The SARS Coronavirus E Protein Interacts with PALS1 and Alters Tight Junction Formation and Epithelial Morphogenesis

• DOI: 10.1091/mbc.e10-04-0338
• Publication Date: 2010-09-23T04:39:46Z
• Authors: Kim-Tat Teoh; Yu-Lam Siu; Wing-Lim Chan; Marc A. Schlüter; Chia-Jen Liu; J. S. Malik Peiris; Roberto Bruzzone; Benjamin Margolis; Béatrice Nal
• Keywords: PDZ domain; Cell polarity; Epithelial polarity; Claudin; Immunoprecipitation; Polarity (international relations)

Intercellular tight junctions define epithelial apicobasal polarity and form a physical fence which protects underlying tissues from pathogen invasions. PALS1, junction-associated protein, is member of the CRUMBS3-PALS1-PATJ complex, crucial for establishment maintenance in mammals. Here we report that carboxy-terminal domain SARS-CoV E small envelope protein (E) binds to human PALS1. Using coimmunoprecipitation pull-down assays, show interacts with PALS1 mammalian cells further demonstrate last four amino acids novel PDZ-binding motif PDZ domain. redistributes ERGIC/Golgi region, where accumulates, SARS-CoV-infected Vero E6 cells. Ectopic expression MDCKII significantly alters cyst morphogenesis and, furthermore, delays formation junctions, affects polarity, modifies subcellular distribution motif-dependent manner. We speculate hijacking by plays determinant role disruption lung epithelium SARS patients.