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1,332 results on '"Stuart, David I."'

1. Improving the representativeness of UK’s national COVID-19 Infection Survey through spatio-temporal regression and post-stratification

Author

Pouwels, Koen B., Eyre, David W., House, Thomas, Aspey, Ben, Matthews, Philippa C., Stoesser, Nicole, Newton, John N., Diamond, Ian, Studley, Ruth, Taylor, Nick G. H., Bell, John I., Farrar, Jeremy, Kolenchery, Jaison, Marsden, Brian D., Hoosdally, Sarah, Jones, E. Yvonne, Stuart, David I., Crook, Derrick W., Peto, Tim E. A., and Walker, A. Sarah

Published
2024
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2. Emerging variants develop total escape from potent monoclonal antibodies induced by BA.4/5 infection

Author

Liu, Chang, Das, Raksha, Dijokaite-Guraliuc, Aiste, Zhou, Daming, Mentzer, Alexander J., Supasa, Piyada, Selvaraj, Muneeswaran, Duyvesteyn, Helen M. E., Ritter, Thomas G., Temperton, Nigel, Klenerman, Paul, Dunachie, Susanna J., Paterson, Neil G., Williams, Mark A., Hall, David R., Fry, Elizabeth E., Mongkolsapaya, Juthathip, Ren, Jingshan, Stuart, David I., and Screaton, Gavin R.

Published
2024
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4. Sample Preparation and Data Collection for High-Speed Fixed-Target Serial Femtosecond Crystallography

Author

Meents, Alke, Roedig, Philip, Ginn, Helen M, Pakendorf, Tim, Sutton, Geoff, Harlos, Karl, Walter, Thomas S, Meyer, Jan, Fischer, Pontus, Duman, Ramona, Vartiainen, Ismo, Reime, Bernd, Warmer, Martin, Brewster, Aaron S, Young, Iris D, Clark, Tara Michels, Sauter, Nicholas K, Sikorsky, Marcin, Nelson, Silke, Damiani, Daniel S, Alonso-Mori, Roberto, Ren, Jingshan, Fry, Elizabeth E, David, Christian, Stuart, David I, and Wagner, Armin H

Published
2023

5. Accelerating Inhibitor Discovery With A Deep Generative Foundation Model: Validation for SARS-CoV-2 Drug Targets

Author

Chenthamarakshan, Vijil, Hoffman, Samuel C., Owen, C. David, Lukacik, Petra, Strain-Damerell, Claire, Fearon, Daren, Malla, Tika R., Tumber, Anthony, Schofield, Christopher J., Duyvesteyn, Helen M. E., Dejnirattisai, Wanwisa, Carrique, Loic, Walter, Thomas S., Screaton, Gavin R., Matviiuk, Tetiana, Mojsilovic, Aleksandra, Crain, Jason, Walsh, Martin A., Stuart, David I., and Das, Payel

Subjects
Quantitative Biology - Quantitative Methods, Computer Science - Machine Learning, Quantitative Biology - Biomolecules, Statistics - Machine Learning
Abstract

The discovery of novel inhibitor molecules for emerging drug-target proteins is widely acknowledged as a challenging inverse design problem: Exhaustive exploration of the vast chemical search space is impractical, especially when the target structure or active molecules are unknown. Here we validate experimentally the broad utility of a deep generative framework trained at-scale on protein sequences, small molecules, and their mutual interactions -- that is unbiased toward any specific target. As demonstrators, we consider two dissimilar and relevant SARS-CoV-2 targets: the main protease and the spike protein (receptor binding domain, RBD). To perform target-aware design of novel inhibitor molecules, a protein sequence-conditioned sampling on the generative foundation model is performed. Despite using only the target sequence information, and without performing any target-specific adaptation of the generative model, micromolar-level inhibition was observed in in vitro experiments for two candidates out of only four synthesized for each target. The most potent spike RBD inhibitor also exhibited activity against several variants in live virus neutralization assays. These results therefore establish that a single, broadly deployable generative foundation model for accelerated hit discovery is effective and efficient, even in the most general case where neither target structure nor binder information is available., Comment: Revised title, abstract, and text; additional figures

Published
2022

7. Immunogenicity of Abdala COVID-19 vaccine in Vietnamese people after primary and booster vaccinations: A prospective observational study in Vietnam

