Dr David Bhella

  • Programme Leader (Centre for Virus Research)

telephone: 01413303685
email: David.Bhella@glasgow.ac.uk

Research interests

CVR logo

The structural components of viruses represent an intriguing area of study for the structural biologist. In their replication cycle, viruses must generate a protective shell (or capsid) to ferry their genome between hosts. These structural proteins may also be required to facilitate entry to and exit from the host cell, as well as packaging the genome and the necessary functional proteins. In many cases structural proteins are also involved in replication and integration of the viral genome. Thus virus particles are dynamic entities, molecular machines evolved to provide a robust protective shell for the genome and capable of undergoing dramatic conformational changes upon infection of a host cell and in response to specific environmental stimuli.

The fact that many viruses generate their capsids from only one or two protein species makes them all the more remarkable. Viruses attain this level of economy by assembling their capsids in a highly symmetrical manner making these structures not only scientifically interesting but also beautiful.

This group applies the techniques of electron-cryomicroscopy and image analysis to the study of viruses. We are equipped with a high-performance JEOL 2200 cryo-microscope suitable both for high-resolution analysis of symmetrical entities e.g. icosahedral and helical viruses, and for tomographic reconstruction of asymmetrical objects such as enveloped viruses and virus-infected cells. We also have facilities for correlative cryo-fluorescence imaging, high-pressure freezing, automated freeze substitution and cryo-ultramicrotomy. The establishment of these capabilities within a dedicated virus research laboratory gives us an exciting opportunity to visualise the process of virus infection at cellular scale and macromolecular resolution.

We are currently engaged in research into caliciviruses, influenzaviruses and paramyxoviruses (respiratory syncytial virus, parainfluenza viruses and measles virus).


Grants and Awards listed are those received whilst working with the University of Glasgow.

  • Characterisation of Zika virus neutralisation and virion structure by cryogenic electron microscopy and 3D reconstruction.
    Medical Research Council
    2016 - 2017
  • A structure analysis of the intact virion and replicative complexes of human respiratory syncytial virus
    Medical Research Council
    2014 - 2017
  • Initiation and regulation of RSV mRNA transcription and genome replication
    National Institutes of Health (NIAID)
    2014 - 2015


List by: Type | Date

Jump to: 2015 | 2014 | 2013 | 2012 | 2011 | 2010 | 2009 | 2008 | 2007 | 2006 | 2004 | 2003 | 2002 | 2000 | 1999
Number of items: 34.


Bhella, D. (2015) The role of cellular adhesion molecules in virus attachment and entry. Philosophical Transactions of the Royal Society B: Biological Sciences, 370(1661), (doi:10.1098/rstb.2014.0035) (PMID:25533093) (PMCID:PMC4275905)

Fan, W. H., Robertson, A. P.E., McElwee, M., Bhella, D., Rixon, F. J., and Lauder, R. (2015) The large tegument protein pUL36 is essential for formation of the capsid vertex-specific component at the capsid-tegument interface of herpes simplex virus 1. Journal of Virology, 89(3), pp. 1502-1511. (doi:10.1128/JVI.02887-14) (PMID:25410861) (PMCID:PMC4300765)

McGonigle, R., Yap, W. B., Ong, S. T., Gatherer, D., Bakker, S. E., Tan, W. S., and Bhella, D. (2015) An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles. Journal of Structural Biology, 189(2), pp. 73-80. (doi:10.1016/j.jsb.2014.12.006)


Hacker, C., Howell, M., Bhella, D., and Lucocq, J. (2014) Strategies for maximizing ATP supply in the microsporidian Encephalitozoon cuniculi: direct binding of mitochondria to the parasitophorous vacuole and clustering of the mitochondrial porin VDAC. Cellular Microbiology, 16(4), pp. 565-579. (doi:10.1111/cmi.12240) (PMID:24245785) (PMCID:PMC4233961)


Bakker, S. E., Duquerroy, S., Galloux, M., Loney, C., Conner, E., Eleouet, J.-F., Rey, F. A., and Bhella, D. (2013) The respiratory syncytial virus nucleoprotein–RNA complex forms a left-handed helical nucleocapsid. Journal of General Virology, 94(8), pp. 1734-1738. (doi:10.1099/vir.0.053025-0) (PMID:23677789) (PMCID:PMC3749527)

Rihn, S.J., Wilson, S.J., Loman, N.J., Alim, M., Bakker, S.E., Bhella, D., Gifford, R.J., Rixon, F.J., and Bieniasz, P.D. (2013) Extreme genetic fragility of the HIV-1 capsid. PLoS Pathogens, 9(6), e1003461. (doi:10.1371/journal.ppat.1003461) (PMID:23818857) (PMCID:PMC3688543)

Bhella, D., and Bakker, S. E. (2013) Pretty Nasty, symmetry in virus architecture. Biochemist, 35(2), pp. 14-19.

