MersV1, PubMed, Corpus, bibRecord, 001004

p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1.

Identifieur interne : 001004 ( PubMed/Corpus ); précédent : 001003; suivant : 001005

p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1.

Auteurs : Yue Ma-Lauer ; Javier Carbajo-Lozoya ; Marco Y. Hein ; Marcel A. Müller ; Wen Deng ; Jian Lei ; Benjamin Meyer ; Yuri Kusov ; Brigitte Von Brunn ; Dev Raj Bairad ; Sabine Hünten ; Christian Drosten ; Heiko Hermeking ; Heinrich Leonhardt ; Matthias Mann ; Rolf Hilgenfeld ; Albrecht Von Brunn

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2016.

RBID : pubmed:27519799

English descriptors

Abstract

Highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) has developed strategies to inhibit host immune recognition. We identify cellular E3 ubiquitin ligase ring-finger and CHY zinc-finger domain-containing 1 (RCHY1) as an interacting partner of the viral SARS-unique domain (SUD) and papain-like protease (PL(pro)), and, as a consequence, the involvement of cellular p53 as antagonist of coronaviral replication. Residues 95-144 of RCHY1 and 389-652 of SUD (SUD-NM) subdomains are crucial for interaction. Association with SUD increases the stability of RCHY1 and augments RCHY1-mediated ubiquitination as well as degradation of p53. The calcium/calmodulin-dependent protein kinase II delta (CAMK2D), which normally influences RCHY1 stability by phosphorylation, also binds to SUD. In vivo phosphorylation shows that SUD does not regulate phosphorylation of RCHY1 via CAMK2D. Similarly to SUD, the PL(pro)s from SARS-CoV, MERS-CoV, and HCoV-NL63 physically interact with and stabilize RCHY1, and thus trigger degradation of endogenous p53. The SARS-CoV papain-like protease is encoded next to SUD within nonstructural protein 3. A SUD-PL(pro) fusion interacts with RCHY1 more intensively and causes stronger p53 degradation than SARS-CoV PL(pro) alone. We show that p53 inhibits replication of infectious SARS-CoV as well as of replicons and human coronavirus NL63. Hence, human coronaviruses antagonize the viral inhibitor p53 via stabilizing RCHY1 and promoting RCHY1-mediated p53 degradation. SUD functions as an enhancer to strengthen interaction between RCHY1 and nonstructural protein 3, leading to a further increase in in p53 degradation. The significance of these findings is that down-regulation of p53 as a major player in antiviral innate immunity provides a long-sought explanation for delayed activities of respective genes.

