Crystal Structure of Glycoprotein B from Herpes Simplex Virus 1
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 α-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended β 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:
-
Science
- Pub Date:
- July 2006
- DOI:
- 10.1126/science.1126548
- Bibcode:
- 2006Sci...313..217H
- Keywords:
-
- BIOCHEM