmembrane domains, and a large C-terminal that extends into the viral particle (2,4). Furthermore, the membrane protein of SARS-CoV-2 has 90.5% sequence identity and 98.2% sequence similarity to that of the membrane protein of SARS-CoV (2).
The membrane protein is synthesized as a 222 amino acid protein with a theoretical molecular weight of 25.1 kDa (2,3). The membrane protein is the most abundant of the four structural proteins, which also includes the envelope protein, spike protein, and nucleocapsid protein (1,2). The SARS-CoV-2 Membrane protein is one of the four major structural proteins of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative agent of COVID-19 (1).
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