Author: 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
Title: The SARS Coronavirus E Protein Interacts with PALS1 and Alters Tight Junction Formation and Epithelial Morphogenesis Document date: 2010_11_15
ID: ufw13pjx_50
Snippet: Because both antibodies recognizing SARS-E and PALS1 were raised in rabbits, our data provide only indirect evidence for colocalization of these two proteins. Thus, in a separate series of experiments, we addressed this issue by transfecting Vero E6 epithelial cells with EYFP-tagged PALS1 and HA-E (wt). As expected, we observed colocalization of EYFP-PALS1 and HA-E (wt) in the perinuclear region in Vero E6 transfected cells (Supplemental Figure S.....
Document: Because both antibodies recognizing SARS-E and PALS1 were raised in rabbits, our data provide only indirect evidence for colocalization of these two proteins. Thus, in a separate series of experiments, we addressed this issue by transfecting Vero E6 epithelial cells with EYFP-tagged PALS1 and HA-E (wt). As expected, we observed colocalization of EYFP-PALS1 and HA-E (wt) in the perinuclear region in Vero E6 transfected cells (Supplemental Figure S1, panel A and B, white color arrow). Altogether, these findings implicate that E interacts with PALS1 and most likely retains PALS1 at the virus assembly site, both in infected and transfected cells.
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