Author

Thanh, Tran Tan, Tu, Nguyen Thi Kha, Nguyet, Lam Anh, Thuy, Cao Thu, Thuan, Nguyen Lam Thai, Ny, Nguyen Thi Han, Nhu, Le Nguyen Truc, Thanh, Le Kim, Hong, Nguyen Thi Thu, Anh, Nguyen To, Truong, Nguyen Thanh, Chau, Nguyen Van Vinh, Yen, Lam Minh, Van E, Phan, Thuong, Nguyen Phong, Van Truc, Nguyen, Trung, Pham Huu, Yap, Wee Chee, Pandey, Rahul, Yee, Sidney, Weng, Ruifen, Mongkolsapaya, Juthathip, Dejnirattisai, Wanwisa, Hamers, Raph L, Chantratita, Narisara, Screaton, Gavin, Dunachie, Susanna J, Jones, E Yvonne, Stuart, David I, Dung, Nguyen Thanh, Thwaites, Guy, Wang, Lin-Fa, Tan, Chee Wah, and Tan, Le Van

Published
2024
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8. A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity

Author

Liu, Chang, Zhou, Daming, Dijokaite-Guraliuc, Aiste, Supasa, Piyada, Duyvesteyn, Helen M.E., Ginn, Helen M., Selvaraj, Muneeswaran, Mentzer, Alexander J., Das, Raksha, de Silva, Thushan I., Ritter, Thomas G., Plowright, Megan, Newman, Thomas A.H., Stafford, Lizzie, Kronsteiner, Barbara, Temperton, Nigel, Lui, Yuan, Fellermeyer, Martin, Goulder, Philip, Klenerman, Paul, Dunachie, Susanna J., Barton, Michael I., Kutuzov, Mikhail A., Dushek, Omer, Fry, Elizabeth E., Mongkolsapaya, Juthathip, Ren, Jingshan, Stuart, David I., and Screaton, Gavin R.

Published
2024
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14. CryoSIM: super-resolution 3D structured illumination cryogenic fluorescence microscopy for correlated ultrastructural imaging

Author

Phillips, Michael A, Harkiolaki, Maria, Pinto, David Miguel Susano, Parton, Richard M, Palanca, Ana, Garcia-Moreno, Manuel, Kounatidis, Ilias, Sedat, John W, Stuart, David I, Castello, Alfredo, Booth, Martin J, Davis, Ilan, and Dobbie, Ian M

Subjects
Bioengineering, 1.1 Normal biological development and functioning, 1.5 Resources and infrastructure (underpinning), Underpinning research, Generic health relevance, Optical Physics, Electrical and Electronic Engineering, Communications Technologies
Abstract

Rapid cryopreservation of biological specimens is the gold standard for visualizing cellular structures in their true structural context. However, current commercial cryo-fluorescence microscopes are limited to low resolutions. To fill this gap, we have developed cryoSIM, a microscope for 3D super-resolution fluorescence cryo-imaging for correlation with cryo-electron microscopy or cryo-soft X-ray tomography. We provide the full instructions for replicating the instrument mostly from off-the-shelf components and accessible, user-friendly, open-source Python control software. Therefore, cryoSIM democratizes the ability to detect molecules using super-resolution fluorescence imaging of cryopreserved specimens for correlation with their cellular ultrastructure.

Published
2020

15. Rapid escape of new SARS-CoV-2 Omicron variants from BA.2-directed antibody responses

Author

Conlon, Christopher, Deeks, Alexandra, Frater, John, Gardiner, Siobhan, Jämsén, Anni, Jeffery, Katie, Malone, Tom, Phillips, Eloise, Kronsteiner-Dobramysl, Barbara, Abraham, Priyanka, Bibi, Sagida, Lambe, Teresa, Longet, Stephanie, Tipton, Tom, Carrol, Miles, Stafford, Lizzie, Dijokaite-Guraliuc, Aiste, Das, Raksha, Zhou, Daming, Ginn, Helen M., Liu, Chang, Duyvesteyn, Helen M.E., Huo, Jiandong, Nutalai, Rungtiwa, Supasa, Piyada, Selvaraj, Muneeswaran, de Silva, Thushan I., Plowright, Megan, Newman, Thomas A.H., Hornsby, Hailey, Mentzer, Alexander J., Skelly, Donal, Ritter, Thomas G., Temperton, Nigel, Klenerman, Paul, Barnes, Eleanor, Dunachie, Susanna J., Roemer, Cornelius, Peacock, Thomas P., Paterson, Neil G., Williams, Mark A., Hall, David R., Fry, Elizabeth E., Mongkolsapaya, Juthathip, Ren, Jingshan, Stuart, David I., and Screaton, Gavin R.