DOI: 10.1073/pnas.1603435113
PubMed: 27519799

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pubmed:27519799

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<author><name sortKey="Ma Lauer, Yue" sort="Ma Lauer, Yue" uniqKey="Ma Lauer Y" first="Yue" last="Ma-Lauer">Yue Ma-Lauer</name>
<affiliation><nlm:affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck and German Center for Infection Research, partner site Luebeck, 23538 Luebeck, Germany; Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF), partner site Munich, 80336 Munich, Germany;</nlm:affiliation>
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<author><name sortKey="Carbajo Lozoya, Javier" sort="Carbajo Lozoya, Javier" uniqKey="Carbajo Lozoya J" first="Javier" last="Carbajo-Lozoya">Javier Carbajo-Lozoya</name>
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<author><name sortKey="Hein, Marco Y" sort="Hein, Marco Y" uniqKey="Hein M" first="Marco Y" last="Hein">Marco Y. Hein</name>
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<author><name sortKey="Muller, Marcel A" sort="Muller, Marcel A" uniqKey="Muller M" first="Marcel A" last="Müller">Marcel A. Müller</name>
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<author><name sortKey="Deng, Wen" sort="Deng, Wen" uniqKey="Deng W" first="Wen" last="Deng">Wen Deng</name>
<affiliation><nlm:affiliation>Department of Biology and Center for Integrated Protein Science, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany;</nlm:affiliation>
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<author><name sortKey="Meyer, Benjamin" sort="Meyer, Benjamin" uniqKey="Meyer B" first="Benjamin" last="Meyer">Benjamin Meyer</name>
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<author><name sortKey="Kusov, Yuri" sort="Kusov, Yuri" uniqKey="Kusov Y" first="Yuri" last="Kusov">Yuri Kusov</name>
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<author><name sortKey="Von Brunn, Brigitte" sort="Von Brunn, Brigitte" uniqKey="Von Brunn B" first="Brigitte" last="Von Brunn">Brigitte Von Brunn</name>
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<author><name sortKey="Bairad, Dev Raj" sort="Bairad, Dev Raj" uniqKey="Bairad D" first="Dev Raj" last="Bairad">Dev Raj Bairad</name>
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<author><name sortKey="Hunten, Sabine" sort="Hunten, Sabine" uniqKey="Hunten S" first="Sabine" last="Hünten">Sabine Hünten</name>
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<author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name>
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</affiliation>
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<author><name sortKey="Hermeking, Heiko" sort="Hermeking, Heiko" uniqKey="Hermeking H" first="Heiko" last="Hermeking">Heiko Hermeking</name>
<affiliation><nlm:affiliation>Experimental and Molecular Pathology, Institute of Pathology, Ludwig-Maximilians-University Munich, 80337 Munich, Germany.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Leonhardt, Heinrich" sort="Leonhardt, Heinrich" uniqKey="Leonhardt H" first="Heinrich" last="Leonhardt">Heinrich Leonhardt</name>
<affiliation><nlm:affiliation>Department of Biology and Center for Integrated Protein Science, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany;</nlm:affiliation>
</affiliation>
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<author><name sortKey="Mann, Matthias" sort="Mann, Matthias" uniqKey="Mann M" first="Matthias" last="Mann">Matthias Mann</name>
<affiliation><nlm:affiliation>Department of Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, 82152 Martinsried, Germany;</nlm:affiliation>
</affiliation>
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<author><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name>
<affiliation><nlm:affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck and German Center for Infection Research, partner site Luebeck, 23538 Luebeck, Germany;</nlm:affiliation>
</affiliation>
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<author><name sortKey="Von Brunn, Albrecht" sort="Von Brunn, Albrecht" uniqKey="Von Brunn A" first="Albrecht" last="Von Brunn">Albrecht Von Brunn</name>
<affiliation><nlm:affiliation>Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF), partner site Munich, 80336 Munich, Germany; vonbrunn@mvp.uni-muenchen.de.</nlm:affiliation>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1.</title>
<author><name sortKey="Ma Lauer, Yue" sort="Ma Lauer, Yue" uniqKey="Ma Lauer Y" first="Yue" last="Ma-Lauer">Yue Ma-Lauer</name>
<affiliation><nlm:affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck and German Center for Infection Research, partner site Luebeck, 23538 Luebeck, Germany; Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF), partner site Munich, 80336 Munich, Germany;</nlm:affiliation>
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<author><name sortKey="Carbajo Lozoya, Javier" sort="Carbajo Lozoya, Javier" uniqKey="Carbajo Lozoya J" first="Javier" last="Carbajo-Lozoya">Javier Carbajo-Lozoya</name>
<affiliation><nlm:affiliation>Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF), partner site Munich, 80336 Munich, Germany;</nlm:affiliation>
</affiliation>
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<author><name sortKey="Hein, Marco Y" sort="Hein, Marco Y" uniqKey="Hein M" first="Marco Y" last="Hein">Marco Y. Hein</name>
<affiliation><nlm:affiliation>Department of Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, 82152 Martinsried, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Muller, Marcel A" sort="Muller, Marcel A" uniqKey="Muller M" first="Marcel A" last="Müller">Marcel A. Müller</name>
<affiliation><nlm:affiliation>Institute of Virology, University of Bonn Medical Centre and German Center for Infection Research, partner site Bonn, 53127 Bonn, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Deng, Wen" sort="Deng, Wen" uniqKey="Deng W" first="Wen" last="Deng">Wen Deng</name>
<affiliation><nlm:affiliation>Department of Biology and Center for Integrated Protein Science, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Lei, Jian" sort="Lei, Jian" uniqKey="Lei J" first="Jian" last="Lei">Jian Lei</name>
