Computational simulation of interactions between SARS coronavirus spike mutants and host species-specific receptors
Identifieur interne : 001904 ( Ncbi/Merge ); précédent : 001903; suivant : 001905Computational simulation of interactions between SARS coronavirus spike mutants and host species-specific receptors
Auteurs : Yuan Zhang [République populaire de Chine] ; Nan Zheng [Japon] ; Peng Nan [République populaire de Chine] ; Ying Cao [Japon] ; Masami Hasegawa [Japon] ; Yang Zhong [République populaire de Chine]Source :
- Computational Biology and Chemistry [ 1476-9271 ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux, Biologie informatique (), Chats, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Humains, Liaison aux protéines, Mutation, Peptidyl-Dipeptidase A (), Peptidyl-Dipeptidase A (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Rats, Récepteurs viraux (), Récepteurs viraux (métabolisme), Souris, Spécificité d'espèce, Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Récepteurs viraux, Virus du SRAS.
- Animaux, Biologie informatique, Chats, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Liaison aux protéines, Mutation, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Rats, Récepteurs viraux, Souris, Spécificité d'espèce.
English descriptors
- KwdEn :
- Animals, Cats, Computational Biology (methods), Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mice, Mutation, Peptidyl-Dipeptidase A (chemistry), Peptidyl-Dipeptidase A (metabolism), Protein Binding, Rats, Receptors, Virus (chemistry), Receptors, Virus (metabolism), SARS Virus (genetics), SARS Virus (metabolism), Species Specificity, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Peptidyl-Dipeptidase A, Receptors, Virus, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Peptidyl-Dipeptidase A, Receptors, Virus, Viral Envelope Proteins.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- methods : Computational Biology.
- Animals, Cats, Humans, Mice, Mutation, Protein Binding, Rats, Species Specificity, Spike Glycoprotein, Coronavirus.
Abstract
As a critical adaptive mechanism, amino acid replacements on the severe acute respiratory syndrome coronavirus (SARS-CoV) spike protein could alter the receptor-binding specificity of this envelope glycoprotein and in turn lead to the emergence or reemergence of this viral zoonosis. Based on the X-ray structures of SARS-CoV spike receptor-binding domain (RBD) in complex with its functional receptor (angiotensin-converting enzyme 2, ACE2), we perform computational simulations of interactions between three representative RBD mutants and four host species-specific receptors. The comparisons between computational predictions and experimental evidences validate our structural bioinformatics approaches. And the predictions further indicate that some viral prototypes might utilize the rat ACE2 while rats might serve as a vector or reservoir of SARS-CoV.
Url:
DOI: 10.1016/j.compbiolchem.2007.02.006
PubMed: 17368104
PubMed Central: 7106403
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PMC:7106403Le document en format XML
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<term>Membrane Glycoproteins (genetics)</term>
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<term>Mice</term>
<term>Mutation</term>
<term>Peptidyl-Dipeptidase A (chemistry)</term>
<term>Peptidyl-Dipeptidase A (metabolism)</term>
<term>Protein Binding</term>
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<term>Receptors, Virus (metabolism)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
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<front><div type="abstract" xml:lang="en"><p>As a critical adaptive mechanism, amino acid replacements on the severe acute respiratory syndrome coronavirus (SARS-CoV) spike protein could alter the receptor-binding specificity of this envelope glycoprotein and in turn lead to the emergence or reemergence of this viral zoonosis. Based on the X-ray structures of SARS-CoV spike receptor-binding domain (RBD) in complex with its functional receptor (angiotensin-converting enzyme 2, ACE2), we perform computational simulations of interactions between three representative RBD mutants and four host species-specific receptors. The comparisons between computational predictions and experimental evidences validate our structural bioinformatics approaches. And the predictions further indicate that some viral prototypes might utilize the rat ACE2 while rats might serve as a vector or reservoir of SARS-CoV.</p>
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<double pmid="17368104"><pmc><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Computational simulation of interactions between SARS coronavirus spike mutants and host species-specific receptors</title>
<author><name sortKey="Zhang, Yuan" sort="Zhang, Yuan" uniqKey="Zhang Y" first="Yuan" last="Zhang">Yuan Zhang</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">School of Life Sciences, Fudan University, Shanghai 200433, China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
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<author><name sortKey="Zheng, Nan" sort="Zheng, Nan" uniqKey="Zheng N" first="Nan" last="Zheng">Nan Zheng</name>
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<country xml:lang="fr">Japon</country>
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<author><name sortKey="Nan, Peng" sort="Nan, Peng" uniqKey="Nan P" first="Peng" last="Nan">Peng Nan</name>
