Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2.
Identifieur interne : 002820 ( PubMed/Curation ); précédent : 002819; suivant : 002821Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2.
Auteurs : Wenhui Li [États-Unis] ; Chengsheng Zhang ; Jianhua Sui ; Jens H. Kuhn ; Michael J. Moore ; Shiwen Luo ; Swee-Kee Wong ; I-Chueh Huang ; Keming Xu ; Natalya Vasilieva ; Akikazu Murakami ; Yaqing He ; Wayne A. Marasco ; Yi Guan ; Hyeryun Choe ; Michael FarzanSource :
- The EMBO journal [ 0261-4189 ] ; 2005.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Carboxypeptidases (), Carboxypeptidases (génétique), Carboxypeptidases (métabolisme), Domaine catalytique, Données de séquences moléculaires, Flambées de maladies, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Liaison aux protéines, Modèles moléculaires, Peptidyl-Dipeptidase A, Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines de l'enveloppe virale (métabolisme), Rats, Sites de fixation, Structure tertiaire des protéines, Syndrome respiratoire aigu sévère (virologie), Syndrome respiratoire aigu sévère (épidémiologie), Séquence d'acides aminés, Virus du SRAS (métabolisme), Viverridae (virologie).
- MESH :
- génétique : Carboxypeptidases, Protéines de fusion recombinantes.
- métabolisme : Carboxypeptidases, Glycoprotéines membranaires, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Virus du SRAS.
- virologie : Syndrome respiratoire aigu sévère, Viverridae.
- épidémiologie : Syndrome respiratoire aigu sévère.
- Alignement de séquences, Animaux, Carboxypeptidases, Domaine catalytique, Données de séquences moléculaires, Flambées de maladies, Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Modèles moléculaires, Peptidyl-Dipeptidase A, Rats, Sites de fixation, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Binding Sites, Carboxypeptidases (chemistry), Carboxypeptidases (genetics), Carboxypeptidases (metabolism), Catalytic Domain, Disease Outbreaks, Humans, Membrane Glycoproteins (metabolism), Models, Molecular, Molecular Sequence Data, Peptidyl-Dipeptidase A, Protein Binding, Protein Structure, Tertiary, Rats, Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (metabolism), Sequence Alignment, Severe Acute Respiratory Syndrome (epidemiology), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism), Viverridae (virology).
- MESH :
- chemical , chemistry : Carboxypeptidases.
- chemical , genetics : Carboxypeptidases, Recombinant Fusion Proteins.
- chemical , metabolism : Carboxypeptidases, Membrane Glycoproteins, Recombinant Fusion Proteins, Viral Envelope Proteins.
- epidemiology : Severe Acute Respiratory Syndrome.
- metabolism : SARS Virus.
- virology : Severe Acute Respiratory Syndrome, Viverridae.
- Amino Acid Sequence, Animals, Binding Sites, Catalytic Domain, Disease Outbreaks, Humans, Models, Molecular, Molecular Sequence Data, Peptidyl-Dipeptidase A, Protein Binding, Protein Structure, Tertiary, Rats, Sequence Alignment, Spike Glycoprotein, Coronavirus.
Abstract
Human angiotensin-converting enzyme 2 (ACE2) is a functional receptor for SARS coronavirus (SARS-CoV). Here we identify the SARS-CoV spike (S)-protein-binding site on ACE2. We also compare S proteins of SARS-CoV isolated during the 2002-2003 SARS outbreak and during the much less severe 2003-2004 outbreak, and from palm civets, a possible source of SARS-CoV found in humans. All three S proteins bound to and utilized palm-civet ACE2 efficiently, but the latter two S proteins utilized human ACE2 markedly less efficiently than did the S protein obtained during the earlier human outbreak. The lower affinity of these S proteins could be complemented by altering specific residues within the S-protein-binding site of human ACE2 to those of civet ACE2, or by altering S-protein residues 479 and 487 to residues conserved during the 2002-2003 outbreak. Collectively, these data describe molecular interactions important to the adaptation of SARS-CoV to human cells, and provide insight into the severity of the 2002-2003 SARS epidemic.
