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.
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Authors | Kurt Swanson, Xiaolin Wen, George P Leser, Reay G Paterson, Robert A Lamb, Theodore S Jardetzky |
Journal | Virology
(Virology)
Vol. 402
Issue 2
Pg. 372-9
(Jul 05 2010)
ISSN: 1096-0341 [Electronic] United States |
PMID | 20439109
(Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)
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Copyright | Copyright 2010 Elsevier Inc. All rights reserved. |
Chemical References |
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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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