scholarly journals Molecular interactions of the M and E integral membrane proteins of SARS-CoV-2

2021 ◽  
Author(s):  
Viviana Monje-Galvan ◽  
Gregory A Voth
Keyword(s):  
Membrane Proteins ◽  
Molecular Interactions ◽  
Protein Interactions ◽  
Integral Membrane Proteins ◽  
Cellular Processes ◽  
Lipid Protein Interactions ◽  
Specific Lipid

Specific lipid-protein interactions are key for cellular processes, and even more so for the replication of pathogens. The COVID-19 pandemic has drastically changed our lives and cause the death of...

scholarly journals Molecular interactions of the M and E integral membrane proteins of SARS-CoV-2

2021 ◽  
Author(s):  
Viviana Monje-Galvan ◽  
Gregory A. Voth
Keyword(s):  
Membrane Proteins ◽  
Protein Interactions ◽  
Protein Complexes ◽  
Integral Membrane Proteins ◽  
Protein Protein Interactions ◽  
Novel Treatments ◽  
Cellular Processes ◽  
Ongoing Work ◽  
Lipid Environment ◽  
Lipid Protein Interactions

AbstractSpecific lipid-protein interactions are key for cellular processes, and even more so for the replication of pathogens. The COVID-19 pandemic has drastically changed our lives and cause the death of nearly three million people worldwide, as of this writing. SARS-CoV-2 is the virus that causes the disease and has been at the center of scientific research over the past year. Most of the research on the virus is focused on key players during its initial attack and entry into the cellular host; namely the S protein, its glycan shield, and its interactions with the ACE2 receptors of human cells. As cases continue to raise around the globe, and new mutants are identified, there is an urgent need to understand the mechanisms of this virus during different stages of its life cycle. Here, we consider two integral membrane proteins of SARS-CoV-2 known to be important for viral assembly and infectivity. We have used microsecond-long all-atom molecular dynamics to examine the lipid-protein and protein-protein interactions of the membrane (M) and envelope (E) structural proteins of SARS-CoV-2 in a complex membrane model. We contrast the two proposed protein complexes for each of these proteins, and quantify their effect on their local lipid environment. This ongoing work also aims to provide molecular-level understanding of the mechanisms of action of this virus to possibly aid in the design of novel treatments.

scholarly journals Lipid-Protein Interactions of Integral Membrane Proteins: A Comparative Simulation Study

2004 ◽  
Vol 87 (6) ◽  
pp. 3737-3749 ◽  
Author(s):  
Sundeep S. Deol ◽  
Peter J. Bond ◽  
Carmen Domene ◽  
Mark S.P. Sansom
Keyword(s):  
Membrane Proteins ◽  
Protein Interactions ◽  
Simulation Study ◽  
Integral Membrane Proteins ◽  
Lipid Protein Interactions

scholarly journals Allostery revealed within lipid binding events to membrane proteins

2018 ◽  
Vol 115 (12) ◽  
pp. 2976-2981 ◽  
Author(s):  
John W. Patrick ◽  
Christopher D. Boone ◽  
Wen Liu ◽  
Gloria M. Conover ◽  
Yang Liu ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Protein Interactions ◽  
Biological Membrane ◽  
Binding Constants ◽  
Native Mass Spectrometry ◽  
Specific Protein ◽  
Lipid Binding ◽  
Allosteric Modulation ◽  
Lipid Species ◽  
Specific Lipid

