Studies on the interaction of HSV-1 multifunctional protein ICP27 with the nuclear pore complex proteins.
PhD thesis, University of Glasgow.
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Herpes simplex virus (HSV-1) ICP27 is a multifunctional immediate early (IE) protein, required for expression of several early and late genes and acts at transcriptional and posttranscriptional levels. ICP27 contains both a nuclear localization signal and a nuclear export signal and shuttles between the nucleus and the cytoplasm. It interacts directly with various cellular proteins including REF and cellular mRNA export receptor TAP to export viral mRNAs. However other transport mechanisms may also be employed. All transport across the nuclear envelope must occur via the nuclear pore complex, which consists of proteins called nucleoporins (NUPs). NUPs act to regulate the transport cargos by interaction with mRNA bound proteins and transport receptors, karyopherins. To further explore the transport requirements for ICP27 and viral mRNA export, we investigated its direct interaction with nucleoporins and show that ICP27 interacts directly with nucleoporins tested, in vitro and in wild type and mutant virus infected cells and from RNase I treated and untreated cell extracts indicating that this interaction is not mediated via RNA. Implications of this interaction is discussed in this thesis.
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