The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis.
Identifieur interne : 002458 ( Main/Merge ); précédent : 002457; suivant : 002459The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis.
Auteurs : Kim-Tat Teoh ; Yu-Lam Siu ; Wing-Lim Chan ; Marc A. Schlüter ; Chia-Jen Liu ; J S Malik Peiris ; Roberto Bruzzone ; Benjamin Margolis ; Béatrice NalSource :
- Molecular biology of the cell [ 1939-4586 ] ; 2010.
Descripteurs français
- KwdFr :
- Animaux, Cellules HEK293, Cellules Vero, Cellules épithéliales (cytologie), Cellules épithéliales (métabolisme), Cellules épithéliales (virologie), Glutathione transferase, Humains, Immunotransfert, Interactions hôte-pathogène, Jonctions serrées (métabolisme), Jonctions serrées (virologie), Liaison aux protéines, Lignée cellulaire, Microscopie de fluorescence, Morphogenèse, Nucleoside phosphate kinase (génétique), Nucleoside phosphate kinase (métabolisme), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines luminescentes (génétique), Protéines luminescentes (métabolisme), Protéines membranaires (génétique), Protéines membranaires (métabolisme), Sites de fixation, Techniques de double hybride, Virus du SRAS (métabolisme), Virus du SRAS (physiologie), Épithélium (croissance et développement), Épithélium (métabolisme).
- MESH :
- croissance et développement : Épithélium.
- cytologie : Cellules épithéliales.
- génétique : Nucleoside phosphate kinase, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Protéines luminescentes, Protéines membranaires.
- métabolisme : Cellules épithéliales, Jonctions serrées, Nucleoside phosphate kinase, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Protéines luminescentes, Protéines membranaires, Virus du SRAS, Épithélium.
- physiologie : Virus du SRAS.
- virologie : Cellules épithéliales, Jonctions serrées.
- Animaux, Cellules HEK293, Cellules Vero, Glutathione transferase, Humains, Immunotransfert, Interactions hôte-pathogène, Liaison aux protéines, Lignée cellulaire, Microscopie de fluorescence, Morphogenèse, Sites de fixation, Techniques de double hybride.
English descriptors
- KwdEn :
- Animals, Binding Sites, Cell Line, Chlorocebus aethiops, Epithelial Cells (cytology), Epithelial Cells (metabolism), Epithelial Cells (virology), Epithelium (growth & development), Epithelium (metabolism), Glutathione Transferase, HEK293 Cells, Host-Pathogen Interactions, Humans, Immunoblotting, Luminescent Proteins (genetics), Luminescent Proteins (metabolism), Membrane Proteins (genetics), Membrane Proteins (metabolism), Microscopy, Fluorescence, Morphogenesis, Nucleoside-Phosphate Kinase (genetics), Nucleoside-Phosphate Kinase (metabolism), Protein Binding, Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (metabolism), SARS Virus (physiology), Tight Junctions (metabolism), Tight Junctions (virology), Two-Hybrid System Techniques, Vero Cells, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , genetics : Luminescent Proteins, Membrane Proteins, Nucleoside-Phosphate Kinase, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemical , metabolism : Luminescent Proteins, Membrane Proteins, Nucleoside-Phosphate Kinase, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemical : Glutathione Transferase.
- cytology : Epithelial Cells.
- growth & development : Epithelium.
- metabolism : Epithelial Cells, Epithelium, SARS Virus, Tight Junctions.
- physiology : SARS Virus.
- virology : Epithelial Cells, Tight Junctions.
- Animals, Binding Sites, Cell Line, Chlorocebus aethiops, HEK293 Cells, Host-Pathogen Interactions, Humans, Immunoblotting, Microscopy, Fluorescence, Morphogenesis, Protein Binding, Two-Hybrid System Techniques, Vero Cells.
