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

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.
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Submitted on : Monday, December 13, 2010 - 4:57:59 AM
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Kim-Tat Teoh, Yu-Lam Siu, Wing-Lim Chan, Marc A Schlüter, Chia-Jen Liu, et al.. The SARS coronavirus E protein interacts with PALS1 and alters tight junction formation and epithelial morphogenesis.. Molecular Biology of the Cell, American Society for Cell Biology, 2010, 21 (22), pp.3838-52. ⟨10.1091/mbc.E10-04-0338⟩. ⟨pasteur-00545808⟩

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