[{"key":"dc.contributor.author","value":"Nie, Yingchao","language":null},{"key":"dc.date.accessioned","value":"2010-02-23T15:10:39Z","language":null},{"key":"dc.date.available","value":"2010-02-23T15:10:39Z","language":null},{"key":"dc.date.issued","value":"2010","language":null},{"key":"dc.identifier.uri","value":"http:\/\/hdl.handle.net\/2429\/20752","language":null},{"key":"dc.description.abstract","value":"Autographa californica multiple nucleopolyhedrovirus expresses two major\ntransregulatory proteins IE0 and IE1 immediately upon infection. IE0 differs from IE1\nonly by 54 additional N-terminal amino acids (aa). Either IE0 or IE1 can support viral\nreplication; however both are required for a wild-type infection. It is unknown what the\ndifferent functions of IE0 and IE1. Both IE0 and IE1 can transactivate viral early genes\nand support viral DNA replication. It is therefore hypothesized that by the addition of Nterminal 54 aa, IE0 acquires different transactivation activity on viral genes and interacts with different viral or host partners. To test this hypothesis, functional comparisons between IE0 and IE1 and the identification of their interaction partners in infected cells were performed.\n\nComparisons of subcellular localization and transactivation activities between IE0 and IE1 showed no difference. However analyses of the nucleocapsid content of occlusion derived virions (ODV) revealed that IE0 and IE1 appear to regulate the number of nucleocapsids per ODV. Deletion within the IE0 specific N-terminal 54 aa did not affect IE0 transactivation dramatically but reduced its ability to support viral DNA replication.\n\nAnalyses of interacting proteins did not identify any proteins that were specific to either\nwith IE0 or IE1. However, the viral protein AC16 (BV\/ODV-E26) was shown to bind to\nboth IE0 and IE1 via a binding domain at IE1 72-99 aa. Mutation of the binding domain\nenhanced budded virus (BV) production by viruses expressing only IE0 but not IE1.\nDeletion of ac16 however resulted in increased levels of IE0 relative to IE1 as the only\nobservable impact. These results would therefore indicate that AC16 regulates ie0\nexpression. Deletion of ac16 and the overlapping gene ac17, interestingly resulted in a\nsignificant delay of viral gene expression for up to 12 hours. However, the delay of viral\ngene expression was only observed with BV-infected cells and not in cells infected by\ntransfecting viral DNA. AC16 and AC17 are therefore critical for rapid gene expression\nduring the very early events of infection, and highlight the fact that proteins interacting\nwith IE0 and IE1 play key roles in baculovirus biology.","language":"en"},{"key":"dc.language.iso","value":"eng","language":"en"},{"key":"dc.publisher","value":"University of British Columbia","language":null},{"key":"dc.rights","value":"Attribution-NonCommercial-NoDerivatives 4.0 International","language":null},{"key":"dc.rights.uri","value":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/","language":null},{"key":"dc.title","value":"Functional comparison and analysis of protein-protein interactions of Autographa californica multiple nucleopolyhedrovirus transregulatory proteins IE0 and IE1","language":"en"},{"key":"dc.type","value":"Text","language":null},{"key":"dc.degree.name","value":"Doctor of Philosophy - PhD","language":"en"},{"key":"dc.degree.discipline","value":"Plant Science","language":"en"},{"key":"dc.degree.grantor","value":"University of British Columbia","language":null},{"key":"dc.date.graduation","value":"2010-05","language":"en"},{"key":"dc.type.text","value":"Thesis\/Dissertation","language":"en"},{"key":"dc.description.affiliation","value":"Land and Food Systems, Faculty of","language":null},{"key":"dc.degree.campus","value":"UBCV","language":"en"},{"key":"dc.description.scholarlevel","value":"Graduate","language":"en"}]