Crystal structure of glycoprotein B from herpes simplex virus 1.

نویسندگان

  • Ekaterina E Heldwein
  • Huan Lou
  • Florent C Bender
  • Gary H Cohen
  • Roselyn J Eisenberg
  • Stephen C Harrison
چکیده

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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عنوان ژورنال:
  • Science

دوره 313 5784  شماره 

صفحات  -

تاریخ انتشار 2006