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Cryo-electron microscopy of the f1 filamentous phage reveals insights into viral infection and assembly.

Conners, R.; León-Quezada, R.I.; McLaren, M.; Bennett, N.J.; Daum, B.; Rakonjac, J. & Gold, V.A.M.

Nature Communications (2023). 

doi: 10.1038/s41467-023-37915-w

Phages are viruses that infect bacteria and dominate every ecosystem on our planet. As well as impacting microbial ecology, physiology and evolution, phages are exploited as tools in molecular biology and biotechnology. This is particularly true for the Ff (f1, fd or M13) phages, which represent a widely distributed group of filamentous viruses. Over nearly five decades, Ffs have seen an extraordinary range of applications, yet the complete structure of the phage capsid and consequently the mechanisms of infection and assembly remain largely mysterious. In this work, we use cryo-electron microscopy and a highly efficient system for production of short Ff-derived nanorods to determine a structure of a filamentous virus including the tips. We show that structure combined with mutagenesis can identify phage domains that are important in bacterial attack and for release of new progeny, allowing new models to be proposed for the phage lifecycle.

All Publications

The consequence of ATP synthase dimer angle on mitochondrial morphology studied by cryo-electron tomography.

Buzzard, E.; McLaren, M.; Bragoszewski, P.; Brancaccio, A.; Ford, H. C.; Daum, B.; Kuwabara, P.; Collinson, I. & Gold, V.A.M*. Biochem J. Accepted. (2024).


Structure of the two-component S-layer of the archaeon Sulfolobus acidocaldarius.

Gambelli, L.; McLaren, M.; Conners, R.; Sanders, K.; Gaines, M. C.; Clark, L.; Gold, V.A.M., Kattnig, D.; Mateusz; S.; Hanus, C.; Isupov, M. N.& Daum, B. eLife Accpeted (2024).


CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state.

McLaren, M.; Conners, R.; Isupov, M.N.; Gil-Díez, P.; Gambelli, L.; Gold, V. A. M.; Walter, A.; Connell, S. R.; Williams, B. & Daum, B. Nat Microbiol (2023).

doi: 10.1038/s41564-023-01469-w

Structure, Biology, and Applications of Filamentous Bacteriophages.

Rakonjac, J. Gold, V.A.M, León-Quezada, R.I & Davenport, C. H. Cold Spring Harb Protoc (2023).

doi: 10.1101/pdb.over107754

A restrictor complex of ZC3H4, WDR82, and ARS2 integrates with PNUTS to control unproductive transcription.

Estell, C., Davidson, L., Eaton, J. D., Kimura, H., Gold, V. A. M & West, S. Mol Cell (2023)

doi: 10.1016/j.molcel.2023.05.029

Cryo-electron microscopy of the f1 filamentous phage reveals insights into viral infection and assembly. Conners, R., León-Quezada, R.I., McLaren, M., Bennett, N.J., Daum, B., Rakonjac, J. & Gold, V.A.M. Nat Commun (2023). 

doi: 10.1038/s41467-023-37915-w


Phage Therapy and The Public: Increasing Awareness Essential To Widespread Use.

McCammon, S., Makarovs, K., Banducci, S. & Gold, V.A.M. PLOS One (2023).

doi: 10.1371/journal.pone.0285824


Interaction of the periplasmic chaperone SurA with the inner membrane protein secretion (Sec) machinery. 

Troman, L., Alvira, S.; Daum, B., Gold V. A. M. & Collinson, I. Biochem J (2023).

doi: 10.1042/bcj20220480 

Electron cryo-microscopy reveals the structure of the archaeal thread filament

Gaines, M.C., Isupov, M. N. l, Sivabalasarma, S., Haque, R., McLaren, M., Mollat, C. M., Tripp, P., Neuhaus, A., Gold, V. A. M., Albers, S-V. & Daum, B. Nat Commun (2022). 

doi: 10.1038/s41467-022-34652-4 

An archaellum filament composed of two alternating subunits.

Gambelli, L., Isupov, M.N., Conners, R., McLaren, M.; Bellack, A.; Gold, V. A. M.; Rachel, R. & Daum, B. Nat Commun (2022).

doi: 10.1038/s41467-022-28337-1

CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage

Conners, R., McLaren, M., Łapińska, U., Sanders, K., Stone, M. R. L., Blaskovich, M. A. T., Pagliara, S., Daum, B., Rakonjac, J. & Gold, V. A. M. Nat Commun (2021). 

doi: 10.1038/s41467-021-26610-3

Maintenance of complex I and its supercomplexes by NDUF-11 is essential for mitochondrial structure, function and health

Knapp-Wilson, A., Pereira, G. C., Buzzard, E., Richardson, A., Corey, R. A., Neal, C., Verkade, P., Halestrap, A., Gold, V. A. M., Kuwabara, P. and & Collinson, I. J Cell Sci (2021)

doi: 10.1242/jcs.258399

Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis

Alvira, S., Watkins, D. W., Troman, L., Allen, W. J., Lorriman, J. S., Degliesposti, G., Cohen, E. J., Beeby, M., Daum, B., Gold, V. A. M., Skehel, M. J. & Collinson, I. eLife (2020).

doi: 10.7554/eLife.60669


Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium

Neuhaus, A., Muniyandi, S., Salzer, R., Langer, J. D., Kruse, K., Sanders, K., Daum, B., Averhoff, B. & Gold, V. A. M. Nat Commun (2020).

doi: 10.1038/s41467-020-15650-w

Architecture and modular assembly of  S-layers revealed by electron cryo-tomography

