Abstract
Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An alpha-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended beta hairpins with hydrophobic tips, homologous to fusion peptides in VSV G, relate gB to class II fusion proteins. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. The domain connectivity within a gB monomer would permit such a rearrangement, including long-range translocations linked to viral and cellular membranes.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Crystallization
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Crystallography, X-Ray
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Epitopes
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Evolution, Molecular
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Herpesvirus 1, Human / chemistry*
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Hydrogen-Ion Concentration
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Hydrophobic and Hydrophilic Interactions
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / physiology
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Models, Molecular
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Molecular Sequence Data
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Subunits / chemistry
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Vesicular stomatitis Indiana virus / chemistry
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Viral Envelope Proteins / chemistry*
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Viral Envelope Proteins / immunology
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Viral Envelope Proteins / physiology
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Viral Fusion Proteins / chemistry*
Substances
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Epitopes
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G protein, vesicular stomatitis virus
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Membrane Glycoproteins
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Protein Subunits
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Viral Envelope Proteins
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Viral Fusion Proteins
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glycoprotein B, Simplexvirus