Abstract
Intercellular tight junctions define epithelial apicobasal polarity and form a physical fence which protects underlying tissues from pathogen invasions. PALS1, a tight junction-associated protein, is a member of the CRUMBS3-PALS1-PATJ polarity complex, which is crucial for the establishment and maintenance of epithelial polarity in mammals. Here we report that the carboxy-terminal domain of the SARS-CoV E small envelope protein (E) binds to human PALS1. Using coimmunoprecipitation and pull-down assays, we show that E interacts with PALS1 in mammalian cells and further demonstrate that the last four carboxy-terminal amino acids of E form a novel PDZ-binding motif that binds to PALS1 PDZ domain. PALS1 redistributes to the ERGIC/Golgi region, where E accumulates, in SARS-CoV-infected Vero E6 cells. Ectopic expression of E in MDCKII epithelial cells significantly alters cyst morphogenesis and, furthermore, delays formation of tight junctions, affects polarity, and modifies the subcellular distribution of PALS1, in a PDZ-binding motif-dependent manner. We speculate that hijacking of PALS1 by SARS-CoV E plays a determinant role in the disruption of the lung epithelium in SARS patients.
Url:
DOI: 10.1091/mbc.E10-04-0338
PubMed: 20861307
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pubmed:20861307Le document en format XML
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Cells</term><term>Tight Junctions</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>HEK293 Cells</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Immunoblotting</term><term>Microscopy, Fluorescence</term><term>Morphogenesis</term><term>Protein Binding</term><term>Two-Hybrid System Techniques</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HEK293</term><term>Cellules Vero</term><term>Glutathione transferase</term><term>Humains</term><term>Immunotransfert</term><term>Interactions hôte-pathogène</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Microscopie de fluorescence</term><term>Morphogenèse</term><term>Sites de fixation</term><term>Techniques de double hybride</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Intercellular tight junctions define epithelial apicobasal polarity and form a physical fence which protects underlying tissues from pathogen invasions. PALS1, a tight junction-associated protein, is a member of the CRUMBS3-PALS1-PATJ polarity complex, which is crucial for the establishment and maintenance of epithelial polarity in mammals. Here we report that the carboxy-terminal domain of the SARS-CoV E small envelope protein (E) binds to human PALS1. Using coimmunoprecipitation and pull-down assays, we show that E interacts with PALS1 in mammalian cells and further demonstrate that the last four carboxy-terminal amino acids of E form a novel PDZ-binding motif that binds to PALS1 PDZ domain. PALS1 redistributes to the ERGIC/Golgi region, where E accumulates, in SARS-CoV-infected Vero E6 cells. Ectopic expression of E in MDCKII epithelial cells significantly alters cyst morphogenesis and, furthermore, delays formation of tight junctions, affects polarity, and modifies the subcellular distribution of PALS1, in a PDZ-binding motif-dependent manner. We speculate that hijacking of PALS1 by SARS-CoV E plays a determinant role in the disruption of the lung epithelium in SARS patients.</div></front></TEI><double doi="10.1091/mbc.E10-04-0338"><HAL><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis.</title><author><name sortKey="Teoh, Kim Tat" sort="Teoh, Kim Tat" uniqKey="Teoh K" first="Kim-Tat" last="Teoh">Kim-Tat Teoh</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author><author><name sortKey="Siu, Yu Lam" sort="Siu, Yu Lam" uniqKey="Siu Y" first="Yu-Lam" last="Siu">Yu-Lam Siu</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author><author><name sortKey="Chan, Wing Lim" sort="Chan, Wing Lim" uniqKey="Chan W" first="Wing-Lim" last="Chan">Wing-Lim Chan</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author><author><name sortKey="Schluter, Marc A" sort="Schluter, Marc A" uniqKey="Schluter M" first="Marc A" last="Schlüter">Marc A. Schlüter</name><affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-136012" status="INCOMING"> <orgName>Medizinische Klinik D</orgName> <desc> <address> <addrLine>Medizinische