title: Covalently circularized nanodiscs for studying membrane proteins and viral entry.
abstract: We engineered covalently circularized nanodiscs (cNDs) which, compared with standard nanodiscs, exhibit enhanced stability, defined diameter sizes and tunable shapes. Reconstitution into cNDs enhanced the quality of nuclear magnetic resonance spectra for both VDAC-1, a β-barrel membrane protein, and the G-protein-coupled receptor NTR1, an α-helical membrane protein. In addition, we used cNDs to visualize how simple, nonenveloped viruses translocate their genomes across membranes to initiate infection.
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: Mahmoud L
authors.initials: ML
authors.lastname: Nasr
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: Diego
authors.initials: D
authors.lastname: Baptista
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: Mike
authors.initials: M
authors.lastname: Strauss
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: Zhen-Yu J
authors.initials: ZJ
authors.lastname: Sun
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: Simina
authors.initials: S
authors.lastname: Grigoriu
authors.affiliation: Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: Sonja
authors.initials: S
authors.lastname: Huser
authors.affiliation: Department of Biochemistry, University of Zurich, Zurich, Switzerland.
authors.forename: Andreas
authors.identifier: 0000-0003-4191-5306
authors.initials: A
authors.lastname: Plückthun
authors.affiliation: Department of Chemistry and Institute for Advanced Study, Technische Universität München and Helmholtz Centre Munich, Munich, Germany.
authors.forename: Franz
authors.initials: F
authors.lastname: Hagn
authors.affiliation: Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: Thomas
authors.initials: T
authors.lastname: Walz
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: James M
authors.initials: JM
authors.lastname: Hogle
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
authors.forename: Gerhard
authors.initials: G
authors.lastname: Wagner
mesh_terms: D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011051:Poliomyelitis / Q000378:metabolism / Q000821:virology; D017955:Poliovirus / Q000502:physiology; D018028:Receptors, Neurotensin / Q000378:metabolism*; D053586:Virus Internalization; D050995:Voltage-Dependent Anion Channel 1 / Q000378:metabolism*
chemical_list: D008051:Lipid Bilayers; D018028:Receptors, Neurotensin; C114036:neurotensin type 1 receptor; D050995:Voltage-Dependent Anion Channel 1