Vijayakrishnan, S., Loney, C., Jackson, D., Suphamungmee, W., Rixon, F.J., and Bhella, D. (2013) Cryotomography of budding influenza a virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal end. PLoS Pathogens, 9(6), e1003413. (doi:10.1371/journal.ppat.1003413)


Schmid, M. F., Hecksel, C. W., Rochat, R. H., Bhella, D., Chiu, W., and Rixon, F. J. (2012) A tail-like assembly at the portal vertex in intact herpes simplex type-1 virions. PLoS Pathogens, 8(10), e1002961. (doi:10.1371/journal.ppat.1002961) (PMID:23055933) (PMCID:PMC3464221)


Bhella, D., and Goodfellow, I. G. (2011) The cryo-electron microscopy structure of feline calicivirus bound to junctional adhesion molecule A at 9-angstrom resolution reveals receptor-induced flexibility and two distinct conformational changes in the capsid protein VP1. Journal of Virology, 85(21), pp. 11381-11390. (doi:10.1128/JVI.05621-11) (PMID:21865392) (PMCID:PMC3194967)

Neuman, B. W. et al. (2011) A structural analysis of M protein in coronavirus assembly and morphology. Journal of Structural Biology, 174(1), pp. 11-22. (doi:10.1016/j.jsb.2010.11.021) (PMID:21130884)


Vijayakrishnan, S., Kelly, S.M., Gilbert, R.J.C., Callow, P., Bhella, D., Forsyth, T., Lindsay, J.G., and Byron, O. (2010) Solution structure and characterisation of the human pyruvate dehydrogenase complex core assembly. Journal of Molecular Biology, 399(1), pp. 71-93. (doi:10.1016/j.jmb.2010.03.043) (PMID:20361979) (PMCID:PMC2880790)

Parsons, J.B., Frank, S., Bhella, D., Liang, M., Prentice, M.B., Mulvihill, D.P., and Warren, M.J. (2010) Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement. Molecular Cell, 38(2), pp. 305-315. (doi:10.1016/j.molcel.2010.04.008) (PMID:20417607)


Tawar, R.G. et al. (2009) Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of respiratory syncytial virus. Science, 326(5957), pp. 1279-1283. (doi:10.1126/science.1177634)

Loney, C., Mottet-Osman, G., Roux, L., and Bhella, D. (2009) Paramyxovirus ultrastructure and genome packaging: cryo-electron tomography of Sendai virus. Journal of Virology, 83(16), pp. 8191-8197. (doi:10.1128/JVI.00693-09)

Alba, R. et al. (2009) Identification of coagulation factor (F)X binding sites on the adenovirus serotype 5 hexon: effect of mutagenesis on FX interactions and gene transfer. Blood, 114(5), pp. 965-971. (doi:10.1182/blood-2009-03-208835)

Greig, J.A. et al. (2009) Influence of Coagulation Factor X on In Vitro and In Vivo Gene Delivery by Adenovirus (Ad) 5, Ad35, and Chimeric Ad5/Ad35 Vectors. Molecular Therapy, 17(10), pp. 1683-1691. (doi:10.1038/mt.2009.152)


Bhella, D., Gatherer, D., Chaudhry, Y., Pink, R., and Goodfellow, I.G. (2008) Structural insights into calicivirus attachment and uncoating. Journal of Virology, 82(16), pp. 8051-8058. (doi:10.1128/JVI.00550-08)

Waddington, S. et al. (2008) Adenovirus serotype 5 hexon mediates liver gene transfer. Cell, 132(3), pp. 397-409. (doi:10.1016/j.cell.2008.01.016)


Maclellan, K., Loney, C., Yeo, R.P., and Bhella, D. (2007) The 24-angstrom structure of respiratory syncytial virus nucleocapsid protein-RNA decameric rings. Journal of Virology, 81(17), pp. 9519-9524. (doi:10.1128/JVI.00526-07)

Tran, T. et al. (2007) The nine C-terminal amino acids of the respiratory syncytial virus protein P are necessary and sufficient for binding to ribonucleoprotein complexes in which six ribonucleotides are contacted per N protein protomer. Journal of general virology, 88(1), pp. 196-206. (doi:10.1099/vir.0.82282-0)

