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Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers
Published on: March 8, 2012
Full-length SARS-CoV-2 envelope protein adopts an interfacial topology in lipid bilayers
Andrew K Morris1, Luke Wardrip1, Indra Dev Sahu2
1Department of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA.
Abstract:
The envelope protein is essential for the replication of coronaviruses. Several structures of the envelope protein of the SARS-CoV-2 and the closely related SARS viruses are available. However, an experimental structure of the entire full-length protein in a native lipid environment has not been determined. In addition, significant structural differences exist between published models, and the conformation adopted by the C-terminal domain is only partially understood. CW-EPR power saturation and EPR lineshape analysis of 15 different labeled sites were carried out on the full-length envelope protein of SARS-CoV-2 in POPC/POPG vesicles to determine the membrane topology. In conjunction with coarse-grained molecular dynamics, the results support a model where the C-terminal domain helices as well as the N-terminal domain are in direct contact with the lipid headgroups of the ER cytoplasmic leaflet of the membrane.
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