The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil.

Abstract

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 alpha-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.

• Authors: W Weissenhorn, L J Calder, S A Wharton, J J Skehel, D C Wiley
• Journal: Proceedings of the National Academy of Sciences of the United States of America (Proc Natl Acad Sci U S A) Vol. 95 Issue 11 Pg. 6032-6 (May 26 1998) ISSN: 0027-8424 [Print] United States
• PMID: 9600912 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Glycoproteins
• Recombinant Fusion Proteins
• Viral Envelope Proteins

Topics

• Amino Acid Sequence
• Cell Membrane (metabolism)
• Ebolavirus (chemistry, metabolism)
• Glycoproteins (chemistry, genetics, metabolism)
• Molecular Sequence Data
• Protein Conformation
• Recombinant Fusion Proteins (chemistry, genetics, metabolism)
• Sequence Analysis
• Viral Envelope Proteins (chemistry, genetics, metabolism)