Serine-scanning mutagenesis studies of the C-terminal heptad repeats in the SARS coronavirus S glycoprotein highlight the important role of the short helical region.
Identifieur interne : 002607 ( PubMed/Corpus ); précédent : 002606; suivant : 002608Serine-scanning mutagenesis studies of the C-terminal heptad repeats in the SARS coronavirus S glycoprotein highlight the important role of the short helical region.
Auteurs : Kathryn E. Follis ; Joanne York ; Jack H. NunbergSource :
- Virology [ 0042-6822 ] ; 2005.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, COS Cells, Chlorocebus aethiops, Membrane Fusion (genetics), Membrane Fusion (physiology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (physiology), Models, Molecular, Molecular Sequence Data, Mutagenesis, Protein Structure, Secondary, Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Repetitive Sequences, Amino Acid, SARS Virus (genetics), SARS Virus (pathogenicity), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Transfection, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (physiology).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- genetics : Membrane Fusion, Membrane Glycoproteins, Recombinant Proteins, SARS Virus, Viral Envelope Proteins.
- pathogenicity : SARS Virus.
- physiology : Membrane Fusion, Membrane Glycoproteins, SARS Virus, Viral Envelope Proteins.
- Amino Acid Sequence, Animals, COS Cells, Chlorocebus aethiops, Models, Molecular, Molecular Sequence Data, Mutagenesis, Protein Structure, Secondary, Repetitive Sequences, Amino Acid, Spike Glycoprotein, Coronavirus, Transfection.
Abstract
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 sidechains at a and d positions only within the short helical segment of the C-terminal heptad-repeat region (I1161, I1165, L1168, A1172, and L1175) are critical for cell-cell fusion. Serine mutations at outlying heptad-repeat residues that form an extended chain in the core structure (V1158, L1179, and L1182) do not affect fusogenicity. Our study provides genetic evidence for the important role of alpha-helical packing in promoting S glycoprotein-mediated membrane fusion.
DOI: 10.1016/j.virol.2005.07.005
PubMed: 16081124
Links to Exploration step
pubmed:16081124Le document en format XML
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Nunberg</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:16081124</idno><idno type="pmid">16081124</idno><idno type="doi">10.1016/j.virol.2005.07.005</idno><idno type="wicri:Area/PubMed/Corpus">002607</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002607</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Serine-scanning mutagenesis studies of the C-terminal heptad repeats in the SARS coronavirus S glycoprotein highlight the important role of the short helical region.</title><author><name sortKey="Follis, Kathryn E" sort="Follis, Kathryn E" uniqKey="Follis K" first="Kathryn E" last="Follis">Kathryn E. Follis</name><affiliation><nlm:affiliation>Montana Biotechnology Center, The University of Montana, Science Complex Room 221, Missoula, MT 59812, USA.</nlm:affiliation></affiliation></author><author><name sortKey="York, Joanne" sort="York, Joanne" uniqKey="York J" first="Joanne" last="York">Joanne York</name></author><author><name sortKey="Nunberg, Jack H" sort="Nunberg, Jack H" uniqKey="Nunberg J" first="Jack H" last="Nunberg">Jack H. 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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 sidechains at a and d positions only within the short helical segment of the C-terminal heptad-repeat region (I1161, I1165, L1168, A1172, and L1175) are critical for cell-cell fusion. Serine mutations at outlying heptad-repeat residues that form an extended chain in the core structure (V1158, L1179, and L1182) do not affect fusogenicity. Our study provides genetic evidence for the important role of alpha-helical packing in promoting S glycoprotein-mediated membrane fusion.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16081124</PMID><DateCompleted><Year>2005</Year><Month>11</Month><Day>08</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0042-6822</ISSN><JournalIssue CitedMedium="Print"><Volume>341</Volume><Issue>1</Issue><PubDate><Year>2005</Year><Month>Oct</Month><Day>10</Day></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>Serine-scanning mutagenesis studies of the C-terminal heptad repeats in the SARS coronavirus S glycoprotein highlight the important role of the short helical region.</ArticleTitle><Pagination><MedlinePgn>122-9</MedlinePgn></Pagination><Abstract><AbstractText>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 sidechains at a and d positions only within the short helical segment of the C-terminal heptad-repeat region (I1161, I1165, L1168, A1172, and L1175) are critical for cell-cell fusion. Serine mutations at outlying heptad-repeat residues that form an extended chain in the core structure (V1158, L1179, and L1182) do not affect fusogenicity. Our study provides genetic evidence for the important role of alpha-helical packing in promoting S glycoprotein-mediated membrane fusion.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Follis</LastName><ForeName>Kathryn E</ForeName><Initials>KE</Initials><AffiliationInfo><Affiliation>Montana Biotechnology Center, The University of Montana, Science Complex Room 221, Missoula, MT 59812, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>York</LastName><ForeName>Joanne</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Nunberg</LastName><ForeName>Jack H</ForeName><Initials>JH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United 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