Membrane proteins interact with a myriad of lipid species in the biological membrane, leading to a bewildering number of possible protein−lipid assemblies. Despite this inherent complexity, the identification of specific protein−lipid interactions and the crucial role of lipids in the folding, structure, and function of membrane proteins is emerging from an increasing number of reports. Fundamental questions remain, however, regarding the ability of specific lipid binding events to membrane proteins to alter remote binding sites for lipids of a different type, a property referred to as allostery [Monod J, Wyman J, Changeux JP (1965)J Mol Biol12:88–118]. Here, we use native mass spectrometry to determine the allosteric nature of heterogeneous lipid binding events to membrane proteins. We monitored individual lipid binding events to the ammonia channel (AmtB) fromEscherichia coli, enabling determination of their equilibrium binding constants. We found that different lipid pairs display a range of allosteric modulation. In particular, the binding of phosphatidylethanolamine and cardiolipin-like molecules to AmtB exhibited the largest degree of allosteric modulation, inspiring us to determine the cocrystal structure of AmtB in this lipid environment. The 2.45-Å resolution structure reveals a cardiolipin-like molecule bound to each subunit of the trimeric complex. Mutation of a single residue in AmtB abolishes the positive allosteric modulation observed for binding phosphatidylethanolamine and cardiolipin-like molecules. Our results demonstrate that specific lipid−protein interactions can act as allosteric modulators for the binding of different lipid types to integral membrane proteins.

scholarly journals Lipid-protein interactions are unique fingerprints for membrane proteins

2017 ◽  
Author(s):  
Valentina Corradi ◽  
Eduardo Mendez-Villuendas ◽  
Helgi I. Ingólfsson ◽  
Ruo-Xu Gu ◽  
Iwona Siuda ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Protein Interactions ◽  
Cell Membranes ◽  
Spatiotemporal Resolution ◽  
Lipid Dynamics ◽  
Lipid Species ◽  
Lipid Environment ◽  
Lipid Protein Interactions ◽  
Dynamics Simulations ◽  
Asymmetrically Distributed

ABSTRACTCell membranes contain hundreds of different proteins and lipids in an asymmetric arrangement. Understanding the lateral organization principles of these complex mixtures is essential for life and health. However, our current understanding of the detailed organization of cell membranes remains rather elusive, owing to the lack of experimental methods suitable for studying these fluctuating nanoscale assemblies of lipids and proteins with the required spatiotemporal resolution. Here, we use molecular dynamics simulations to characterize the lipid environment of ten membrane proteins. 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 leaflets. The simulations detail how each protein modulates its local lipid environment through local lipid composition, thickness, curvature and lipid dynamics. Our results provide a molecular glimpse of the complexity of lipid-protein interactions, with potentially far reaching implications for the overall organization of the cell membrane.

scholarly journals Curvature and Specific Lipid-Protein Interactions Modulate Activity of Rhodopsin

2009 ◽  
Vol 96 (3) ◽  
pp. 378a
Author(s):  
Olivier Soubias ◽  
Shui-Lin Niu ◽  
Drake C. Mitchell ◽  
Klaus Gawrisch
Keyword(s):  
Protein Interactions ◽  
Lipid Protein Interactions ◽  
Specific Lipid

Melittin: a Membrane-active Peptide with Diverse Functions

2007 ◽  
Vol 27 (4-5) ◽  
pp. 189-223 ◽  
Author(s):  
H. Raghuraman ◽  
Amitabha Chattopadhyay
Keyword(s):  
Protein Interactions ◽  
Terminal Region ◽  
Membrane Properties ◽  
Suitable Model ◽  
Amino Acid Residues ◽  
Linear Peptide ◽  
Amino Terminal ◽  
Cellular Processes ◽  
Lipid Protein Interactions ◽  
Carboxy Terminal

Melittin is the principal toxic component in the venom of the European honey bee Apis mellifera and is a cationic, hemolytic peptide. It is a small linear peptide composed of 26 amino acid residues in which the amino-terminal region is predominantly hydrophobic whereas the carboxy-terminal region is hydrophilic due to the presence of a stretch of positively charged amino acids. This amphiphilic property of melittin has resulted in melittin being used as a suitable model peptide for monitoring lipid–protein interactions in membranes. In this review, the solution and membrane properties of melittin are highlighted, with an emphasis on melittin–membrane interaction using biophysical approaches. The recent applications of melittin in various cellular processes are discussed.

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