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TitleStructure of the dengue virus glycoprotein non-structural protein 1 by electron microscopy and single-particle analysis.
Journal, issue, pagesJ Gen Virol, Vol. 93, Issue Pt 4, Page 771-779, Year 2012
Publish dateJan 13, 2012
AuthorsDavid A Muller / Michael J Landsberg / Cheryl Bletchly / Rosalba Rothnagel / Lynne Waddington / Ben Hankamer / Paul R Young /
PubMed AbstractThe 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 ...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.
External linksJ Gen Virol / PubMed:22238236
MethodsEM (single particle)
Resolution23.0 Å
Structure data

EMDB-2073:
Structure of the dengue virus glycoprotein non-structural protein 1 by electron microscopy and single-particle analysis
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • Dengue virus 2

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