Professor David Bhella
- Professor of Structural Virology (Virology)
telephone:
01413303685
email:
David.Bhella@glasgow.ac.uk
pronouns:
He/him/his
Centre for Virus Research, Sir Michael Stoker Building, 464 Bearsden Road, Glasgow, G61 1qh
https://orcid.org/0000-0003-2096-8310Research interests
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 and viral proteins. We have access to state of the art instrumentation through the Scottish centre for macromolecular imaging (SCMI). 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, coronaviruses, influenzaviruses and pneumoviruses. Our research focusses on viral entry processes, evolution in the face of host immunity and virion assembly.
Publications
Number of items: 54.
2023
Weckener, M., Woodward, L. S., Clarke, B. R., Liu, H., Ward, P. N., Le Bas, A., Bhella, D. , Whitfield, C. and Naismith, J. H. (2023) The lipid linked oligosaccharide polymerase Wzy and its regulating co-polymerase, Wzz, from enterobacterial common antigen biosynthesis form a complex. Open Biology, 13(3), 220373. (doi: 10.1098/rsob.220373) (PMID:36944376) (PMCID:PMC10030265)
2022
Haney, J., Vijayakrishnan, S. , Streetley, J. , Dee, K., Goldfarb, D. M., Clarke, M. , Mullin, M., Carter, S. D. , Bhella, D. and Murcia, P. R. (2022) Coinfection by influenza A virus and respiratory syncytial virus produces hybrid virus particles. Nature Microbiology, 7(11), pp. 1879-1890. (doi: 10.1038/s41564-022-01242-5) (PMID:36280786)
Conley, M. J. et al. (2022) Helical ordering of envelope associated proteins and glycoproteins in respiratory syncytial virus. EMBO Journal, 41(3), e109728. (doi: 10.15252/embj.2021109728) (PMID:34935163) (PMCID:PMC8804925)
Plucinski, A., Pavlovic, M., Clarke, M. , Bhella, D. and Schmidt, B. V.K.J. (2022) Stimuli-responsive aggregation of high molar mass poly(N,N-diethylacrylamide)-b-poly(4-acryloylmorpholine) in tetrahydrofuran. Macromolecular Rapid Communications, 43(3), 2100656. (doi: 10.1002/marc.202100656) (PMID:34783099)
Loundras, E.-A., Streetley, J. , Herod, M. R., Thompson, R., Harris, M., Bhella, D. and Stonehouse, N. J. (2022) Higher-order structures of the foot-and-mouth disease virus RNA-dependent RNA polymerase required for genome replication. Communications Biology, 5, 61. (doi: 10.1038/s42003-021-02989-z) (PMID:35039618) (PMCID:PMC8764057)
2021
Mahindra, A. et al. (2021) Peptides derived from the SARS-CoV-2 receptor binding motif bind to ACE2 but do not block ACE2-mediated host cell entry or pro-inflammatory cytokine induction. PLoS ONE, 16(11), e0260283. (doi: 10.1371/journal.pone.0260283) (PMID:34793553) (PMCID:PMC8601423)
Morgan, D. C. et al. (2021) Stapled ACE2 peptidomimetics designed to target the SARS-CoV-2 spike protein do not prevent virus internalisation. Peptide Science, 113(4), e24217. (doi: 10.1002/pep2.24217) (PMID:33615115) (PMCID:PMC7883042)
Sutherland, H., Conley, M. J. , Emmott, E., Streetley, J. , Goodfellow, I. G. and Bhella, D. (2021) The cryo-EM structure of vesivirus 2117 highlights functional variations in entry pathways for viruses in different clades of the vesivirus genus. Journal of Virology, 95(13), e0028221. (doi: 10.1128/JVI.00282-21) (PMID:33853966)
2020
Vijayakrishnan, S. , McElwee, M., Loney, C. , Rixon, F. and Bhella, D. (2020) In situ structure of virus capsids within cell nuclei by correlative light and cryo-electron tomography. Scientific Reports, 10, 17596. (doi: 10.1038/s41598-020-74104-x) (PMID:33077791) (PMCID:PMC7572381)
Guzik, T. J. et al. (2020) COVID-19 and the cardiovascular system: implications for risk assessment, diagnosis, and treatment options. Cardiovascular Research, 116(10), pp. 1666-1687. (doi: 10.1093/cvr/cvaa106) (PMID:32352535) (PMCID:PMC7197627)
