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Science 14 July 2006:
Vol. 313. no. 5784, pp. 217 - 220
DOI: 10.1126/science.1126548
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Reports

Crystal Structure of Glycoprotein B from Herpes Simplex Virus 1

Ekaterina E. Heldwein,1,2* Huan Lou,4 Florent C. Bender,4 Gary H. Cohen,4 Roselyn J. Eisenberg,5 Stephen C. Harrison1,2,3

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 ß 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.

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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Science. ISSN 0036-8075 (print), 1095-9203 (online)