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Dr Stephen Graham

Dr Stephen Graham

Sir Henry Dale Fellow and University Lecturer

Division of Virology

Molecular mechanisms of membrane trafficking and viral infection

Department of Pathology
University of Cambridge
Tennis Court Road
Cambridge
CB2 1QP

Office Phone: +44 (0)1223 336920

Biography:

In 2018 Stephen collaborated with the Wellcome Trust as part of their Researcher Stories initiative. Read the full article at the Wellcome Trust website or watch the video below.

Research themes

Virology:

Molecular mechanisms of membrane trafficking and viral infection

Division

Virology:

Research Interests

Graham Research 2

After replication viruses face a logistical challenge: How do they ensure progeny virions are efficiently released from host cells? While human pathogens such as herpes simplex virus and vaccinia virus (the smallpox vaccine) are known to subvert host-cell intracellular membrane trafficking pathways in order to leave infected cells, little is known about the molecular mechanisms used to achieve this. We are using a combination of cell biology, biochemistry, biophysics and structural biology to define the interactions between host cell and virus proteins that enable enveloped viruses to exit infected cells and thereby spread the infection to new hosts.

In order to establish a fruitful infection viruses must evade the immune surveillance systems of the host. I am interested in how viruses directly interfere with innate and intrinstic immune responses during infection, how they modify the surface of infected cells to minimise the adaptive immune response, and how some viruses have even managed to hijack mammalian innate immune proteins and ‘re-program’ these to suit the needs of the virus.

  • Group Members: 
    Susanna Colaco, Tomasz Benedyk, Ben Butt, Kamal Nahas, Henry Barrow
  • Visiting Scientists:
    Natalia Barbosa (University of São Paulo)

Key Publications

    1. S.C. Graham, B. Nagar, G.G. Privé, J.E. Deane (2019) Molecular models should not be published without the corresponding atomic coordinates. Proceedings of the National Academy of Sciences of the USA, 116: 11099–11100
      doi: 10.1073/pnas.1904409116
    2. C. Gao, M.A. Pallett, T.I. Croll, G.L. Smith, S.C. Graham (2019) Molecular basis of cullin-3 (Cul3) ubiquitin ligase subversion by vaccinia virus protein A55. Journal of Biological Chemistry, 294: 6416–6429
      doi: 10.1074/jbc.RA118.006561
    3. J.M. Alves, M. Carneiro, J.Y. Cheng, A. Lemos de Matos, M.M. Rahman, L. Loog, P.F. Campos, N. Wales, A. Eriksson, A. Manica, T. Strive, S.C. Graham, S. Afonso, D.J. Bell, L. Belmont, J.P. Day, S.J. Fuller, S. Marchandeau, W.J. Palmer, G. Queney, A.K. Surridge, F.G. Vieira, G. McFadden, R. Nielsen, M.T.P. Gilbert, P.J. Esteves, N. Ferrand, F.M. Jiggins (2019) Parallel adaptation of rabbit populations to myxoma virus. Science, 363: 1319–1326
      doi: 10.1126/science.aau7285
    4. M.R. Hunter, G.G. Hesketh, T.H. Benedyk, A.C. Gingras, S.C. Graham (2018) Proteomic and biochemical comparison of the cellular interaction partners of human VPS33A and VPS33B. Journal of Molecular Biology, 430: 2153–2163
      doi: 10.1016/j.jmb.2018.05.019
    5. A. Albecka, D.J. Owen, L. Ivanova, J. Brun, R. Liman, L. Davies, M.F. Ahmed, S. Colaco, M. Hollinshead, S.C. Graham^ and C.M. Crump^ (2017) Dual function of the pUL7-pUL51 tegument protein complex in HSV-1 infection. Journal of Virology, 81: e02196-16
      doi: 10.1128/JVI.02196-16
    6. J. Muenzner, L.M. Traub, B.T. Kelly^, S.C. Graham^ (2017) Cellular and viral peptides bind multiple sites on the N-terminal domain of clathrin. Traffic, 18: 44–57
      doi: 10.1111/tra.12457

     (^Joint corresponding authors)