ArticleBiochimica et biophysica acta. Biomembranes2026
Full-length SARS-CoV-2 envelope protein adopts an interfacial topology in lipid bilayers.
Article in Biochimica et biophysica acta. Biomembranes, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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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