<affiliation><nlm:affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck and German Center for Infection Research, partner site Luebeck, 23538 Luebeck, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Meyer, Benjamin" sort="Meyer, Benjamin" uniqKey="Meyer B" first="Benjamin" last="Meyer">Benjamin Meyer</name>
<affiliation><nlm:affiliation>Institute of Virology, University of Bonn Medical Centre and German Center for Infection Research, partner site Bonn, 53127 Bonn, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Kusov, Yuri" sort="Kusov, Yuri" uniqKey="Kusov Y" first="Yuri" last="Kusov">Yuri Kusov</name>
<affiliation><nlm:affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck and German Center for Infection Research, partner site Luebeck, 23538 Luebeck, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Von Brunn, Brigitte" sort="Von Brunn, Brigitte" uniqKey="Von Brunn B" first="Brigitte" last="Von Brunn">Brigitte Von Brunn</name>
<affiliation><nlm:affiliation>Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF), partner site Munich, 80336 Munich, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Bairad, Dev Raj" sort="Bairad, Dev Raj" uniqKey="Bairad D" first="Dev Raj" last="Bairad">Dev Raj Bairad</name>
<affiliation><nlm:affiliation>Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF), partner site Munich, 80336 Munich, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Hunten, Sabine" sort="Hunten, Sabine" uniqKey="Hunten S" first="Sabine" last="Hünten">Sabine Hünten</name>
<affiliation><nlm:affiliation>Experimental and Molecular Pathology, Institute of Pathology, Ludwig-Maximilians-University Munich, 80337 Munich, Germany.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name>
<affiliation><nlm:affiliation>Institute of Virology, University of Bonn Medical Centre and German Center for Infection Research, partner site Bonn, 53127 Bonn, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Hermeking, Heiko" sort="Hermeking, Heiko" uniqKey="Hermeking H" first="Heiko" last="Hermeking">Heiko Hermeking</name>
<affiliation><nlm:affiliation>Experimental and Molecular Pathology, Institute of Pathology, Ludwig-Maximilians-University Munich, 80337 Munich, Germany.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Leonhardt, Heinrich" sort="Leonhardt, Heinrich" uniqKey="Leonhardt H" first="Heinrich" last="Leonhardt">Heinrich Leonhardt</name>
<affiliation><nlm:affiliation>Department of Biology and Center for Integrated Protein Science, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Mann, Matthias" sort="Mann, Matthias" uniqKey="Mann M" first="Matthias" last="Mann">Matthias Mann</name>
<affiliation><nlm:affiliation>Department of Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, 82152 Martinsried, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Hilgenfeld, Rolf" sort="Hilgenfeld, Rolf" uniqKey="Hilgenfeld R" first="Rolf" last="Hilgenfeld">Rolf Hilgenfeld</name>
<affiliation><nlm:affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck and German Center for Infection Research, partner site Luebeck, 23538 Luebeck, Germany;</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Von Brunn, Albrecht" sort="Von Brunn, Albrecht" uniqKey="Von Brunn A" first="Albrecht" last="Von Brunn">Albrecht Von Brunn</name>
<affiliation><nlm:affiliation>Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF), partner site Munich, 80336 Munich, Germany; vonbrunn@mvp.uni-muenchen.de.</nlm:affiliation>
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<idno type="eISSN">1091-6490</idno>
<imprint><date when="2016" type="published">2016</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (genetics)</term>
<term>Calcium-Calmodulin-Dependent Protein Kinase Type 2 (genetics)</term>
<term>Calcium-Calmodulin-Dependent Protein Kinase Type 2 (metabolism)</term>
<term>Cysteine Endopeptidases (genetics)</term>
<term>Cysteine Endopeptidases (metabolism)</term>
<term>Down-Regulation</term>
<term>Host-Pathogen Interactions</term>
<term>Humans</term>
<term>Protein Binding</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
<term>SARS Virus (physiology)</term>
<term>Severe Acute Respiratory Syndrome (genetics)</term>
<term>Severe Acute Respiratory Syndrome (metabolism)</term>
<term>Severe Acute Respiratory Syndrome (virology)</term>
<term>Tumor Suppressor Protein p53 (metabolism)</term>
<term>Ubiquitin-Protein Ligases (genetics)</term>
<term>Ubiquitin-Protein Ligases (metabolism)</term>
<term>Ubiquitination</term>
<term>Viral Nonstructural Proteins (genetics)</term>
<term>Viral Nonstructural Proteins (metabolism)</term>
<term>Viral Proteins (genetics)</term>
<term>Viral Proteins (metabolism)</term>
<term>Virus Replication (genetics)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2</term>
<term>Cysteine Endopeptidases</term>
<term>Ubiquitin-Protein Ligases</term>
<term>Viral Nonstructural Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Binding Sites</term>
<term>SARS Virus</term>
<term>Severe Acute Respiratory Syndrome</term>
<term>Virus Replication</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2</term>
<term>Cysteine Endopeptidases</term>
<term>SARS Virus</term>
<term>Severe Acute Respiratory Syndrome</term>
<term>Tumor Suppressor Protein p53</term>
<term>Ubiquitin-Protein Ligases</term>
<term>Viral Nonstructural Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" 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>Down-Regulation</term>
<term>Host-Pathogen Interactions</term>
<term>Humans</term>
<term>Protein Binding</term>
<term>Ubiquitination</term>
