Journal
SCIENCE
Volume 313, Issue 5784, Pages 217-220Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1126548
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Funding
- NIAID NIH HHS [AI056045, R21 AI065886, AI065886, AI049980] Funding Source: Medline
- NINDS NIH HHS [NS36731] Funding Source: Medline
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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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