Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein.
Identifieur interne : 002273 ( PubMed/Corpus ); précédent : 002272; suivant : 002274Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein.
Auteurs : Bruno Sainz ; Eric C. Mossel ; William R. Gallaher ; William C. Wimley ; C J Peters ; Russell B. Wilson ; Robert F. GarrySource :
- Virus research [ 0168-1702 ] ; 2006.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cell Line, Dose-Response Relationship, Drug, Hemagglutinins (chemistry), Hemagglutinins, Viral (chemistry), Membrane Glycoproteins (chemistry), Molecular Sequence Data, Murine hepatitis virus (chemistry), Peptides (chemical synthesis), Peptides (genetics), Peptides (pharmacology), Protein Subunits (chemical synthesis), Protein Subunits (genetics), Protein Subunits (pharmacology), SARS Virus (drug effects), SARS Virus (growth & development), SARS Virus (pathogenicity), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Plaque Assay, Virulence (drug effects).
- MESH :
- chemical , chemical synthesis : Peptides, Protein Subunits.
- chemical , chemistry : Hemagglutinins, Hemagglutinins, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- chemistry : Murine hepatitis virus.
- drug effects : SARS Virus, Virulence.
- chemical , genetics : Peptides, Protein Subunits.
- growth & development : SARS Virus.
- pathogenicity : SARS Virus.
- chemical , pharmacology : Peptides, Protein Subunits.
- Amino Acid Sequence, Animals, Cell Line, Dose-Response Relationship, Drug, Molecular Sequence Data, Spike Glycoprotein, Coronavirus, Viral Plaque Assay.
Abstract
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the cause of an atypical pneumonia that affected Asia, North America and Europe in 2002-2003. The viral spike (S) glycoprotein is responsible for mediating receptor binding and membrane fusion. Recent studies have proposed that the carboxyl terminal portion (S2 subunit) of the S protein is a class I viral fusion protein. The Wimley and White interfacial hydrophobicity scale was used to identify regions within the CoV S2 subunit that may preferentially associate with lipid membranes with the premise that peptides analogous to these regions may function as inhibitors of viral infectivity. Five regions of high interfacial hydrophobicity spanning the length of the S2 subunit of SARS-CoV and murine hepatitis virus (MHV) were identified. Peptides analogous to regions of the N-terminus or the pre-transmembrane domain of the S2 subunit inhibited SARS-CoV plaque formation by 40-70% at concentrations of 15-30 microM. Interestingly, peptides analogous to the SARS-CoV or MHV loop region inhibited viral plaque formation by >80% at similar concentrations. The observed effects were dose-dependent (IC50 values of 2-4 microM) and not a result of peptide-mediated cell cytotoxicity. The antiviral activity of the CoV peptides tested provides an attractive basis for the development of new fusion peptide inhibitors corresponding to regions outside the fusion protein heptad repeat regions.
DOI: 10.1016/j.virusres.2006.03.001
PubMed: 16616792
Links to Exploration step
pubmed:16616792Le document en format XML
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Wimley</name></author><author><name sortKey="Peters, C J" sort="Peters, C J" uniqKey="Peters C" first="C J" last="Peters">C J Peters</name></author><author><name sortKey="Wilson, Russell B" sort="Wilson, Russell B" uniqKey="Wilson R" first="Russell B" last="Wilson">Russell B. Wilson</name></author><author><name sortKey="Garry, Robert F" sort="Garry, Robert F" uniqKey="Garry R" first="Robert F" last="Garry">Robert F. 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Mossel</name></author><author><name sortKey="Gallaher, William R" sort="Gallaher, William R" uniqKey="Gallaher W" first="William R" last="Gallaher">William R. Gallaher</name></author><author><name sortKey="Wimley, William C" sort="Wimley, William C" uniqKey="Wimley W" first="William C" last="Wimley">William C. Wimley</name></author><author><name sortKey="Peters, C J" sort="Peters, C J" uniqKey="Peters C" first="C J" last="Peters">C J Peters</name></author><author><name sortKey="Wilson, Russell B" sort="Wilson, Russell B" uniqKey="Wilson R" first="Russell B" last="Wilson">Russell B. Wilson</name></author><author><name sortKey="Garry, Robert F" sort="Garry, Robert F" uniqKey="Garry R" first="Robert F" last="Garry">Robert F. Garry</name></author></analytic><series><title level="j">Virus research</title><idno type="ISSN">0168-1702</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Dose-Response Relationship, Drug</term><term>Hemagglutinins (chemistry)</term><term>Hemagglutinins, Viral (chemistry)</term><term>Membrane Glycoproteins (chemistry)</term><term>Molecular Sequence Data</term><term>Murine hepatitis virus (chemistry)</term><term>Peptides (chemical synthesis)</term><term>Peptides (genetics)</term><term>Peptides (pharmacology)</term><term>Protein Subunits (chemical synthesis)</term><term>Protein Subunits (genetics)</term><term>Protein Subunits (pharmacology)</term><term>SARS Virus (drug effects)</term><term>SARS Virus (growth & development)</term><term>SARS Virus (pathogenicity)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Plaque Assay</term><term>Virulence (drug effects)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Peptides</term><term>Protein