DOI: 10.1038/sj.emboj.7600640
PubMed: 15791205
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pubmed:15791205Le document en format XML
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(metabolism)</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptidyl-Dipeptidase A</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Rats</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>SARS Virus (metabolism)</term><term>Sequence Alignment</term><term>Severe Acute Respiratory Syndrome (epidemiology)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (metabolism)</term><term>Viverridae (virology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Carboxypeptidases ()</term><term>Carboxypeptidases (génétique)</term><term>Carboxypeptidases (métabolisme)</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Flambées de maladies</term><term>Glycoprotéine de spicule des 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scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxypeptidases</term><term>Membrane Glycoproteins</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="epidemiology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Carboxypeptidases</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carboxypeptidases</term><term>Glycoprotéines membranaires</term><term>Protéines de fusion recombinantes</term><term>Protéines de l'enveloppe virale</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term><term>Viverridae</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term><term>Viverridae</term></keywords><keywords scheme="MESH" qualifier="épidémiologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Catalytic Domain</term><term>Disease Outbreaks</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptidyl-Dipeptidase A</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Rats</term><term>Sequence Alignment</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Carboxypeptidases</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Flambées de maladies</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Peptidyl-Dipeptidase A</term><term>Rats</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Human angiotensin-converting enzyme 2 (ACE2) is a functional receptor for SARS coronavirus (SARS-CoV). Here we identify the SARS-CoV spike (S)-protein-binding site on ACE2. We also compare S proteins of SARS-CoV isolated during the 2002-2003 SARS outbreak and during the much less severe 2003-2004 outbreak, and from palm civets, a possible source of SARS-CoV found in humans. All three S proteins bound to and utilized palm-civet ACE2 efficiently, but the latter two S proteins utilized human ACE2 markedly less efficiently than did the S protein obtained during the earlier human outbreak. The lower affinity of these S proteins could be complemented by altering specific residues within the S-protein-binding site of human ACE2 to those of civet ACE2, or by altering S-protein residues 479 and 487 to residues conserved during the 2002-2003 outbreak. Collectively, these data describe molecular interactions important to the adaptation of SARS-CoV to human cells, and provide insight into the severity of the 2002-2003 SARS epidemic.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15791205</PMID><DateCompleted><Year>2005</Year><Month>07</Month><Day>12</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0261-4189</ISSN><JournalIssue CitedMedium="Print"><Volume>24</Volume><Issue>8</Issue><PubDate><Year>2005</Year><Month>Apr</Month><Day>20</Day></PubDate></JournalIssue><Title>The EMBO journal</Title><ISOAbbreviation>EMBO J.</ISOAbbreviation></Journal><ArticleTitle>Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2.</ArticleTitle><Pagination><MedlinePgn>1634-43</MedlinePgn></Pagination><Abstract><AbstractText>Human angiotensin-converting enzyme 2 (ACE2) is a functional receptor for SARS coronavirus (SARS-CoV). Here we identify the SARS-CoV spike (S)-protein-binding site on ACE2. We also compare S proteins of SARS-CoV isolated during the 2002-2003 SARS outbreak and during the much less severe 2003-2004 outbreak, and from palm civets, a possible source of SARS-CoV found in humans. All three S proteins bound to and utilized palm-civet ACE2 efficiently, but the latter two S proteins utilized human ACE2 markedly less efficiently than did the S protein obtained during the earlier human outbreak. The lower affinity of these S proteins could be complemented by altering specific residues within the S-protein-binding site of human ACE2 to those of civet ACE2, or by altering S-protein residues 479 and 487 to residues conserved during the 2002-2003 outbreak. Collectively, these data describe molecular interactions important to the adaptation of SARS-CoV to human cells, and provide insight into the severity of the 2002-2003 SARS epidemic.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Wenhui</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Molecular Genetics, Harvard Medical School, New England Primate Research Center, Southborough, MA 01772-9102, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Chengsheng</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Sui</LastName><ForeName>Jianhua</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Kuhn</LastName><ForeName>Jens H</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Moore</LastName><ForeName>Michael J</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Luo</LastName><ForeName>Shiwen</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Wong</LastName><ForeName>Swee-Kee</ForeName><Initials>SK</Initials></Author><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>I-Chueh</ForeName><Initials>IC</Initials></Author><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Keming</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Vasilieva</LastName><ForeName>Natalya</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Murakami</LastName><ForeName>Akikazu</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>He</LastName><ForeName>Yaqing</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Marasco</LastName><ForeName>Wayne A</ForeName><Initials>WA</Initials></Author><Author ValidYN="Y"><LastName>Guan</LastName><ForeName>Yi</ForeName><Initials>Y</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><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI043891</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>03</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>EMBO J</MedlineTA><NlmUniqueID>8208664</NlmUniqueID><ISSNLinking>0261-4189</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D002268">Carboxypeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.15.1</RegistryNumber><NameOfSubstance UI="D007703">Peptidyl-Dipeptidase A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.17.-</RegistryNumber><NameOfSubstance UI="C413524">angiotensin converting enzyme 2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002268" MajorTopicYN="N">Carboxypeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004196" MajorTopicYN="N">Disease Outbreaks</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007703" MajorTopicYN="N">Peptidyl-Dipeptidase A</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion 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