Klinik D, Universitätsklinikum Münster, Albert-Schweitzer-Str. 33, D-48149 Münster,</addrLine> <country key="DE"></country> </address> </desc> <listRelation> <relation active="#struct-333017" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-333017" type="direct"><org type="institution" xml:id="struct-333017" status="INCOMING"> <orgName>Universitätsklinikum Münster</orgName> <desc> <address> <country key="FR"></country> </address> </desc> </org></tutelle></tutelles></hal:affiliation><country>Allemagne</country></affiliation></author><author><name sortKey="Liu, Chia Jen" sort="Liu, Chia Jen" uniqKey="Liu C" first="Chia-Jen" last="Liu">Chia-Jen Liu</name><affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-136013" status="INCOMING"> <orgName>Department of Internal Medicine</orgName> <desc> <address> <addrLine>University of Michigan Medical School, 109 Zina Pitcher Place, Ann Arbor, MI 48109</addrLine> <country key="US"></country> </address> </desc> <listRelation> <relation active="#struct-24332" type="direct"></relation> <relation active="#struct-566437" type="indirect"></relation> </listRelation> <tutelles><tutelle active="#struct-24332" type="direct"><org type="institution" xml:id="struct-24332" status="VALID"> <orgName>University of Michigan [Ann Arbor]</orgName> <desc> <address> <addrLine>500 Church Street Ann Arbor, MI 48109-1090</addrLine> <country key="US"></country> </address> <ref type="url">http://www.umich.edu/</ref> </desc> <listRelation> <relation active="#struct-566437" type="direct"></relation> </listRelation> </org></tutelle><tutelle active="#struct-566437" type="indirect"><org type="regroupinstitution" xml:id="struct-566437" status="VALID"> <orgName>University of Michigan System</orgName> <desc> <address> <addrLine>Michigan</addrLine> <country key="US"></country> </address> <ref type="url">https://umich.edu/</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>États-Unis</country></affiliation></author><author><name sortKey="Peiris, J S Malik" sort="Peiris, J S Malik" uniqKey="Peiris J" first="J S Malik" last="Peiris">J S Malik Peiris</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author><author><name sortKey="Bruzzone, Roberto" sort="Bruzzone, Roberto" uniqKey="Bruzzone R" first="Roberto" last="Bruzzone">Roberto Bruzzone</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author><author><name sortKey="Margolis, Benjamin" sort="Margolis, Benjamin" uniqKey="Margolis B" first="Benjamin" last="Margolis">Benjamin Margolis</name><affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-136013" status="INCOMING"> <orgName>Department of Internal Medicine</orgName> <desc> <address> <addrLine>University of Michigan Medical School, 109 Zina Pitcher Place, Ann Arbor, MI 48109</addrLine> <country key="US"></country> </address> </desc> <listRelation> <relation active="#struct-24332" type="direct"></relation> <relation active="#struct-566437" type="indirect"></relation> </listRelation> <tutelles><tutelle active="#struct-24332" type="direct"><org type="institution" xml:id="struct-24332" status="VALID"> <orgName>University of Michigan [Ann Arbor]</orgName> <desc> <address> <addrLine>500 Church Street Ann Arbor, MI 48109-1090</addrLine> <country key="US"></country> </address> <ref type="url">http://www.umich.edu/</ref> </desc> <listRelation> <relation active="#struct-566437" type="direct"></relation> </listRelation> </org></tutelle><tutelle active="#struct-566437" type="indirect"><org type="regroupinstitution" xml:id="struct-566437" status="VALID"> <orgName>University of Michigan System</orgName> <desc> <address> <addrLine>Michigan</addrLine> <country key="US"></country> </address> <ref type="url">https://umich.edu/</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>États-Unis</country></affiliation></author><author><name sortKey="Nal, Beatrice" sort="Nal, Beatrice" uniqKey="Nal B" first="Béatrice" last="Nal">Béatrice Nal</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">HAL</idno><idno type="RBID">Hal:pasteur-00545808</idno><idno type="halId">pasteur-00545808</idno><idno type="halUri">https://hal-riip.archives-ouvertes.fr/pasteur-00545808</idno><idno type="url">https://hal-riip.archives-ouvertes.fr/pasteur-00545808</idno><idno type="doi">10.1091/mbc.E10-04-0338</idno><date when="2010-11">2010-11</date><idno type="wicri:Area/Hal/Corpus">000162</idno><idno type="wicri:Area/Hal/Curation">000162</idno><idno type="wicri:Area/Hal/Checkpoint">000132</idno><idno type="wicri:explorRef" wicri:stream="Hal" wicri:step="Checkpoint">000132</idno><idno type="wicri:doubleKey">1059-1524:2010:Teoh K:the:sars:coronavirus</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis.