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Crystal Structure of Glycoprotein B from Herpes Simplex Virus 1
Ekaterina E. Heldwein,1,2*Huan Lou,4Florent C. Bender,4Gary H. Cohen,4Roselyn J. Eisenberg,5Stephen C. Harrison1,2,3
Glycoprotein B (gB) is the most conserved component of the complexcell-entry machinery of herpes viruses. A crystal structureof the gB ectodomain from herpes simplex virus type 1 revealsa multidomain trimer with unexpected homology to glycoproteinG from vesicular stomatitis virus (VSV G). An -helical coiled-coilcore relates gB to class I viral membrane fusion glycoproteins;two extended ß hairpins with hydrophobic tips, homologousto fusion peptides in VSV G, relate gB to class II fusion proteins.Members of both classes accomplish fusion through a large-scaleconformational change, triggered by a signal from a receptor-bindingcomponent. The domain connectivity within a gB monomer wouldpermit such a rearrangement, including long-range translocationslinked to viral and cellular membranes.
1 Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, USA. 2 Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA. 3 Howard Hughes Medical Institute, Children's Hospital, 320 Longwood Avenue, Boston, MA 02115, USA. 4 Department of Microbiology, School of Dental Medicine, University of Pennsylvania, 240 South 40th Street, Philadelphia, PA 19104, USA. 5 Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, 240 South 40th Street, Philadelphia, PA 19104, USA.
* To whom correspondence should be addressed. E-mail: heldwein{at}crystal.harvard.edu
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