Postgrad LIVE! Study Fairs

Birmingham | Edinburgh | Liverpool | Sheffield | Southampton | Bristol

University of Liverpool Featured PhD Programmes
University College London Featured PhD Programmes
Birkbeck, University of London Featured PhD Programmes
University of Kent Featured PhD Programmes
Birkbeck, University of London Featured PhD Programmes

Molecular mechanisms of herpesviral infection

  • Full or part time
  • Application Deadline
    Applications accepted all year round
  • Self-Funded PhD Students Only
    Self-Funded PhD Students Only

Project Description

Herpes viruses are known to cause a wide range of human diseases, ranging from simple cold sores to cancer, Kaposi Sarcoma. Kaposi Sarcoma, for example, is a type of cancer which affects immunocompromised patients and is endemic in Africa, where it is linked with the spread of HIV infection and AIDS. Herpes viruses take over the normal cellular mechanisms, for example mRNA nuclear export, and force cells to produce viruses instead. Understanding these processes at molecular level, how viral proteins interact with host cell proteins, may help to create new drugs which block virus replication, and thus relieve or prevent diseases associated with herpes viruses.

The student will study how exactly ICP27 and other signature proteins coded by herpes viruses (HSV-1 and KSHV) interact with cellular proteins, leading to herpesvirus hijacking human cell. A wide range of biochemical and biophysical methods will be used to address these questions comprehensively. The methods will include molecular biology, protein expression, purification and characterization using biochemical and biophysical techniques (e.g. column chromatography, circular dichroism, SPR, ITC, X-ray crystallography and NMR spectroscopy). The project will be carried out in the multidisciplinary environment of the Manchester Institute of Biotechnology and supervised by Dr Alexander Golovanov. The student will receive extensive training in molecular and structural biology. The School of Chemistry has state-of-the-art research facilities, including crystallography and NMR equipped with multichannel 500, 600 and 800 MHz spectrometers with cyroprobes.

Contact for further Information:

Dr Alexander Golovanov

Funding Notes

Applications are invited from self-funded students. For UK/EU tuition fees are £15,000 and International are £29,500 for 2018/19 academic year.

Candidates are expected to hold (or be about to obtain) a minimum upper second class honours degree (or the overseas equivalent) in a related area / subject. Candidates with experience in molecular biology or with an interest in structural biology and NMR spectroscopy are encouraged to apply.

Please select PhD Biological Chemistry on the online application form.

References

Tunnicliffe RB, Collins RF, Ruiz Nivia HD, Sandri-Goldin RM, Golovanov AP. The ICP27 Homology Domain of the Human Cytomegalovirus Protein UL69 Adopts a Dimer-of-Dimers Structure. MBio. 2018 Jun 19;9(3). pii: e01112-18. doi: 10.1128/mBio.01112-18.

Tunnicliffe RB, Lockhart-Cairns MP, Levy C, Mould AP, Jowitt TA, Sito H, Baldock C, Sandri-Goldin RM, Golovanov AP. The herpes viral transcription factor ICP4 forms a novel DNA recognition complex. Nucleic Acids Res. 2017 Jul 27;45(13):8064-8078. doi: 10.1093/nar/gkx419.

Tunnicliffe RB, Schacht M, Levy C, Jowitt TA, Sandri-Goldin RM, Golovanov AP. The structure of the folded domain from the signature multifunctional protein ICP27 from herpes simplex virus-1 reveals an intertwined dimer. Sci Rep. 2015 Jun 11;5:11234. doi: 10.1038/srep11234.

Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. PLoS Pathog. 2014 Feb 13;10(2):e1003907. doi: 10.1371/journal.ppat.1003907.

Tian X, Devi-Rao G, Golovanov AP, Sandri-Goldin RM. The interaction of the cellular export adaptor protein Aly/REF with ICP27 contributes to the efficiency of herpes simplex virus 1 mRNA export. J Virol. 2013 Jul;87(13):7210-7. doi: 10.1128/JVI.00738-13.

Email Now

Insert previous message below for editing? 
You haven’t included a message. Providing a specific message means universities will take your enquiry more seriously and helps them provide the information you need.
Why not add a message here
* required field
Send a copy to me for my own records.

Your enquiry has been emailed successfully





FindAPhD. Copyright 2005-2018
All rights reserved.