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<country xml:lang="fr">République populaire de Chine</country>
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<author><name sortKey="Cao, Ying" sort="Cao, Ying" uniqKey="Cao Y" first="Ying" last="Cao">Ying Cao</name>
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<affiliation wicri:level="1"><nlm:aff id="aff4">Department of Biosystems Science, The Graduate University for Advanced Studies, Hayama, Kanagawa 240-0193, Japan</nlm:aff>
<country xml:lang="fr">Japon</country>
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<author><name sortKey="Hasegawa, Masami" sort="Hasegawa, Masami" uniqKey="Hasegawa M" first="Masami" last="Hasegawa">Masami Hasegawa</name>
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<affiliation wicri:level="1"><nlm:aff id="aff4">Department of Biosystems Science, The Graduate University for Advanced Studies, Hayama, Kanagawa 240-0193, Japan</nlm:aff>
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<wicri:regionArea>Department of Biosystems Science, The Graduate University for Advanced Studies, Hayama, Kanagawa 240-0193</wicri:regionArea>
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</author>
<author><name sortKey="Zhong, Yang" sort="Zhong, Yang" uniqKey="Zhong Y" first="Yang" last="Zhong">Yang Zhong</name>
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<wicri:noRegion>Shanghai 200433</wicri:noRegion>
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<affiliation wicri:level="1"><nlm:aff id="aff5">Shanghai Center for Bioinformation Technology, Shanghai 200235, China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Shanghai Center for Bioinformation Technology, Shanghai 200235</wicri:regionArea>
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<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7106403</idno>
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<idno type="doi">10.1016/j.compbiolchem.2007.02.006</idno>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Computational simulation of interactions between SARS coronavirus spike mutants and host species-specific receptors</title>
<author><name sortKey="Zhang, Yuan" sort="Zhang, Yuan" uniqKey="Zhang Y" first="Yuan" last="Zhang">Yuan Zhang</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">School of Life Sciences, Fudan University, Shanghai 200433, China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>School of Life Sciences, Fudan University, Shanghai 200433</wicri:regionArea>
<wicri:noRegion>Shanghai 200433</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Zheng, Nan" sort="Zheng, Nan" uniqKey="Zheng N" first="Nan" last="Zheng">Nan Zheng</name>
<affiliation wicri:level="1"><nlm:aff id="aff2">Division of Viral Immunology, Center for AIDS Research, Kumamoto University, 2-2-1 Honjo, Kumamoto 860-0811, Japan</nlm:aff>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>Division of Viral Immunology, Center for AIDS Research, Kumamoto University, 2-2-1 Honjo, Kumamoto 860-0811</wicri:regionArea>
<wicri:noRegion>Kumamoto 860-0811</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Nan, Peng" sort="Nan, Peng" uniqKey="Nan P" first="Peng" last="Nan">Peng Nan</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">School of Life Sciences, Fudan University, Shanghai 200433, China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>School of Life Sciences, Fudan University, Shanghai 200433</wicri:regionArea>
<wicri:noRegion>Shanghai 200433</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Cao, Ying" sort="Cao, Ying" uniqKey="Cao Y" first="Ying" last="Cao">Ying Cao</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">The Institute of Statistical Mathematics, 4-6-7 Minami-Azabu, Minato-ku, Tokyo 106, Japan</nlm:aff>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>The Institute of Statistical Mathematics, 4-6-7 Minami-Azabu, Minato-ku, Tokyo 106</wicri:regionArea>
<placeName><settlement type="city">Tokyo</settlement>
<region type="région">Région de Kantō</region>
</placeName>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff4">Department of Biosystems Science, The Graduate University for Advanced Studies, Hayama, Kanagawa 240-0193, Japan</nlm:aff>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>Department of Biosystems Science, The Graduate University for Advanced Studies, Hayama, Kanagawa 240-0193</wicri:regionArea>
<wicri:noRegion>Kanagawa 240-0193</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Hasegawa, Masami" sort="Hasegawa, Masami" uniqKey="Hasegawa M" first="Masami" last="Hasegawa">Masami Hasegawa</name>
<affiliation wicri:level="1"><nlm:aff id="aff3">The Institute of Statistical Mathematics, 4-6-7 Minami-Azabu, Minato-ku, Tokyo 106, Japan</nlm:aff>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>The Institute of Statistical Mathematics, 4-6-7 Minami-Azabu, Minato-ku, Tokyo 106</wicri:regionArea>
<placeName><settlement type="city">Tokyo</settlement>
<region type="région">Région de Kantō</region>
</placeName>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff4">Department of Biosystems Science, The Graduate University for Advanced Studies, Hayama, Kanagawa 240-0193, Japan</nlm:aff>
<country xml:lang="fr">Japon</country>
<wicri:regionArea>Department of Biosystems Science, The Graduate University for Advanced Studies, Hayama, Kanagawa 240-0193</wicri:regionArea>
<wicri:noRegion>Kanagawa 240-0193</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Zhong, Yang" sort="Zhong, Yang" uniqKey="Zhong Y" first="Yang" last="Zhong">Yang Zhong</name>
