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

Teoh, Kim-Tat; Siu, Yu-Lam; Chan, Wing-Lim; Schlüter, Marc A.; Liu, Chia-Jen; Peiris, J. S. Malik; Bruzzone, Roberto; Margolis, Benjamin; Nal, Béatrice

In a recent large-scale genome-wide screen, Obenauer and coworkers have discovered the presence of a PBM at the CT of NS1 protein of the H5N1 avian influenza A virus (Obenauer et al., 2006). Presence of this PBM was shown to be detrimental virulence factor in mice (Jackson et al., 2008). Interestingly, similar PBM have been characterized and identified at the CT of several viral oncoproteins, namely adenovirus type 9 E4-ORF1, human T-cell leukemia virus type 1 Tax1, and human papillomavirus E6. These viral PBM bind to PDZ domain-containing proteins involved in the regulation of epithelial cell polarity and induced epithelial-to-mesenchyme transformation in a PBM–dependent manner (reviewed in Javier, 2008; Liu and Baleja, 2008; Thomas et al., 2008; Tungteakkhun et al., 2008; Wise-Draper and Wells, 2008; Tomaic et al., 2009). Likewise, SARS-CoV may interfere with epithelial apicobasal polarity through molecular interactions involving the E CT domain.