Crystal structure of glycoprotein B from herpes simplex virus 1 |
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| Authors: | Heldwein Ekaterina E Lou Huan Bender Florent C Cohen Gary H Eisenberg Roselyn J Harrison Stephen C |
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| Institution: | Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, USA. heldwein@crystal.harvard.edu |
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| 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. |
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