</title><author><name sortKey="Teoh, Kim Tat" sort="Teoh, Kim Tat" uniqKey="Teoh K" first="Kim-Tat" last="Teoh">Kim-Tat Teoh</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author><author><name sortKey="Siu, Yu Lam" sort="Siu, Yu Lam" uniqKey="Siu Y" first="Yu-Lam" last="Siu">Yu-Lam Siu</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author><author><name sortKey="Chan, Wing Lim" sort="Chan, Wing Lim" uniqKey="Chan W" first="Wing-Lim" last="Chan">Wing-Lim Chan</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author><author><name sortKey="Schluter, Marc A" sort="Schluter, Marc A" uniqKey="Schluter M" first="Marc A" last="Schlüter">Marc A. Schlüter</name><affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-136012" status="INCOMING"> <orgName>Medizinische Klinik D</orgName> <desc> <address> <addrLine>Medizinische Klinik D, Universitätsklinikum Münster, Albert-Schweitzer-Str. 33, D-48149 Münster,</addrLine> <country key="DE"></country> </address> </desc> <listRelation> <relation active="#struct-333017" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-333017" type="direct"><org type="institution" xml:id="struct-333017" status="INCOMING"> <orgName>Universitätsklinikum Münster</orgName> <desc> <address> <country key="FR"></country> </address> </desc> </org></tutelle></tutelles></hal:affiliation><country>Allemagne</country></affiliation></author><author><name sortKey="Liu, Chia Jen" sort="Liu, Chia Jen" uniqKey="Liu C" first="Chia-Jen" last="Liu">Chia-Jen Liu</name><affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-136013" status="INCOMING"> <orgName>Department of Internal Medicine</orgName> <desc> <address> <addrLine>University of Michigan Medical School, 109 Zina Pitcher Place, Ann Arbor, MI 48109</addrLine> <country key="US"></country> </address> </desc> <listRelation> <relation active="#struct-24332" type="direct"></relation> <relation active="#struct-566437" type="indirect"></relation> </listRelation> <tutelles><tutelle active="#struct-24332" type="direct"><org type="institution" xml:id="struct-24332" status="VALID"> <orgName>University of Michigan [Ann Arbor]</orgName> <desc> <address> <addrLine>500 Church Street Ann Arbor, MI 48109-1090</addrLine> <country key="US"></country> </address> <ref type="url">http://www.umich.edu/</ref> </desc> <listRelation> <relation active="#struct-566437" type="direct"></relation> </listRelation> </org></tutelle><tutelle active="#struct-566437" type="indirect"><org type="regroupinstitution" xml:id="struct-566437" status="VALID"> <orgName>University of Michigan System</orgName> <desc> <address> <addrLine>Michigan</addrLine> <country key="US"></country> </address> <ref type="url">https://umich.edu/</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>États-Unis</country></affiliation></author><author><name sortKey="Peiris, J S Malik" sort="Peiris, J S Malik" uniqKey="Peiris J" first="J S Malik" last="Peiris">J S Malik Peiris</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author><author><name sortKey="Bruzzone, Roberto" sort="Bruzzone, Roberto" uniqKey="Bruzzone R" first="Roberto" last="Bruzzone">Roberto Bruzzone</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author><author><name sortKey="Margolis, Benjamin" sort="Margolis, Benjamin" uniqKey="Margolis B" first="Benjamin" last="Margolis">Benjamin Margolis</name><affiliation wicri:level="1"><hal:affiliation type="laboratory" xml:id="struct-136013" status="INCOMING"> <orgName>Department of Internal Medicine</orgName> <desc> <address> <addrLine>University of Michigan Medical School, 109 Zina Pitcher Place, Ann Arbor, MI 48109</addrLine> <country key="US"></country> </address> </desc> <listRelation> <relation active="#struct-24332" type="direct"></relation> <relation active="#struct-566437" type="indirect"></relation> </listRelation> <tutelles><tutelle active="#struct-24332" type="direct"><org