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<front><div type="abstract" xml:lang="en">Highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) has developed strategies to inhibit host immune recognition. We identify cellular E3 ubiquitin ligase ring-finger and CHY zinc-finger domain-containing 1 (RCHY1) as an interacting partner of the viral SARS-unique domain (SUD) and papain-like protease (PL(pro)), and, as a consequence, the involvement of cellular p53 as antagonist of coronaviral replication. Residues 95-144 of RCHY1 and 389-652 of SUD (SUD-NM) subdomains are crucial for interaction. Association with SUD increases the stability of RCHY1 and augments RCHY1-mediated ubiquitination as well as degradation of p53. The calcium/calmodulin-dependent protein kinase II delta (CAMK2D), which normally influences RCHY1 stability by phosphorylation, also binds to SUD. In vivo phosphorylation shows that SUD does not regulate phosphorylation of RCHY1 via CAMK2D. Similarly to SUD, the PL(pro)s from SARS-CoV, MERS-CoV, and HCoV-NL63 physically interact with and stabilize RCHY1, and thus trigger degradation of endogenous p53. The SARS-CoV papain-like protease is encoded next to SUD within nonstructural protein 3. A SUD-PL(pro) fusion interacts with RCHY1 more intensively and causes stronger p53 degradation than SARS-CoV PL(pro) alone. We show that p53 inhibits replication of infectious SARS-CoV as well as of replicons and human coronavirus NL63. Hence, human coronaviruses antagonize the viral inhibitor p53 via stabilizing RCHY1 and promoting RCHY1-mediated p53 degradation. SUD functions as an enhancer to strengthen interaction between RCHY1 and nonstructural protein 3, leading to a further increase in in p53 degradation. The significance of these findings is that down-regulation of p53 as a major player in antiviral innate immunity provides a long-sought explanation for delayed activities of respective genes.</div>
</front>
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<DateCompleted><Year>2018</Year>
<Month>03</Month>
<Day>26</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>25</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>113</Volume>
<Issue>35</Issue>
<PubDate><Year>2016</Year>
<Month>08</Month>
<Day>30</Day>
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<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
<ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation>
</Journal>
<ArticleTitle>p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1.</ArticleTitle>
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<Abstract><AbstractText>Highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) has developed strategies to inhibit host immune recognition. We identify cellular E3 ubiquitin ligase ring-finger and CHY zinc-finger domain-containing 1 (RCHY1) as an interacting partner of the viral SARS-unique domain (SUD) and papain-like protease (PL(pro)), and, as a consequence, the involvement of cellular p53 as antagonist of coronaviral replication. Residues 95-144 of RCHY1 and 389-652 of SUD (SUD-NM) subdomains are crucial for interaction. Association with SUD increases the stability of RCHY1 and augments RCHY1-mediated ubiquitination as well as degradation of p53. The calcium/calmodulin-dependent protein kinase II delta (CAMK2D), which normally influences RCHY1 stability by phosphorylation, also binds to SUD. In vivo phosphorylation shows that SUD does not regulate phosphorylation of RCHY1 via CAMK2D. Similarly to SUD, the PL(pro)s from SARS-CoV, MERS-CoV, and HCoV-NL63 physically interact with and stabilize RCHY1, and thus trigger degradation of endogenous p53. The SARS-CoV papain-like protease is encoded next to SUD within nonstructural protein 3. A SUD-PL(pro) fusion interacts with RCHY1 more intensively and causes stronger p53 degradation than SARS-CoV PL(pro) alone. We show that p53 inhibits replication of infectious SARS-CoV as well as of replicons and human coronavirus NL63. Hence, human coronaviruses antagonize the viral inhibitor p53 via stabilizing RCHY1 and promoting RCHY1-mediated p53 degradation. SUD functions as an enhancer to strengthen interaction between RCHY1 and nonstructural protein 3, leading to a further increase in in p53 degradation. The significance of these findings is that down-regulation of p53 as a major player in antiviral innate immunity provides a long-sought explanation for delayed activities of respective genes.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ma-Lauer</LastName>
<ForeName>Yue</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck and German Center for Infection Research, partner site Luebeck, 23538 Luebeck, Germany; Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF), partner site Munich, 80336 Munich, Germany;</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Carbajo-Lozoya</LastName>
<ForeName>Javier</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich and German Center for Infection Research (DZIF), partner site Munich, 80336 Munich, Germany;</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hein</LastName>
<ForeName>Marco Y</ForeName>
<Initials>MY</Initials>
<Identifier Source="ORCID">0000-0002-9490-2261</Identifier>
<AffiliationInfo><Affiliation>Department of Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, 82152 Martinsried, Germany;</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Müller</LastName>
<ForeName>Marcel A</ForeName>
<Initials>MA</Initials>
<AffiliationInfo><Affiliation>Institute of Virology, University of Bonn Medical Centre and German Center for Infection Research, partner site Bonn, 53127 Bonn, Germany;</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Deng</LastName>
<ForeName>Wen</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Department of Biology and Center for Integrated Protein Science, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany;</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lei</LastName>
<ForeName>Jian</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck and German Center for Infection Research, partner site Luebeck, 23538 Luebeck, Germany;</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Meyer</LastName>
<ForeName>Benjamin</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Institute of Virology, University of Bonn Medical Centre and German Center for Infection Research, partner site Bonn, 53127 Bonn, Germany;</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kusov</LastName>
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   |texte=   p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1.
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p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1.

p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1.

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