Ontology highlight
ABSTRACT:
SUBMITTER: Follis KE
PROVIDER: S-EPMC7111819 | biostudies-literature | 2005 Oct
REPOSITORIES: biostudies-literature
Follis Kathryn E KE York Joanne J Nunberg Jack H JH
Virology 20051001 1
The fusion subunit of the SARS-CoV S glycoprotein contains two regions of hydrophobic heptad-repeat amino acid sequences that have been shown in biophysical studies to form a six-helix bundle structure typical of the fusion-active core found in Class I viral fusion proteins. Here, we have applied serine-scanning mutagenesis to the C-terminal-most heptad-repeat region in the SARS-CoV S glycoprotein to investigate the functional role of this region in membrane fusion. We show that hydrophobic side ...[more]