type="institution" xml:id="struct-24332" status="VALID"> <orgName>University of Michigan [Ann Arbor]</orgName> <desc> <address> <addrLine>500 Church Street Ann Arbor, MI 48109-1090</addrLine> <country key="US"></country> </address> <ref type="url">http://www.umich.edu/</ref> </desc> <listRelation> <relation active="#struct-566437" type="direct"></relation> </listRelation> </org></tutelle><tutelle active="#struct-566437" type="indirect"><org type="regroupinstitution" xml:id="struct-566437" status="VALID"> <orgName>University of Michigan System</orgName> <desc> <address> <addrLine>Michigan</addrLine> <country key="US"></country> </address> <ref type="url">https://umich.edu/</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>États-Unis</country></affiliation></author><author><name sortKey="Nal, Beatrice" sort="Nal, Beatrice" uniqKey="Nal B" first="Béatrice" last="Nal">Béatrice Nal</name><affiliation wicri:level="1"><hal:affiliation type="institution" xml:id="struct-55925" status="VALID"> <orgName>Centre de recherche Université de Hong-Kong-Pasteur</orgName> <desc> <address> <addrLine>Hong Kong University Pasteur Research Centre - 1/F Dexter HC Man Building 8, Sassoon Road Pokfulam</addrLine> <country key="HK"></country> </address> <ref type="url">http://www.hkupasteur.hku.hk/</ref> </desc> <listRelation> <relation active="#struct-301247" type="direct"></relation> </listRelation> <tutelles><tutelle active="#struct-301247" type="direct"><org type="regroupinstitution" xml:id="struct-301247" status="VALID"> <orgName>Réseau International des Instituts Pasteur</orgName> <orgName type="acronym">RIIP</orgName> <desc> <address> <addrLine>25, rue du Dr Roux 75724 Paris Cedex 15</addrLine> <country key="FR"></country> </address> <ref type="url">https://research.pasteur.fr/ip-network</ref> </desc> </org></tutelle></tutelles></hal:affiliation><country>Hong Kong</country></affiliation></author></analytic><idno type="DOI">10.1091/mbc.E10-04-0338</idno><series><title level="j">Molecular Biology of the Cell</title><idno type="ISSN">1059-1524</idno><imprint><date type="datePub">2010-11</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"> <p>Intercellular tight junctions define epithelial apicobasal polarity and form a physical fence which protects underlying tissues from pathogen invasions. PALS1, a tight junction-associated protein, is a member of the CRUMBS3-PALS1-PATJ polarity complex, which is crucial for the establishment and maintenance of epithelial polarity in mammals. Here we report that the carboxy-terminal domain of the SARS-CoV E small envelope protein (E) binds to human PALS1. Using coimmunoprecipitation and pull-down assays, we show that E interacts with PALS1 in mammalian cells and further demonstrate that the last four carboxy-terminal amino acids of E form a novel PDZ-binding motif that binds to PALS1 PDZ domain. PALS1 redistributes to the ERGIC/Golgi region, where E accumulates, in SARS-CoV-infected Vero E6 cells. Ectopic expression of E in MDCKII epithelial cells significantly alters cyst morphogenesis and, furthermore, delays formation of tight junctions, affects polarity, and modifies the subcellular distribution of PALS1, in a PDZ-binding motif-dependent manner. We speculate that hijacking of PALS1 by SARS-CoV E plays a determinant role in the disruption of the lung epithelium in SARS patients.</p> </div></front></TEI></HAL><PubMed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis.</title><author><name sortKey="Teoh, Kim Tat" sort="Teoh, Kim Tat" uniqKey="Teoh K" first="Kim-Tat" last="Teoh">Kim-Tat Teoh</name><affiliation><nlm:affiliation>HKU-Pasteur Research Centre, Pokfulam, Hong Kong SAR China.