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Article: The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis

TitleThe SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis
Authors
KeywordsAnimal Cell
Article
Carboxy Terminal Sequence
Cell Polarity
Cellular Distribution
Controlled Study
Cyst
Human
Human Cell
Immunoprecipitation
Lung Alveolus Epithelium
Mammal Cell
Nonhuman
Pdz Domain
Priority Journal
Protein Motif
Protein Protein Interaction
Sars Coronavirus
Tight Junction
Virus Morphogenesis
Issue Date2010
PublisherAmerican Society for Cell Biology. The Journal's web site is located at http://www.molbiolcell.org/
Citation
Molecular Biology Of The Cell, 2010, v. 21 n. 22, p. 3838-3852 How to Cite?
AbstractIntercellular 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. © 2010 K.-T. Teoh et al.
Persistent Identifierhttp://hdl.handle.net/10722/132669
ISSN
2015 Impact Factor: 4.037
2015 SCImago Journal Rankings: 3.665
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Research Fund for the Control of Infectious Diseases08070992
International Network of Pasteur Institutes
Area of Excellence Scheme of the UniversityAoE/M-12/06
National Institutes of HealthDK58208
DK69605
The University of Hong Kong
Funding Information:

We thank Nadege Lagarde and Dr. Jean-Michel Garcia (HKU-Pasteur Research Centre) for treatment of images acquired by confocal microscopy, preparation of cysts, 3D models, and advice on statistical analysis, respectively. We thank Dr. Michael Chan and Dr. Renee Chan (Department of Microbiology, The University of Hong Kong) for providing the wd-NHBE cells and Dr. John Nicholls and Kevin Fung (Department of Pathology, the University of Hong Kong) for immunohistochemistry analysis of post mortem biopsies from SARS-CoV-infected patients. We acknowledge the Core Imaging Facility of the Faculty of Medicine of the University of Hong Kong. We also thank Professor Yu-lung Lau (Department of Pediatrics and Adolescent Medicine, The University of Hong Kong) for his continuous encouragement during this project. This work was supported by the Research Fund for the Control of Infectious Diseases (Grant Ref#08070992), the RESPARI project of the International Network of Pasteur Institutes, and the Area of Excellence Scheme of the University Grants Committee (Grant AoE/M-12/06) (to B.N.) and National Institutes of Health grants (DK58208, and DK69605) (to B.M.). K.-T.T was a Ph.D. student supported by The University of Hong Kong.

References
Grants

 

DC FieldValueLanguage
dc.contributor.authorTeoh, KTen_HK
dc.contributor.authorSiu, YLen_HK
dc.contributor.authorChan, WLen_HK
dc.contributor.authorSchlüter, MAen_HK
dc.contributor.authorLiu, CJen_HK
dc.contributor.authorPeiris, JSMen_HK
dc.contributor.authorBruzzone, Ren_HK
dc.contributor.authorMargolis, Ben_HK
dc.contributor.authorNal, Ben_HK
dc.date.accessioned2011-03-28T09:28:04Z-
dc.date.available2011-03-28T09:28:04Z-
dc.date.issued2010en_HK
dc.identifier.citationMolecular Biology Of The Cell, 2010, v. 21 n. 22, p. 3838-3852en_HK
dc.identifier.issn1059-1524en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132669-
dc.description.abstractIntercellular 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. © 2010 K.-T. Teoh et al.en_HK
dc.languageengen_US
dc.publisherAmerican Society for Cell Biology. The Journal's web site is located at http://www.molbiolcell.org/en_HK
dc.relation.ispartofMolecular Biology of the Cellen_HK
dc.subjectAnimal Cellen_US
dc.subjectArticleen_US
dc.subjectCarboxy Terminal Sequenceen_US
dc.subjectCell Polarityen_US
dc.subjectCellular Distributionen_US
dc.subjectControlled Studyen_US
dc.subjectCysten_US
dc.subjectHumanen_US
dc.subjectHuman Cellen_US
dc.subjectImmunoprecipitationen_US
dc.subjectLung Alveolus Epitheliumen_US
dc.subjectMammal Cellen_US
dc.subjectNonhumanen_US
dc.subjectPdz Domainen_US
dc.subjectPriority Journalen_US
dc.subjectProtein Motifen_US
dc.subjectProtein Protein Interactionen_US
dc.subjectSars Coronavirusen_US
dc.subjectTight Junctionen_US
dc.subjectVirus Morphogenesisen_US
dc.titleThe SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesisen_HK
dc.typeArticleen_HK
dc.identifier.emailPeiris, JSM: malik@hkucc.hku.hken_HK
dc.identifier.emailBruzzone, R: bruzzone@hkucc.hku.hken_HK
dc.identifier.emailNal, B: bnal@hkucc.hku.hken_HK
dc.identifier.authorityPeiris, JSM=rp00410en_HK
dc.identifier.authorityBruzzone, R=rp01442en_HK
dc.identifier.authorityNal, B=rp00541en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1091/mbc.E10-04-0338en_HK
dc.identifier.pmid20861307-
dc.identifier.pmcidPMC2982091-
dc.identifier.scopuseid_2-s2.0-78649684164en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-78649684164&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume21en_HK
dc.identifier.issue22en_HK
dc.identifier.spage3838en_HK
dc.identifier.epage3852en_HK
dc.identifier.eissn1939-4586-
dc.identifier.isiWOS:000284216800036-
dc.publisher.placeUnited Statesen_HK
dc.relation.projectControl of Pandemic and Inter-pandemic Influenza-
dc.identifier.scopusauthoridTeoh, KT=25637993600en_HK
dc.identifier.scopusauthoridSiu, YL=25227033200en_HK
dc.identifier.scopusauthoridChan, WL=37057154900en_HK
dc.identifier.scopusauthoridSchlüter, MA=25423165200en_HK
dc.identifier.scopusauthoridLiu, CJ=7409785798en_HK
dc.identifier.scopusauthoridPeiris, JSM=7005486823en_HK
dc.identifier.scopusauthoridBruzzone, R=7006793327en_HK
dc.identifier.scopusauthoridMargolis, B=7006152726en_HK
dc.identifier.scopusauthoridNal, B=6506672380en_HK

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