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PMID: 9600912 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Weissenhorn W, Calder LJ, Wharton SA, Skehel JJ, Wiley DC

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.

MeSH Terms
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
Chemicals
Glycoproteins Recombinant Fusion Proteins Viral Envelope Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Weissenhorn W
Laboratory of Molecular Medicine, Howard Hughes Medical Institute, The Children's Hospital, 320 Longwood Avenue Boston, MA 02215, USA.
Calder L J
Wharton S A
Skehel J J
Wiley D C
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1998-05-26
Pages
6032-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC27580
Subset
IM
Grants
NIAID NIH HHS · 5RO1AI13654-20 · United States
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