2019
Bhella, D. (2019) Cryo-electron microscopy: an introduction to the technique, and considerations when working to establish a national facility. Biophysical Reviews, 11(4), pp. 515-519. (doi: 10.1007/s12551-019-00571-w) (PMID:31359340) (PMCID:PMC6682334)
Conley, M.J. and Bhella, D. (2019) Asymmetric analysis reveals novel virus capsid features. Biophysical Reviews, 11(4), pp. 603-609. (doi: 10.1007/s12551-019-00572-9) (PMID:31342264) (PMCID:PMC6682188)
Conley, M. J. , McElwee, M., Azmi, L., Gabrielsen, M. , Byron, O. , Goodfellow, I. G. and Bhella, D. (2019) Calicivirus VP2 forms a portal-like assembly following receptor engagement. Nature, 565(7739), pp. 377-381. (doi: 10.1038/s41586-018-0852-1) (PMID:30626974)
2018
Ho, K. L., Gabrielsen, M., Beh, P. L., Kueh, C. L., Qiu Xian, T., Streetley, J. , Tan, W. S. and Bhella, D. (2018) Structure of the Macrobrachium rosenbergii nodavirus: a new genus within the Nodaviridae? PLoS Biology, 16(10), e3000038. (doi: 10.1371/journal.pbio.3000038) (PMID:30346944) (PMCID:PMC6211762)
McElwee, M., Vijayakrishnan, S. , Rixon, F. and Bhella, D. (2018) Structure of the herpes-simplex virus portal-vertex. PLoS Biology, 16(6), e2006191. (doi: 10.1371/journal.pbio.2006191) (PMID:29924793) (PMCID:PMC6028144)
2017
Burns, A. M. and Bhella, D. (2017) Killer microbes in movies. Microbiology Today, 44(4), pp. 162-165.
Barski, M., Brennan, B. , Miller, O. K., Potter, J. A., Vijayakrishnan, S. , Bhella, D. , Naismith, J. H., Elliott, R. M. and Schwarz-Linek, U. (2017) Rift Valley fever phlebovirus NSs protein core domain structure suggests molecular basis for nuclear filaments. eLife, 6, e29236. (doi: 10.7554/elife.29236) (PMID:28915104) (PMCID:PMC5601994)
Ho, K. L., Kueh, C. L., Beh, P. L., Tan, W. S. and Bhella, D. (2017) Cryo-electron microscopy structure of the Macrobrachium rosenbergii nodavirus capsid at 7 angstroms resolution. Scientific Reports, 7, 2083. (doi: 10.1038/s41598-017-02292-0) (PMID:28522842) (PMCID:PMC5437026)
Conley, M. , Emmott, E., Orton, R. , Taylor, D., Carneiro, D. G., Murata, K., Goodfellow, I. G., Hansman, G. S. and Bhella, D. (2017) Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures. Journal of General Virology, 98(1), pp. 68-76. (doi: 10.1099/jgv.0.000658) (PMID:27902397) (PMCID:PMC537039)
2016
Dadonaite, B., Vijayakrishnan, S. , Fodor, E., Bhella, D. and Hutchinson, E. C. (2016) Filamentous influenza viruses. Journal of General Virology, 97(8), pp. 1755-1764. (doi: 10.1099/jgv.0.000535) (PMID:27365089)
2015
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) (PMID:25557498) (PMCID:PMC4318616)
2014
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)
2013
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)
2012
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)
2011
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)
2010
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)
2009
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)
2008
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)
2007
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
2006
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)
2004
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)
2003
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)
2002
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)
2000
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)
1999
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 Thu Nov 21 03:45:47 2024 GMT.
Jump to: Articles | Book Sections
Number of items: 54.