</nlm:affiliation><wicri:noCountry code="subField">Hong Kong SAR China</wicri:noCountry></affiliation></author><author><name sortKey="Siu, Yu Lam" sort="Siu, Yu Lam" uniqKey="Siu Y" first="Yu-Lam" last="Siu">Yu-Lam Siu</name></author><author><name sortKey="Chan, Wing Lim" sort="Chan, Wing Lim" uniqKey="Chan W" first="Wing-Lim" last="Chan">Wing-Lim Chan</name></author><author><name sortKey="Schluter, Marc A" sort="Schluter, Marc A" uniqKey="Schluter M" first="Marc A" last="Schlüter">Marc A. Schlüter</name></author><author><name sortKey="Liu, Chia Jen" sort="Liu, Chia Jen" uniqKey="Liu C" first="Chia-Jen" last="Liu">Chia-Jen Liu</name></author><author><name sortKey="Peiris, J S Malik" sort="Peiris, J S Malik" uniqKey="Peiris J" first="J S Malik" last="Peiris">J S Malik Peiris</name></author><author><name sortKey="Bruzzone, Roberto" sort="Bruzzone, Roberto" uniqKey="Bruzzone R" first="Roberto" last="Bruzzone">Roberto Bruzzone</name></author><author><name sortKey="Margolis, Benjamin" sort="Margolis, Benjamin" uniqKey="Margolis B" first="Benjamin" last="Margolis">Benjamin Margolis</name></author><author><name sortKey="Nal, Beatrice" sort="Nal, Beatrice" uniqKey="Nal B" first="Béatrice" last="Nal">Béatrice Nal</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20861307</idno><idno type="pmid">20861307</idno><idno type="doi">10.1091/mbc.E10-04-0338</idno><idno type="wicri:Area/PubMed/Corpus">001626</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001626</idno><idno type="wicri:Area/PubMed/Curation">001626</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001626</idno><idno type="wicri:Area/PubMed/Checkpoint">001572</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001572</idno><idno type="wicri:Area/Ncbi/Merge">002215</idno><idno type="wicri:Area/Ncbi/Curation">002215</idno><idno type="wicri:Area/Ncbi/Checkpoint">002215</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis.</title><author><name sortKey="Teoh, Kim Tat" sort="Teoh, Kim Tat" uniqKey="Teoh K" first="Kim-Tat" last="Teoh">Kim-Tat Teoh</name><affiliation><nlm:affiliation>HKU-Pasteur Research Centre, Pokfulam, Hong Kong SAR China.</nlm:affiliation><wicri:noCountry code="subField">Hong Kong SAR China</wicri:noCountry></affiliation></author><author><name sortKey="Siu, Yu Lam" sort="Siu, Yu Lam" uniqKey="Siu Y" first="Yu-Lam" last="Siu">Yu-Lam Siu</name></author><author><name sortKey="Chan, Wing Lim" sort="Chan, Wing Lim" uniqKey="Chan W" first="Wing-Lim" last="Chan">Wing-Lim Chan</name></author><author><name sortKey="Schluter, Marc A" sort="Schluter, Marc A" uniqKey="Schluter M" first="Marc A" last="Schlüter">Marc A. Schlüter</name></author><author><name sortKey="Liu, Chia Jen" sort="Liu, Chia Jen" uniqKey="Liu C" first="Chia-Jen" last="Liu">Chia-Jen Liu</name></author><author><name sortKey="Peiris, J S Malik" sort="Peiris, J S Malik" uniqKey="Peiris J" first="J S Malik" last="Peiris">J S Malik Peiris</name></author><author><name sortKey="Bruzzone, Roberto" sort="Bruzzone, Roberto" uniqKey="Bruzzone R" first="Roberto" last="Bruzzone">Roberto Bruzzone</name></author><author><name sortKey="Margolis, Benjamin" sort="Margolis, Benjamin" uniqKey="Margolis B" first="Benjamin" last="Margolis">Benjamin Margolis</name></author><author><name sortKey="Nal, Beatrice" sort="Nal, Beatrice" uniqKey="Nal B" first="Béatrice" last="Nal">Béatrice Nal</name></author></analytic><series><title level="j">Molecular biology of the cell</title><idno type="eISSN">1939-4586</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Epithelial Cells (cytology)</term><term>Epithelial Cells (metabolism)</term><term>Epithelial Cells (virology)</term><term>Epithelium (growth & development)</term><term>Epithelium (metabolism)</term><term>Glutathione Transferase</term><term>HEK293 Cells</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Immunoblotting</term><term>Luminescent Proteins (genetics)</term><term>Luminescent Proteins (metabolism)</term><term>Membrane Proteins (genetics)</term><term>Membrane Proteins (metabolism)</term><term>Microscopy, Fluorescence</term><term>Morphogenesis</term><term>Nucleoside-Phosphate Kinase (genetics)</term><term>Nucleoside-Phosphate Kinase (metabolism)</term><term>Protein Binding</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>SARS Virus (metabolism)</term><term>SARS Virus (physiology)</term><term>Tight Junctions (metabolism)</term><term>Tight Junctions (virology)</term><term>Two-Hybrid System Techniques</term><term>Vero Cells</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules HEK293</term><term>Cellules Vero</term><term>Cellules épithéliales (cytologie)</term><term>Cellules épithéliales (métabolisme)</term><term>Cellules épithéliales (virologie)</term><term>Glutathione transferase</term><term>Humains</term><term>Immunotransfert</term><term>Interactions hôte-pathogène</term><term>Jonctions serrées (métabolisme)</term><term>Jonctions