Gambelli, L., Meyer, B., McLaren, M., Sanders, K., Quax, T. E. F., Gold, V. A. M., Albers, S. & Daum, B. Proc Natl Acad Sci USA (2019).

doi: 10.1073/pnas.1911262116


Twitch or swim: towards the understanding of prokaryotic motion based on the type IV pilus blueprint

Daum, B.* & Gold, V. A. M.* Biol Chem (2018).

doi: 10.1515/hsz-2018-0157

*joint corresponding authors


The ER morphology-regulating lunapark protein induces the formation of stacked bilayer discs

Wang, S., Powers, R. E., Gold, V. A. M. & Rapoport, T. A. Life Sci Alliance (2018).

doi: 10.26508/lsa.201700014


Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo-tomography

Gold, V. A. M.*, Chroscicki, P., Bragoszewski, P. & Chacinska, A.*  EMBO Rep (2017).

doi: 10.15252/embr.201744261

*joint corresponding authors


Analysis of mitochondrial membrane protein complexes by electron cryo-tomography

Gold V. A. M., Brandt, T., Cavellini, L., Cohen, M. M., Ieva, R. & van der Laan, M. Methods Mol Biol (2017).

doi: 10.1007/978-1-4939-6824-4_19


Recent progress in structure and dynamics of dual-membrane-spanning bacterial nanomachines

Gold V. A. M.* & Kudryashev, M.* Curr Opin Struct Biol (2016).

doi: 10.1016/

*corresponding authors


Topology and structure/function correlation of ring and gate forming domains in a dynamic secretin complex.

Salzer, R., D’Imprima, E., Gold V. A. M., Rose, I., Drechsler, M., Vonck, J. & Averhoff, B. J Biol Chem (2016).

doi: 10.1074/jbc.M116.724153


Protein import by the mitochondrial presequence translocase in the absence of a membrane potential

Turakhiya, U., von der Malsburg, K., Gold V. A. M., van der Laan, M. & Ieva, R. J Mol Bio (2016).

doi: 10.1016/j.jmb.2016.01.020


Structure of the type IV pilus machinery in the open and closed state.

Gold, V. A. M. *, Salzer, R., Averhoff, B. & Kühlbrandt, W. eLife (2015).

doi: 10.7554/eLife.07380

*corresponding author


Visualizing active membrane protein complexes by electron cryotomography

Gold, V. A. M.*, Ieva, R., Walter, A., van der Laan, M., Pfanner, N. & Kühlbrandt, W. Nat Commun (2014).

doi: 10.1038/ncomms5129

*corresponding author


Visualization of ATP synthase dimers in mitochondria by electron cryo-tomography

Davies, K. M., Daum, B., Gold, V. A. M., Mühleip, A. W., Brandt, T., Blum, T. B., Mills, D. J. & Kühlbrandt, K. J Vis Exp (2014).

doi: 10.3791/51228


Membrane protein insertion and PMF-driven protein export by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC

Schulze, R. J., Komar, J., Botte, M., Whitehouse, S., Gold, V. A. M., Huard, K., Berger, I., Schaffitzel, C. & Collinson, I. Proc Natl Acad Sci USA (2014).

doi: 10.1073/pnas.1315901111


A cell model for the initial phase of sporadic Alzheimer’s disease

Stockburger, C., Gold, V. A. M., Pallas, T., Kolesova, N., Miano, D., Leuner, K. & Müller, W. E. J Alz Dis (2014).

doi: 10.3233/JAD-140381


The dynamic action of SecA during the initiation of protein translocation

Gold, V. A. M., Whitehouse, S., Robson, A. & Collinson, I.  J Biol Chem (2013).

doi: 10.7554/eLife.35112

Mobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complex

Whitehouse, S., Gold, V. A. M., Sessions, R. B. & Collinson, I. J Cell Biol (2012).

doi: 10.1083/jcb.201205191


Structure of the SecY complex unlocked by a preprotein mimic

Hizlan, D., Robson, A., Whitehouse, S., Gold, V. A. M., Vonck, J., Mills, D. J., Kühlbrandt, W. & Collinson, I.  Cell Rep (2012).

doi: 10.1016/j.celrep.2011.11.003


The oligomeric state and arrangement of the active bacterial translocon

Deville, K.,# .Gold, V. A. M.,# Robson, A., Sessions, R. B., Baldwin, S., Radford, S. & Collinson, I. J Biol Chem (2011).

doi: 10.1074/jbc.M110.175638

#equal first author contribution


The action of cardiolipin on the bacterial translocon

Gold, V. A. M., Robson, A., Bao, H., Romantsov, T., Duong, F. & Collinson, I. Proc Natl Acad Sci USA (2010).

doi: 10.1073/pnas.0914680107

Energy transduction in protein transport and the ATP hydrolytic cycle of SecA

Robson, A.,# Gold, V. A. M.# Hodson, S., Clarke, A. R., & Collinson, I. Proc Natl Acad Sci USA (2009).

doi: 10.1073/pnas.0809592106

#equal first author contribution.

A large conformational change couples the ATP binding site of SecA to the SecY protein channel

Robson, A., Booth, A. E., Gold V. A. M, Clarke, A. R. & Collinson, I. J Mol Biol (2007).

doi: 10.1016/j.jmb.2007.09.086


Structure and function of the bacterial Sec translocon

Gold V. A. M., Duong, F. & Collinson I. Mol Membr Biol. (2007).

doi: 10.1080/09687680701416570


Allosteric regulation of SecA: magnesium-mediated control of conformation and activity

Gold V. A. M., Robson, A., Clarke, A. R. & Collinson, I. J Biol Chem (2007).

doi: 10.1074/jbc.M702066200

Group members are highlighted in bold

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