Virus assembly and egress
Colin Crump is accepting applications for PhD students.
Departments and Institutes
- Royal Society University Research Fellow
My laboratory studies the assembly and egress of viruses with a focus on the cellular mechanisms utilised and modified by viruses during their replication. We primarily study two families of important human pathogens: herpesviruses and polyomaviruses.
Herpesviruses are large (~200nm) and complex enveloped dsDNA viruses that are ubiquitous pathogens of vertebrates and establish life-long latent infections in their hosts. Infections by the nine known human herpesviruses are associated with many serious diseases including certain lymphomas and life-threatening conditions in immuno-compromised patients. The assembly of herpesviruses is known to involve the budding of nucleocapsids, together with the complex layer of tegument proteins, at membranes derived from post-Golgi endocytic compartments. Once formed, the membrane-bound compartments containing the mature virions undergo exocytosis to release infectious viruses from the cell.
Polyomaviruses are small (~45nm) non-enveloped dsDNA viruses that are ubiquitous pathogens in humans and can establish life-long persistent infections with periodic virus shedding. While polyomavirus infections are generally benign in immuno-competent hosts they are known to cause serious disease in immuno-compromised patients including haemorrhagic cystitis, polyomavirus-associated nephropathy, Merkel cell carcinoma, and progressive multifocal leukoencephalopathy.
Examples of current ongoing projects in the lab are:
- Developing super-resolution microscopy to image the structure and assembly of viruses in cells
- Viral and cellular mechanisms of herpes simplex virus envelopment
- The role of herpesvirus tegument proteins in virus assembly and egress
- Secretion and release of herpesviruses from infected cells
- Cellular pathways involved in polyomavirus egress
- Zenner HL, Mauricio R, Banting G and Crump CM. (2013) Herpes simplex virus type-1 counteracts tetherin restriction via its virion host shutoff activity. J. Virol. doi: 10.1128/JVI.02167-13
- Griffiths SJ, Koegl M, Boutell C, Zenner HL, Crump CM, Pica F, Gonzalez O, Friedel CC, Barry G, Martin K, Craigon MH, Chen R, Kaza LN, Fossum E, Fazakerley JK, Efstathiou S, Volpi A, Zimmer R, Ghazal P, and Haas J. (2013) A Systematic Analysis of Host Factors Reveals a Med23- Interferon-l Regulatory Axis against Herpes Simplex Virus Type 1 Replication. PLoS Pathogens 9(8): e1003514
- Ren Y, Bell S, Zenner HL, Lau SYK, and Crump CM. (2012) Glycoprotein M is important for the efficient incorporation of glycoprotein H-L into herpes simplex virus type 1 particles. J. Gen. Virol. 93: 319-329
- Svobodova S, Bell S and Crump CM. (2012) Analysis of the interaction between the essential herpes simplex virus 1 tegument proteins VP16 and VP1/2. J. Virol. 86: 473-483
- Zenner HL, Yoshimura S, Barr FA and Crump CM. (2011) Analysis of Rab GTPase-Activating Proteins Indicates that Rab1a/b and Rab43 Are Important for Herpes Simplex Virus 1 Secondary Envelopment. J Virol. 85:8012-21
- Pawliczek T, and Crump CM. (2009) Herpes simplex virus type-1 production requires a functional ESCRT-III complex, but is independent of TSG101 and/or ALIX expression. J. Virol. 83 11254-11264