serrées (virologie)</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Microscopie de fluorescence</term><term>Morphogenèse</term><term>Nucleoside phosphate kinase (génétique)</term><term>Nucleoside phosphate kinase (métabolisme)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Protéines luminescentes (génétique)</term><term>Protéines luminescentes (métabolisme)</term><term>Protéines membranaires (génétique)</term><term>Protéines membranaires (métabolisme)</term><term>Sites de fixation</term><term>Techniques de double hybride</term><term>Virus du SRAS (métabolisme)</term><term>Virus du SRAS (physiologie)</term><term>Épithélium (croissance et développement)</term><term>Épithélium (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Luminescent Proteins</term><term>Membrane Proteins</term><term>Nucleoside-Phosphate Kinase</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Luminescent Proteins</term><term>Membrane Proteins</term><term>Nucleoside-Phosphate Kinase</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Épithélium</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Cellules épithéliales</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Epithelial Cells</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Epithelium</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Nucleoside phosphate kinase</term><term>Protéines de fusion recombinantes</term><term>Protéines de l'enveloppe virale</term><term>Protéines luminescentes</term><term>Protéines membranaires</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Epithelial Cells</term><term>Epithelium</term><term>SARS Virus</term><term>Tight Junctions</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellules épithéliales</term><term>Jonctions serrées</term><term>Nucleoside phosphate kinase</term><term>Protéines de fusion recombinantes</term><term>Protéines de l'enveloppe virale</term><term>Protéines luminescentes</term><term>Protéines membranaires</term><term>Virus du SRAS</term><term>Épithélium</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Cellules épithéliales</term><term>Jonctions serrées</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Epithelial Cells</term><term>Tight Junctions</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>HEK293 Cells</term><term>Host-Pathogen Interactions</term><term>Humans</term><term>Immunoblotting</term><term>Microscopy, Fluorescence</term><term>Morphogenesis</term><term>Protein Binding</term><term>Two-Hybrid System Techniques</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HEK293</term><term>Cellules Vero</term><term>Glutathione transferase</term><term>Humains</term><term>Immunotransfert</term><term>Interactions hôte-pathogène</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Microscopie de fluorescence</term><term>Morphogenèse</term><term>Sites de fixation</term><term>Techniques de double hybride</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Intercellular tight junctions define epithelial apicobasal polarity and form a physical fence which protects underlying tissues from pathogen invasions. PALS1, a tight junction-associated protein, is a member of the CRUMBS3-PALS1-PATJ polarity complex, which is crucial for the establishment and maintenance of epithelial polarity in mammals. Here we report that the carboxy-terminal domain of the SARS-CoV E small envelope protein (E) binds to human PALS1. Using coimmunoprecipitation and pull-down assays, we show that E interacts with PALS1 in mammalian cells and further demonstrate that the last four carboxy-terminal amino acids of E form a novel PDZ-binding motif that binds to PALS1 PDZ domain. PALS1 redistributes to the ERGIC/Golgi region, where E accumulates, in SARS-CoV-infected Vero E6 cells. Ectopic expression of E in MDCKII epithelial cells significantly alters cyst morphogenesis and, furthermore, delays formation of tight junctions, affects polarity, and modifies the subcellular distribution of PALS1, in a PDZ-binding motif-dependent manner. We speculate that hijacking of PALS1 by SARS-CoV E plays a determinant role in the disruption of the lung epithelium in SARS patients.</div></front></TEI></PubMed></double></record>Pour manipuler ce document sous Unix (Dilib)
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