Articles
Weckener, M., Woodward, L. S., Clarke, B. R., Liu, H., Ward, P. N., Le Bas, A., Bhella, D. , Whitfield, C. and Naismith, J. H. (2023) The lipid linked oligosaccharide polymerase Wzy and its regulating co-polymerase, Wzz, from enterobacterial common antigen biosynthesis form a complex. Open Biology, 13(3), 220373. (doi: 10.1098/rsob.220373) (PMID:36944376) (PMCID:PMC10030265)
Haney, J., Vijayakrishnan, S. , Streetley, J. , Dee, K., Goldfarb, D. M., Clarke, M. , Mullin, M., Carter, S. D. , Bhella, D. and Murcia, P. R. (2022) Coinfection by influenza A virus and respiratory syncytial virus produces hybrid virus particles. Nature Microbiology, 7(11), pp. 1879-1890. (doi: 10.1038/s41564-022-01242-5) (PMID:36280786)
Conley, M. J. et al. (2022) Helical ordering of envelope associated proteins and glycoproteins in respiratory syncytial virus. EMBO Journal, 41(3), e109728. (doi: 10.15252/embj.2021109728) (PMID:34935163) (PMCID:PMC8804925)
Plucinski, A., Pavlovic, M., Clarke, M. , Bhella, D. and Schmidt, B. V.K.J. (2022) Stimuli-responsive aggregation of high molar mass poly(N,N-diethylacrylamide)-b-poly(4-acryloylmorpholine) in tetrahydrofuran. Macromolecular Rapid Communications, 43(3), 2100656. (doi: 10.1002/marc.202100656) (PMID:34783099)
Loundras, E.-A., Streetley, J. , Herod, M. R., Thompson, R., Harris, M., Bhella, D. and Stonehouse, N. J. (2022) Higher-order structures of the foot-and-mouth disease virus RNA-dependent RNA polymerase required for genome replication. Communications Biology, 5, 61. (doi: 10.1038/s42003-021-02989-z) (PMID:35039618) (PMCID:PMC8764057)
Mahindra, A. et al. (2021) Peptides derived from the SARS-CoV-2 receptor binding motif bind to ACE2 but do not block ACE2-mediated host cell entry or pro-inflammatory cytokine induction. PLoS ONE, 16(11), e0260283. (doi: 10.1371/journal.pone.0260283) (PMID:34793553) (PMCID:PMC8601423)
Morgan, D. C. et al. (2021) Stapled ACE2 peptidomimetics designed to target the SARS-CoV-2 spike protein do not prevent virus internalisation. Peptide Science, 113(4), e24217. (doi: 10.1002/pep2.24217) (PMID:33615115) (PMCID:PMC7883042)
Sutherland, H., Conley, M. J. , Emmott, E., Streetley, J. , Goodfellow, I. G. and Bhella, D. (2021) The cryo-EM structure of vesivirus 2117 highlights functional variations in entry pathways for viruses in different clades of the vesivirus genus. Journal of Virology, 95(13), e0028221. (doi: 10.1128/JVI.00282-21) (PMID:33853966)
Vijayakrishnan, S. , McElwee, M., Loney, C. , Rixon, F. and Bhella, D. (2020) In situ structure of virus capsids within cell nuclei by correlative light and cryo-electron tomography. Scientific Reports, 10, 17596. (doi: 10.1038/s41598-020-74104-x) (PMID:33077791) (PMCID:PMC7572381)
Guzik, T. J. et al. (2020) COVID-19 and the cardiovascular system: implications for risk assessment, diagnosis, and treatment options. Cardiovascular Research, 116(10), pp. 1666-1687. (doi: 10.1093/cvr/cvaa106) (PMID:32352535) (PMCID:PMC7197627)
Bhella, D. (2019) Cryo-electron microscopy: an introduction to the technique, and considerations when working to establish a national facility. Biophysical Reviews, 11(4), pp. 515-519. (doi: 10.1007/s12551-019-00571-w) (PMID:31359340) (PMCID:PMC6682334)
Conley, M.J. and Bhella, D. (2019) Asymmetric analysis reveals novel virus capsid features. Biophysical Reviews, 11(4), pp. 603-609. (doi: 10.1007/s12551-019-00572-9) (PMID:31342264) (PMCID:PMC6682188)
Conley, M. J. , McElwee, M., Azmi, L., Gabrielsen, M. , Byron, O. , Goodfellow, I. G. and Bhella, D. (2019) Calicivirus VP2 forms a portal-like assembly following receptor engagement. Nature, 565(7739), pp. 377-381. (doi: 10.1038/s41586-018-0852-1) (PMID:30626974)
Ho, K. L., Gabrielsen, M., Beh, P. L., Kueh, C. L., Qiu Xian, T., Streetley, J. , Tan, W. S. and Bhella, D. (2018) Structure of the Macrobrachium rosenbergii nodavirus: a new genus within the Nodaviridae? PLoS Biology, 16(10), e3000038. (doi: 10.1371/journal.pbio.3000038) (PMID:30346944) (PMCID:PMC6211762)
McElwee, M., Vijayakrishnan, S. , Rixon, F. and Bhella, D. (2018) Structure of the herpes-simplex virus portal-vertex. PLoS Biology, 16(6), e2006191. (doi: 10.1371/journal.pbio.2006191) (PMID:29924793) (PMCID:PMC6028144)
Burns, A. M. and Bhella, D. (2017) Killer microbes in movies. Microbiology Today, 44(4), pp. 162-165.
