Crystal structure of glycoprotein B from herpes simplex virus 1.

Publication Type:

Journal Article


Science, Volume 313, Issue 5784, p.217-20 (2006)


Amino Acid Sequence, Crystallization, Crystallography, X-Ray, Epitopes, Evolution, Molecular, Herpesvirus 1, Human, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits, Vesicular stomatitis Indiana virus, Viral Envelope Proteins, Viral Fusion Proteins


<p>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.</p>