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Structure of the Newcastle disease virus F protein in the post-fusion conformation.

Abstract
The paramyxovirus F protein is a class I viral membrane fusion protein which undergoes a significant refolding transition during virus entry. Previous studies of the Newcastle disease virus, human parainfluenza virus 3 and parainfluenza virus 5 F proteins revealed differences in the pre- and post-fusion structures. The NDV Queensland (Q) F structure lacked structural elements observed in the other two structures, which are key to the refolding and fusogenic activity of F. Here we present the NDV Australia-Victoria (AV) F protein post-fusion structure and provide EM evidence for its folding to a pre-fusion form. The NDV AV F structure contains heptad repeat elements missing in the previous NDV Q F structure, forming a post-fusion six-helix bundle (6HB) similar to the post-fusion hPIV3 F structure. Electrostatic and temperature factor analysis of the F structures points to regions of these proteins that may be functionally important in their membrane fusion activity.
AuthorsKurt Swanson, Xiaolin Wen, George P Leser, Reay G Paterson, Robert A Lamb, Theodore S Jardetzky
JournalVirology (Virology) Vol. 402 Issue 2 Pg. 372-9 (Jul 05 2010) ISSN: 1096-0341 [Electronic] United States
PMID20439109 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)
CopyrightCopyright 2010 Elsevier Inc. All rights reserved.
Chemical References
  • Viral Fusion Proteins
Topics
  • Crystallography, X-Ray
  • Microscopy, Electron
  • Models, Molecular
  • Newcastle disease virus (chemistry, ultrastructure)
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Tertiary
  • Viral Fusion Proteins (chemistry, metabolism, ultrastructure)

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