Subunits</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Hemagglutinins</term><term>Hemagglutinins, Viral</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>SARS Virus</term><term>Virulence</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peptides</term><term>Protein Subunits</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Peptides</term><term>Protein Subunits</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Dose-Response Relationship, Drug</term><term>Molecular Sequence Data</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Plaque Assay</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the cause of an atypical pneumonia that affected Asia, North America and Europe in 2002-2003. The viral spike (S) glycoprotein is responsible for mediating receptor binding and membrane fusion. Recent studies have proposed that the carboxyl terminal portion (S2 subunit) of the S protein is a class I viral fusion protein. The Wimley and White interfacial hydrophobicity scale was used to identify regions within the CoV S2 subunit that may preferentially associate with lipid membranes with the premise that peptides analogous to these regions may function as inhibitors of viral infectivity. Five regions of high interfacial hydrophobicity spanning the length of the S2 subunit of SARS-CoV and murine hepatitis virus (MHV) were identified. Peptides analogous to regions of the N-terminus or the pre-transmembrane domain of the S2 subunit inhibited SARS-CoV plaque formation by 40-70% at concentrations of 15-30 microM. Interestingly, peptides analogous to the SARS-CoV or MHV loop region inhibited viral plaque formation by >80% at similar concentrations. The observed effects were dose-dependent (IC50 values of 2-4 microM) and not a result of peptide-mediated cell cytotoxicity. The antiviral activity of the CoV peptides tested provides an attractive basis for the development of new fusion peptide inhibitors corresponding to regions outside the fusion protein heptad repeat regions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16616792</PMID><DateCompleted><Year>2006</Year><Month>09</Month><Day>07</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0168-1702</ISSN><JournalIssue CitedMedium="Print"><Volume>120</Volume><Issue>1-2</Issue><PubDate><Year>2006</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Virus research</Title><ISOAbbreviation>Virus Res.</ISOAbbreviation></Journal><ArticleTitle>Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein.</ArticleTitle><Pagination><MedlinePgn>146-55</MedlinePgn></Pagination><Abstract><AbstractText>Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the cause of an atypical pneumonia that affected Asia, North America and Europe in 2002-2003. The viral spike (S) glycoprotein is responsible for mediating receptor binding and membrane fusion. Recent studies have proposed that the carboxyl terminal portion (S2 subunit) of the S protein is a class I viral fusion protein. The Wimley and White interfacial hydrophobicity scale was used to identify regions within the CoV S2 subunit that may preferentially associate with lipid membranes with the premise that peptides analogous to these regions may function as inhibitors of viral infectivity. Five regions of high interfacial hydrophobicity spanning the length of the S2 subunit of SARS-CoV and murine hepatitis virus (MHV) were identified. Peptides analogous to regions of the N-terminus or the pre-transmembrane domain of the S2 subunit inhibited SARS-CoV plaque formation by 40-70% at concentrations of 15-30 microM. Interestingly, peptides analogous to the SARS-CoV or MHV loop region inhibited viral plaque formation by >80% at similar concentrations. The observed effects were dose-dependent (IC50 values of 2-4 microM) and not a result of peptide-mediated cell cytotoxicity. The antiviral activity of the CoV peptides tested provides an attractive basis for the development of new fusion peptide inhibitors corresponding to regions outside the fusion protein heptad repeat regions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sainz</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><Suffix>Jr</Suffix><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Tulane University Health Sciences Center, New Orleans, LA 70112, USA. bsainz@scripps.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mossel</LastName><ForeName>Eric C</ForeName><Initials>EC</Initials></Author><Author ValidYN="Y"><LastName>Gallaher</LastName><ForeName>William R</ForeName><Initials>WR</Initials></Author><Author ValidYN="Y"><LastName>Wimley</LastName><ForeName>William C</ForeName><Initials>WC</Initials></Author><Author ValidYN="Y"><LastName>Peters</LastName><ForeName>C J</ForeName><Initials>CJ</Initials></Author><Author ValidYN="Y"><LastName>Wilson</LastName><ForeName>Russell B</ForeName><Initials>RB</Initials></Author><Author ValidYN="Y"><LastName>Garry</LastName><ForeName>Robert F</ForeName><Initials>RF</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>N01 AI 25489</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>CA 08921</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI 007536</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32 AI007536</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>RR 018229</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 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