Bhella, D. (2007) Measles virus nucleocapsid structure, conformational flexibility and the rule of six. In: Longhi, S. (ed.) Measles Virus Nucleoprotein. Series: Intrinsically disordered proteins. Nova Publishers, pp. 37-50. ISBN 9781606925218

Cao, Z., Bhella, D., and Lindsay, J.G. (2007) Reconstitution of the mitochondrial PrxII antioxidant defence pathway: General properties and factors affecting PrxII activity and oligomeric state. Journal of Molecular Biology, 372, pp. 1022-1033. (doi:10.1016/j.jmb.2007.07.018)

Davidson, A.J., and Bhella, D. (2007) Comparative genome and virion structure. In: Arvin, A., Campadelli-Fiume, G. and Mocarski, E. (eds.) Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis. Cambridge University Press. ISBN 9780521827140


Pettigrew, D.M., Williams, D.T., Kerrigan, D., Evans, D.J., Lea, S.M., and Bhella, D. (2006) Structural and functional insights into the interaction of echoviruses and decay-accelerating factor. Journal of Biological Chemistry, 281, pp. 5169-5177. (doi:10.1074/jbc.M510362200)


Bhella, D., Ralph, A., and Yeo, R.P. (2004) Conformational flexibility in recombinant measles virus nucleocapsids visualised by cryo-negative stain electron microscopy and real-space helical reconstruction. Journal of molecular biology, 340(2), pp. 319-331. (doi:10.1016/j.jmb.2004.05.015)

Bhella, D., Goodfellow, I.G., Roversi, P., Pettigrew, D., Chaudhry, Y., Evans, D.J., and Lea, S.M. (2004) The structure of echovirus type 12 bound to a two-domain fragment of its cellular attachment protein decay-accelerating factor (CD 55). Journal of Biological Chemistry, 279, pp. 8325-8332. (doi:10.1074/jbc.M311334200)


Longhi, S., Receveur-Bréchot, V., Karlin, D., Johansson, K., Darbon, H., Bhella, D., Yeo, R., Finet, S., and Canard, B. (2003) The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. Journal of Biological Chemistry, 278(20), pp. 18638-18648. (doi:10.1074/jbc.M300518200)

Murphy, L.B., Loney, C., Murray, J., Bhella, D., Ashton, P., and Yeo, R.P. (2003) Investigations into the amino-terminal domain of the respiratory syncytial virus nucleocapsid protein reveal elements important for nucleocapsid formation and interaction with the phosphoprotein. Virology, 307(1), pp. 143-53. (doi:10.1016/S0042-6822(02)00063-6)


Bhella, D., Ralph, A., Murphy, L., and Yeo, R.P. (2002) Significant differences in nucleocapsid morphology within the Paramyxoviridae. Journal of General Virology, 83(8), pp. 1831-1839.

Clayton, R.F., Owsianka, A., Aitken, J., Graham, S., Bhella, D., and Patel, A.H. (2002) Analysis of antigenicity and topology of E2 glycoprotein present on recombinant hepatitis C virus-like particles. Journal of Virology, 76(18), p. 9562. (doi:10.1128/jvi.76.18.9562.2002)

McCLelland, D.A., Aitken, J.D., Bhella, D., McNab, D., Mitchell, J., Kelly, S.M., Price, N.C., and Rixon, F.J. (2002) pH reduction as a trigger for dissociation of herpes simplex virus type 1 scaffolds. Journal of Virology, 76, pp. 7407-7417. (doi:10.1128/VJI.76.15.7407-7417.2002)


Bhella, D., Rixon, F.J., and Dargan, D.J. (2000) Cryomicroscopy of human cytomegalovirus virions reveals more densely packed genomic DNA than in herpes simplex virus type 1. Journal of Molecular Biology, 295(2), pp. 155-161. (doi:10.1006/jmbi.1999.3344)


AL-Khayat, H.A., Bhella, D., Kenney, J.M., Roth, J.F., Kingsman, A.J., Martin-Rendon, E., and Saibil, H.R. (1999) Yeast Ty retrotransposons assemble into virus-like particles whose T-numbers depend on the C-terminal length of the capsid protein. Journal of molecular biology, 292(1), pp. 65-73. (doi:10.1006/jmbi.1999.3055)

This list was generated on Fri May 27 18:53:15 2016 BST.

Visit the Bhella Group webpage