<affiliation wicri:level="1"><nlm:aff id="aff1">School of Life Sciences, Fudan University, Shanghai 200433, China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>School of Life Sciences, Fudan University, Shanghai 200433</wicri:regionArea>
<wicri:noRegion>Shanghai 200433</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff5">Shanghai Center for Bioinformation Technology, Shanghai 200235, China</nlm:aff>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>Shanghai Center for Bioinformation Technology, Shanghai 200235</wicri:regionArea>
<wicri:noRegion>Shanghai 200235</wicri:noRegion>
</affiliation>
</author>
</analytic>
<series><title level="j">Computational Biology and Chemistry</title>
<idno type="ISSN">1476-9271</idno>
<idno type="eISSN">1476-928X</idno>
<imprint><date when="2007">2007</date>
</imprint>
</series>
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<front><div type="abstract" xml:lang="en"><p>As a critical adaptive mechanism, amino acid replacements on the severe acute respiratory syndrome coronavirus (SARS-CoV) spike protein could alter the receptor-binding specificity of this envelope glycoprotein and in turn lead to the emergence or reemergence of this viral zoonosis. Based on the X-ray structures of SARS-CoV spike receptor-binding domain (RBD) in complex with its functional receptor (angiotensin-converting enzyme 2, ACE2), we perform computational simulations of interactions between three representative RBD mutants and four host species-specific receptors. The comparisons between computational predictions and experimental evidences validate our structural bioinformatics approaches. And the predictions further indicate that some viral prototypes might utilize the rat ACE2 while rats might serve as a vector or reservoir of SARS-CoV.</p>
</div>
</front>
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<pubmed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Computational simulation of interactions between SARS coronavirus spike mutants and host species-specific receptors.</title>
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<affiliation wicri:level="1"><nlm:affiliation>School of Life Sciences, Fudan University, Shanghai 200433, China. yuanzhang5@fudan.edu.cn</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>School of Life Sciences, Fudan University, Shanghai 200433</wicri:regionArea>
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<author><name sortKey="Zheng, Nan" sort="Zheng, Nan" uniqKey="Zheng N" first="Nan" last="Zheng">Nan Zheng</name>
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<author><name sortKey="Nan, Peng" sort="Nan, Peng" uniqKey="Nan P" first="Peng" last="Nan">Peng Nan</name>
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<author><name sortKey="Cao, Ying" sort="Cao, Ying" uniqKey="Cao Y" first="Ying" last="Cao">Ying Cao</name>
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<author><name sortKey="Hasegawa, Masami" sort="Hasegawa, Masami" uniqKey="Hasegawa M" first="Masami" last="Hasegawa">Masami Hasegawa</name>
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<author><name sortKey="Zhong, Yang" sort="Zhong, Yang" uniqKey="Zhong Y" first="Yang" last="Zhong">Yang Zhong</name>
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<author><name sortKey="Zhang, Yuan" sort="Zhang, Yuan" uniqKey="Zhang Y" first="Yuan" last="Zhang">Yuan Zhang</name>
<affiliation wicri:level="1"><nlm:affiliation>School of Life Sciences, Fudan University, Shanghai 200433, China. yuanzhang5@fudan.edu.cn</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>School of Life Sciences, Fudan University, Shanghai 200433</wicri:regionArea>
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<term>Membrane Glycoproteins (metabolism)</term>
<term>Mice</term>
<term>Mutation</term>
<term>Peptidyl-Dipeptidase A (chemistry)</term>
<term>Peptidyl-Dipeptidase A (metabolism)</term>
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<term>Receptors, Virus (metabolism)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
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<term>Spike Glycoprotein, Coronavirus</term>
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<term>Chats</term>
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<term>Liaison aux protéines</term>
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<term>Liaison aux protéines</term>
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<front><div type="abstract" xml:lang="en">As a critical adaptive mechanism, amino acid replacements on the severe acute respiratory syndrome coronavirus (SARS-CoV) spike protein could alter the receptor-binding specificity of this envelope glycoprotein and in turn lead to the emergence or reemergence of this viral zoonosis. Based on the X-ray structures of SARS-CoV spike receptor-binding domain (RBD) in complex with its functional receptor (angiotensin-converting enzyme 2, ACE2), we perform computational simulations of interactions between three representative RBD mutants and four host species-specific receptors. The comparisons between computational predictions and experimental evidences validate our structural bioinformatics approaches. And the predictions further indicate that some viral prototypes might utilize the rat ACE2 while rats might serve as a vector or reservoir of SARS-CoV.</div>
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