Severe acute respiratory syndrome coronavirus entry as a target of antiviral therapies.
Identifieur interne : 001C98 ( PubMed/Corpus ); précédent : 001C97; suivant : 001C99Severe acute respiratory syndrome coronavirus entry as a target of antiviral therapies.
Auteurs : Jens H. Kuhn ; Wenhui Li ; Sheli R. Radoshitzky ; Hyeryun Choe ; Michael FarzanSource :
- Antiviral therapy [ 1359-6535 ] ; 2007.
English descriptors
- KwdEn :
- Animals, Antiviral Agents (pharmacology), Antiviral Agents (therapeutic use), Cats, Cattle, Dogs, Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (drug effects), Membrane Glycoproteins (metabolism), Models, Molecular, Peptidyl-Dipeptidase A (drug effects), Peptidyl-Dipeptidase A (metabolism), Rabbits, Rats, Receptors, Virus (drug effects), Receptors, Virus (metabolism), SARS Virus (drug effects), SARS Virus (pathogenicity), Severe Acute Respiratory Syndrome (drug therapy), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (drug effects), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , drug effects : Membrane Glycoproteins, Peptidyl-Dipeptidase A, Receptors, Virus, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Peptidyl-Dipeptidase A, Receptors, Virus, Viral Envelope Proteins.
- chemical , pharmacology : Antiviral Agents.
- chemical , therapeutic use : Antiviral Agents.
- drug effects : SARS Virus.
- drug therapy : Severe Acute Respiratory Syndrome.
- pathogenicity : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Animals, Cats, Cattle, Dogs, Humans, Models, Molecular, Rabbits, Rats, Spike Glycoprotein, Coronavirus.
Abstract
The identification in 2003 of a coronavirus as the aetiological agent of severe acute respiratory syndrome (SARS) intensified efforts to understand the biology of coronaviruses in general and SARS coronavirus (SARS-CoV) in particular. Rapid progress was made in describing the SARS-CoV genome, evolution and lifecycle. Identification of angiotensin-converting enzyme 2 (ACE2) as an obligate cellular receptor for SARS-CoV contributed to understanding of the SARS-CoV entry process, and helped to characterize two targets of antiviral therapeutics: the SARS-CoV spike protein and ACE2. Here we describe the role of these proteins in SARS-CoV replication and potential therapeutic strategies aimed at preventing entry of SARS-CoV into target cells.
PubMed: 17944271
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Radoshitzky</name></author><author><name sortKey="Choe, Hyeryun" sort="Choe, Hyeryun" uniqKey="Choe H" first="Hyeryun" last="Choe">Hyeryun Choe</name></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17944271</idno><idno type="pmid">17944271</idno><idno type="wicri:Area/PubMed/Corpus">001C98</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001C98</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Severe acute respiratory syndrome coronavirus entry as a target of antiviral therapies.</title><author><name sortKey="Kuhn, Jens H" sort="Kuhn, Jens H" uniqKey="Kuhn J" first="Jens H" last="Kuhn">Jens H. Kuhn</name><affiliation><nlm:affiliation>Department of Microbiology and Molecular Genetics, Harvard Medical School, New England Primate Research Center, Southborough, MA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Wenhui" sort="Li, Wenhui" uniqKey="Li W" first="Wenhui" last="Li">Wenhui Li</name></author><author><name sortKey="Radoshitzky, Sheli R" sort="Radoshitzky, Sheli R" uniqKey="Radoshitzky S" first="Sheli R" last="Radoshitzky">Sheli R. Radoshitzky</name></author><author><name sortKey="Choe, Hyeryun" sort="Choe, Hyeryun" uniqKey="Choe H" first="Hyeryun" last="Choe">Hyeryun Choe</name></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name></author></analytic><series><title level="j">Antiviral therapy</title><idno type="ISSN">1359-6535</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antiviral Agents (pharmacology)</term><term>Antiviral Agents (therapeutic use)</term><term>Cats</term><term>Cattle</term><term>Dogs</term><term>Humans</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (drug effects)</term><term>Membrane Glycoproteins (metabolism)</term><term>Models, Molecular</term><term>Peptidyl-Dipeptidase A (drug effects)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Rabbits</term><term>Rats</term><term>Receptors, Virus (drug effects)</term><term>Receptors, Virus (metabolism)</term><term>SARS Virus (drug effects)</term><term>SARS Virus (pathogenicity)</term><term>Severe Acute Respiratory Syndrome (drug therapy)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (drug effects)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term></keywords><keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Antiviral Agents</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cats</term><term>Cattle</term><term>Dogs</term><term>Humans</term><term>Models, Molecular</term><term>Rabbits</term><term>Rats</term><term>Spike Glycoprotein, Coronavirus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The identification in 2003 of a coronavirus as the aetiological agent of severe acute respiratory syndrome (SARS) intensified efforts to understand the biology of coronaviruses in general and SARS coronavirus (SARS-CoV) in particular. Rapid progress was made in describing the SARS-CoV genome, evolution and lifecycle. Identification of angiotensin-converting enzyme 2 (ACE2) as an obligate cellular receptor for SARS-CoV contributed to understanding of the SARS-CoV entry process, and helped to characterize two targets of antiviral therapeutics: the SARS-CoV spike protein and ACE2. Here we describe the role of these proteins in SARS-CoV replication and potential therapeutic strategies aimed at preventing entry of SARS-CoV into target cells.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17944271</PMID><DateCompleted><Year>2007</Year><Month>11</Month><Day>01</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1359-6535</ISSN><JournalIssue CitedMedium="Print"><Volume>12</Volume><Issue>4 Pt B</Issue><PubDate><Year>2007</Year></PubDate></JournalIssue><Title>Antiviral therapy</Title><ISOAbbreviation>Antivir. Ther. (Lond.)</ISOAbbreviation></Journal><ArticleTitle>Severe acute respiratory syndrome coronavirus entry as a target of antiviral therapies.</ArticleTitle><Pagination><MedlinePgn>639-50</MedlinePgn></Pagination><Abstract><AbstractText>The identification in 2003 of a coronavirus as the aetiological agent of severe acute respiratory syndrome (SARS) intensified efforts to understand the biology of coronaviruses in general and SARS coronavirus (SARS-CoV) in particular. Rapid progress was made in describing the SARS-CoV genome, evolution and lifecycle. Identification of angiotensin-converting enzyme 2 (ACE2) as an obligate cellular receptor for SARS-CoV contributed to understanding of the SARS-CoV entry process, and helped to characterize two targets of antiviral therapeutics: the SARS-CoV spike protein and ACE2. Here we describe the role of these proteins in SARS-CoV replication and potential therapeutic strategies aimed at preventing entry of SARS-CoV into target cells.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kuhn</LastName><ForeName>Jens H</ForeName><Initials>JH</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Molecular Genetics, Harvard Medical School, New England Primate Research Center, Southborough, MA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Wenhui</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Radoshitzky</LastName><ForeName>Sheli R</ForeName><Initials>SR</Initials></Author><Author ValidYN="Y"><LastName>Choe</LastName><ForeName>Hyeryun</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Farzan</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Antivir Ther</MedlineTA><NlmUniqueID>9815705</NlmUniqueID><ISSNLinking>1359-6535</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011991">Receptors, Virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, 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UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>163</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>10</Month><Day>20</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>11</Month><Day>2</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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