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• W87380010 abstract "NSP4, encoded by rotavirus genome segment 10 has been shown to be atransmembrane, endoplasmic reticulum (ER) specific N-linked glycoprotein.Consistent with its localization to the ER membrane, NSP4 was first shown to have arole in the morphogenesis of the infectious virion. The protein has also been reportedto have cytotoxic activity when applied extracellularly to cells. Consequently it hasbeen earmarked as an enterotoxin being secreted from virus-infected cells to causeearly cellular pathology in the gut.The effect of expressing the NSP4 protein of group A rotaviruses in cells hasbeen studied. It led to the rapid appearance of long cytoplasmic extrusions.Site-directed mutagenesis was used to block N-linked glycosylation at both of theknown glycosylation sites near the amino terminus of NSP4. This revealed that theNSP4 induced formation of the cytoplasmic extrusions was dependent on theprotein’s ability to become fully glycosylated. The cytoplasmic extrusions seen incells expressing glycosylated NSP4 were also evident in virus-infected cells.Using real-time confocal microscopy a dynamic elongation of the cytoplasmicextrusions with a growth speed of 2 μm/min was observed in virus-infected cells.The cytoplasmic extrusions were found to contain β-tubulin and F-actin. Inhibitingtheir polymerization prevented the formation of the extrusions from virus-infectedcells. Functional studies using Cell Tracker dyes showed that the cytoplasmicextrusions could disseminate vesicles from virus-infected cells onto the plasmamembrane surface of uninfected cells. The vesicles were then found in the interior ofthe uninfected cells. Mono-specific antibody to NSP4 revealed the presence of theprotein in the vesicles suggesting that the cytoplasmic extrusions facilitated the directcell-cell spread of NSP4.The effect of NSP4 expression on the microtubular network of cells wasanalysed. It was found that NSP4 de-polymerized the microtubular network from thecentre of cells and promoted the assembly of microtubules at the periphery of thecells in a glycosylation independent manner. Similar de-polymerization andre-assembly of the microtubules was observed in the virus-infected cells.Interestingly in the presence of nocodazole, tubular structures containing tubulin andviral proteins excluding NSP4 were found in virus-infected cells.A YFP-PCA assay was established to screen for cellular partners of NSP4. Thefunctionality and the sensitivity of the assay were examined, but only two falsepositive colonies were isolated in the first screening.In conclusion, the function of glycosylated and unglycosylated NSP4 wasexamined with the former possessing the ability to promote the formation of thecytoplasmic extrusions from cells and both being capable of disrupting themicrotubular network indicating that two forms of NSP4 play different roles in NSP4function. The cytoplasmic extrusions seen in our studies may be relevant to rotavirusinfection and pathogenesis." @default.
• W87380010 created "2016-06-24" @default.
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• W87380010 date "2010-09-01" @default.
• W87380010 modified "2023-09-23" @default.
• W87380010 title "Functional studies of the group A rotavirus non-structural protein NSP4" @default.
• W87380010 hasPublicationYear "2010" @default.
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