title: Structure of the dengue virus glycoprotein non-structural protein 1 by electron microscopy and single-particle analysis.
abstract: The flavivirus non-structural protein 1 (NS1) is a glycoprotein that is secreted as a soluble hexameric complex during the course of natural infection. Growing evidence indicates that this secreted form of NS1 (sNS1) plays a significant role in immune evasion and modulation during infection. Attempts to determine the crystal structure of NS1 have been unsuccessful to date and relatively little is known about the macromolecular organization of the sNS1 hexamer. Here, we have applied single-particle analysis to images of baculovirus-derived recombinant dengue 2 virus NS1 obtained by electron microscopy to determine its 3D structure to a resolution of 23 Å. This structure reveals a barrel-like organization of the three dimeric units that comprise the hexamer and provides further insights into the overall organization of oligomeric sNS1.
authors.affiliation: Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, 4072, Australia.
authors.forename: David A
authors.initials: DA
authors.lastname: Muller
authors.affiliation: Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland, 4072, Australia.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Landsberg
authors.affiliation: Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, 4072, Australia.
authors.forename: Cheryl
authors.initials: C
authors.lastname: Bletchly
authors.affiliation: Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland, 4072, Australia.
authors.forename: Rosalba
authors.initials: R
authors.lastname: Rothnagel
authors.affiliation: CSIRO, Materials Science and Engineering, Bayview Avenue, Clayton South, Victoria, 3169, Australia.
authors.forename: Lynne
authors.initials: L
authors.lastname: Waddington
authors.affiliation: Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland, 4072, Australia.
authors.forename: Ben
authors.initials: B
authors.lastname: Hankamer
authors.affiliation: Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland, 4072, Australia.|Australian Infectious Diseases Research Centre, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, 4072, Australia.
authors.forename: Paul R
authors.initials: PR
authors.lastname: Young
mesh_terms: D000818:Animals; D000956:Antigens, Viral / Q000276:immunology; D002522:Chlorocebus aethiops; D003716:Dengue Virus / Q000648:ultrastructure*; D004591:Electrophoresis, Polyacrylamide Gel; D007090:Image Interpretation, Computer-Assisted; D046529:Microscopy, Electron, Transmission; D011487:Protein Conformation; D011994:Recombinant Proteins; D014709:Vero Cells; D017361:Viral Nonstructural Proteins / Q000276:immunology / Q000302:isolation & purification / Q000648:ultrastructure*
chemical_list: D000956:Antigens, Viral; C079340:NS1 protein, Dengue virus type 2; D011994:Recombinant Proteins; D017361:Viral Nonstructural Proteins