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

Autor: Rebecca Conners, Rayén Ignacia León-Quezada, Mathew McLaren, Nicholas J. Bennett, Bertram Daum, Jasna Rakonjac, Vicki A. M. Gold

Publikováno v: Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)

Abstract 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

Externí odkaz: https://doaj.org/article/98015dc4b2d946138e69693418cb0023

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

Autor: Rebecca Conners, Mathew McLaren, Urszula Łapińska, Kelly Sanders, M. Rhia L. Stone, Mark A. T. Blaskovich, Stefano Pagliara, Bertram Daum, Jasna Rakonjac, Vicki A. M. Gold

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)

New virions of Ff bacteriophages are extruded from the host cell via the channel built from phage protein pIV, homologous to bacterial secretins. Here, the authors report the structure of this channel from the f1 filamentous bacteriophage and propose

Externí odkaz: https://doaj.org/article/f71d9956f4a9496997c3360054dba2c1

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

Autor: Lavinia Gambelli, Mathew McLaren, Rebecca Conners, Kelly Sanders, Matthew C. Gaines, Lewis Clark, Vicki Gold, Daniel Kattnig, Mateusz Sikora, Cyril Hanus, Michail N. Isupov, Bertram Daum

Surface layers (S-layers) are resilient two-dimensional protein lattices that encapsulate many bacteria and most archaea. In archaea, S-layers usually form the only structural component of the cell wall and thus act as the final frontier between the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::92ba0db0b5a3f00f2959942659d35e8c
https://doi.org/10.1101/2022.10.07.511299

New insights into the architecture and dynamics of archaella

Autor: Lavinia Gambelli, Michail N. Isupov, Rebecca Conners, Mathew McLaren, Annett Bellack, Vicki Gold, Reinhard Rachel, Bertram Daum

Publikováno v: BioRxiv
bioRxiv

Archaea swim by means of a unique molecular machine called the archaellum. The archaellum consists of an ATP-powered intracellular motor that drives the rotation of an extracellular filament, allowing the cell to rapidly propel itself through liquid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb467dc229f585033c38dc81b0a76412
https://doi.org/10.1101/2021.10.01.462426

Structural effects of the highly protective V127 polymorphism on human prion protein

Autor: Katherine McAuley, Jan Bieschke, Daljit Sangar, Matthew J. Cliff, Elizabeth B. Sawyer, John Collinge, Graham S. Jackson, Jonathan P. Waltho, Mark Batchelor, Rebecca Conners, R. Leo Brady, Laszlo L. P. Hosszu, Andrea M. Hounslow, Stuart Fisher

Publikováno v: Hosszu, L L P, Conners, R, Sangar, D, Batchelor, M, Sawyer, E B, Fisher, S, Cliff, M J, Hounslow, A M, McAuley, K, Brady, R L, Jackson, G S, Bieschke, J, Waltho, J P & Collinge, J 2020, ' Structural effects of the highly protective V127 polymorphism on human prion protein ', Communications Biology . https://doi.org/10.1038/s42003-020-01126-6
Communications Biology, Vol 3, Iss 1, Pp 1-12 (2020)
Hosszu, L L P, Conners, R, Sangar, D, Batchelor, M, Sawyer, E B, Fisher, S, Cliff, M J, Hounslow, A M, McAuley, K, Brady, R L, Jackson, G S, Bieschke, J, Waltho, J P & Collinge, J 2020, ' Structural effects of the highly protective V127 polymorphism on human prion protein ', Communications Biology, vol. 3, 402 . https://doi.org/10.1038/s42003-020-01126-6
Communications Biology

Prion diseases, a group of incurable, lethal neurodegenerative disorders of mammals including humans, are caused by prions, assemblies of misfolded host prion protein (PrP). A single point mutation (G127V) in human PrP prevents prion disease, however

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::804aab64475c96d92a6f0edafe6af6be
https://doi.org/10.1038/s42003-020-01126-6