Publications by authors named "Kimberly A Dolan"
Article Synopsis
- M is a crucial structural protein in coronaviruses, specifically SARS-CoV-2, playing a key role in forming infectious virus particles and existing in two conformational states.
- The study identifies a specific interaction between the M protein and a type of lipid (ceramide-1-phosphate) that influences M's structure and its ability to facilitate virus assembly.
- Disrupting this lipid-protein interaction impacts M's localization and its interactions with other viral proteins, ultimately hindering the virus's ability to enter host cells.
SARS-CoV-2 encodes four structural proteins incorporated into virions, spike (S), envelope (E), nucleocapsid (N), and membrane (M). M plays an essential role in viral assembly by organizing other structural proteins through physical interactions and directing them to sites of viral budding. As the most abundant protein in the viral envelope and a target of patient antibodies, M is a compelling target for vaccines and therapeutics.
View Article and Find Full Text PDFGap junctions establish direct pathways for cells to transfer metabolic and electrical messages. The local lipid environment is known to affect the structure, stability and intercellular channel activity of gap junctions; however, the molecular basis for these effects remains unknown. Here, we incorporate native connexin-46/50 (Cx46/50) intercellular channels into a dual lipid nanodisc system, mimicking a native cell-to-cell junction.
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