The Central Structural Feature of the Membrane Fusion Protein Subunit from the Ebola Virus Glycoprotein is a Long Triple-Stranded Coiled Coil

The ectodomain of the Ebola virus Gp2 glycoprotein was solubilized with a trimeric, isoleucine zipper derived from GCN4 (pIIGCN4) in place of the hydrophobic fusion peptide at the N terminus. This chimeric molecule forms a trimeric, highly α -helical, and very thermostable molecule, as determined by...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1998-05, Vol.95 (11), p.6032-6036
Main Authors: Weissenhorn, Winfried, Calder, Lesley J., Wharton, Stephen A., Skehel, John J., Wiley, Don C.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biochemistry
Biological Sciences
Cell Membrane - metabolism
Crosslinking
Disulfides
Ebola virus
Ebolavirus - chemistry
Ebolavirus - metabolism
Electron micrographs
Glycoproteins - chemistry
Glycoproteins - genetics
Glycoproteins - metabolism
HIV 1
Membranes
Molecular Sequence Data
Molecules
Orthomyxoviridae
Protein Conformation
Proteins
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Sequence Analysis
Viral Envelope Proteins - chemistry
Viral Envelope Proteins - genetics
Viral Envelope Proteins - metabolism
Viral morphology
Virology
Viruses
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Summary:The ectodomain of the Ebola virus Gp2 glycoprotein was solubilized with a trimeric, isoleucine zipper derived from GCN4 (pIIGCN4) in place of the hydrophobic fusion peptide at the N terminus. This chimeric molecule forms a trimeric, highly α -helical, and very thermostable molecule, as determined by chemical crosslinking and circular dichroism. Electron microscopy indicates that Gp2 folds into a rod-like structure like influenza HA2 and HIV-1 gp41, providing further evidence that viral fusion proteins from diverse families such as Orthomyxoviridae (Influenza), Retroviridae (HIV-1), and Filoviridae (Ebola) share common structural features, and suggesting a common membrane fusion mechanism.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.95.11.6032