Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-Å resolution

Ebola virions contain a surface transmembrane glycoprotein (GP) that is responsible for binding to target cells and subsequent fusion of the viral and host-cell membranes. GP is expressed as a single-chain precursor that is posttranslationally processed into the disulfide-linked fragments GP1 and GP...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1999-03, Vol.96 (6), p.2662-2667
Main Authors: Malashkevich, V N, Schneider, B J, McNally, M L, Milhollen, M A, Pang, J X, Kim, P S
Format: Article
Language:English
Subjects:
ADVANCED LIGHT SOURCE
ADVANCED LIGHT SOURCE ALS
Amino Acid Sequence
Biological Sciences
Cellular biology
Crystallography, X-Ray
Ebolavirus - chemistry
GLYCOPROTEINS
Molecular Sequence Data
PARTICLE ACCELERATORS
Protein Folding
Proteins
RESOLUTION
Ribonucleic acid
RNA
Viral Envelope Proteins - chemistry
Viruses
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Summary:Ebola virions contain a surface transmembrane glycoprotein (GP) that is responsible for binding to target cells and subsequent fusion of the viral and host-cell membranes. GP is expressed as a single-chain precursor that is posttranslationally processed into the disulfide-linked fragments GP1 and GP2. The GP2 subunit is thought to mediate membrane fusion. A soluble fragment of the GP2 ectodomain, lacking the fusion-peptide region and the transmembrane helix, folds into a stable, highly helical structure in aqueous solution. Limited proteolysis studies identify a stable core of the GP2 ectodomain. This 74-residue core, denoted Ebo-74, was crystallized, and its x-ray structure was determined at 1.9-Å resolution. Ebo-74 forms a trimer in which a long, central three-stranded coiled coil is surrounded by shorter C-terminal helices that are packed in an antiparallel orientation into hydrophobic grooves on the surface of the coiled coil. Our results confirm the previously anticipated structural similarity between the Ebola GP2 ectodomain and the core of the transmembrane subunit from oncogenic retroviruses. The Ebo-74 structure likely represents the fusion-active conformation of the protein, and its overall architecture resembles several other viral membrane-fusion proteins, including those from HIV and influenza. x-ray crystallography membrane fusion filovirus oncogenic retroviruses
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.96.6.2662