Barski, M., Brennan, B. , Miller, O. K., Potter, J. A., Vijayakrishnan, S. , Bhella, D. , Naismith, J. H., Elliott, R. M. and Schwarz-Linek, U. (2017) Rift Valley fever phlebovirus NSs protein core domain structure suggests molecular basis for nuclear filaments. eLife, 6, e29236. (doi: 10.7554/elife.29236) (PMID:28915104) (PMCID:PMC5601994)
Ho, K. L., Kueh, C. L., Beh, P. L., Tan, W. S. and Bhella, D. (2017) Cryo-electron microscopy structure of the Macrobrachium rosenbergii nodavirus capsid at 7 angstroms resolution. Scientific Reports, 7, 2083. (doi: 10.1038/s41598-017-02292-0) (PMID:28522842) (PMCID:PMC5437026)
Conley, M. , Emmott, E., Orton, R. , Taylor, D., Carneiro, D. G., Murata, K., Goodfellow, I. G., Hansman, G. S. and Bhella, D. (2017) Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures. Journal of General Virology, 98(1), pp. 68-76. (doi: 10.1099/jgv.0.000658) (PMID:27902397) (PMCID:PMC537039)
Dadonaite, B., Vijayakrishnan, S. , Fodor, E., Bhella, D. and Hutchinson, E. C. (2016) Filamentous influenza viruses. Journal of General Virology, 97(8), pp. 1755-1764. (doi: 10.1099/jgv.0.000535) (PMID:27365089)
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) (PMID:25557498) (PMCID:PMC4318616)
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)
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)
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)
Book Sections
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
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
This list was generated on Thu Nov 21 03:45:47 2024 GMT.
Grants
Grants and Awards listed are those received whilst working with the University of Glasgow.
- Accelerating throughput at Scotland's national Cryo-EM centre - a next generation direct electron detector for SCMI.
Medical Research Council
2022 - 2023
- Molecular basis for Rift Valley fever phlebovirus NSs protein function
Medical Research Council
2022 - 2025
- Host and viral factors in the emergence of a virulent strain of calicivirus
Biotechnology and Biological Sciences Research Council
2020 - 2022
- CryoEM - SULSA
Scottish Universities Life Sciences Alliance
2018 - 2022
- SMIC-SULSA
Scottish Funding Council
2018 - 2021
- The Scottish Macromolecular Imaging Centre (SMIC)
Medical Research Council
2017 - 2022
- SCMI - CryoEM - St Andrews
University of St Andrews
2017 - 2022
- SCMI - CryoEM - University of Dundee
University of Dundee
2017 - 2022
- SCMI - CryoEM - University of Edinburgh
University of Edinburgh
2017 - 2022
- Quinquennial Core Funds
Medical Research Council
2016 - 2021
- 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 - 2019
- Initiation and regulation of RSV mRNA transcription and genome replication
National Institute of Allergy and Infectious Diseases
2014 - 2018
- Structural studies of human viruses and host interactions
Medical Research Council
2013 - 2016
Research datasets
Jump to: 2021
Number of items: 2.
2021
Syme, C. , Bhella, D. and Hutchinson, E. (2021) A global map of the Zika virus phosphoproteome reveals host-driven regulation of viral budding. [Data Collection]
Goldfarb, D. M., Piras, I., Bone, J., Amat, J., Parrish, C., Bhella, D. , Hutchinson, E. and Murcia, P. (2021) Identification of previously unknown genetic determinants of influenza A virus morphology. [Data Collection]
This list was generated on Thu Nov 21 03:45:49 2024 GMT.
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