Published
2023
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16. Continuous population-level monitoring of SARS-CoV-2 seroprevalence in a large European metropolitan region

Author

Emmenegger, Marc, De Cecco, Elena, Lamparter, David, Jacquat, Raphaël P.B., Riou, Julien, Menges, Dominik, Ballouz, Tala, Ebner, Daniel, Schneider, Matthias M., Morales, Itzel Condado, Doğançay, Berre, Guo, Jingjing, Wiedmer, Anne, Domange, Julie, Imeri, Marigona, Moos, Rita, Zografou, Chryssa, Batkitar, Leyla, Madrigal, Lidia, Schneider, Dezirae, Trevisan, Chiara, Gonzalez-Guerra, Andres, Carrella, Alessandra, Dubach, Irina L., Xu, Catherine K., Meisl, Georg, Kosmoliaptsis, Vasilis, Malinauskas, Tomas, Burgess-Brown, Nicola, Owens, Ray, Hatch, Stephanie, Mongkolsapaya, Juthathip, Screaton, Gavin R., Schubert, Katharina, Huck, John D., Liu, Feimei, Pojer, Florence, Lau, Kelvin, Hacker, David, Probst-Müller, Elsbeth, Cervia, Carlo, Nilsson, Jakob, Boyman, Onur, Saleh, Lanja, Spanaus, Katharina, von Eckardstein, Arnold, Schaer, Dominik J., Ban, Nenad, Tsai, Ching-Ju, Marino, Jacopo, Schertler, Gebhard F.X., Ebert, Nadine, Thiel, Volker, Gottschalk, Jochen, Frey, Beat M., Reimann, Regina R., Hornemann, Simone, Ring, Aaron M., Knowles, Tuomas P.J., Puhan, Milo A., Althaus, Christian L., Xenarios, Ioannis, Stuart, David I., and Aguzzi, Adriano

Published
2023
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17. A delicate balance between antibody evasion and ACE2 affinity for Omicron BA.2.75

Author

Huo, Jiandong, Dijokaite-Guraliuc, Aiste, Liu, Chang, Zhou, Daming, Ginn, Helen M., Das, Raksha, Supasa, Piyada, Selvaraj, Muneeswaran, Nutalai, Rungtiwa, Tuekprakhon, Aekkachai, Duyvesteyn, Helen M.E., Mentzer, Alexander J., Skelly, Donal, Ritter, Thomas G., Amini, Ali, Bibi, Sagida, Adele, Sandra, Johnson, Sile Ann, Paterson, Neil G., Williams, Mark A., Hall, David R., Plowright, Megan, Newman, Thomas A.H., Hornsby, Hailey, de Silva, Thushan I., Temperton, Nigel, Klenerman, Paul, Barnes, Eleanor, Dunachie, Susanna J., Pollard, Andrew J., Lambe, Teresa, Goulder, Philip, Fry, Elizabeth E., Mongkolsapaya, Juthathip, Ren, Jingshan, Stuart, David I., and Screaton, Gavin R.

Published
2023
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18. Antibody responses and correlates of protection in the general population after two doses of the ChAdOx1 or BNT162b2 vaccines

Author

Wei, Jia, Pouwels, Koen B., Stoesser, Nicole, Matthews, Philippa C., Diamond, Ian, Studley, Ruth, Rourke, Emma, Cook, Duncan, Bell, John I., Newton, John N., Farrar, Jeremy, Howarth, Alison, Marsden, Brian D., Hoosdally, Sarah, Jones, E. Yvonne, Stuart, David I., Crook, Derrick W., Peto, Tim E. A., Walker, A. Sarah, and Eyre, David W.

Published
2022
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20. Oligomerization-driven avidity correlates with SARS-CoV-2 cellular binding and inhibition.

Author

Asor, Roi, Olerinyova, Anna, Burnap, Sean A., Kushwah, Manish S., Soltermann, Fabian, Rudden, Lucas S. P., Hensen, Mario, Vasiljevic, Snežana, Brun, Juliane, Hill, Michelle, Liu Chang, Dejnirattisai, Wanwisa, Supasa, Piyada, Mongkolsapaya, Juthathip, Daming Zhou, Stuart, David I., Screaton, Gavin R., Degiacomi, Matteo T., Zitzmann, Nicole, and Benesch, Justin L. P.

Subjects
ANGIOTENSIN converting enzyme, RECEPTOR antibodies, OLIGOMERIZATION, SARS-CoV-2, CELL membranes
Abstract

Cellular processes are controlled by the thermodynamics of the underlying biomolecular interactions. Frequently, structural investigations use one monomeric binding partner, while ensemble measurements of binding affinities generally yield one affinity representative of a 1:1 interaction, despite the majority of the proteome consisting of oligomeric proteins. For example, viral entry and inhibition in SARS-CoV-2 involve a trimeric spike surface protein, a dimeric angiotensin-converting enzyme 2 (ACE2) cell-surface receptor and dimeric antibodies. Here, we reveal that cooperativity correlates with infectivity and inhibition as opposed to 1:1 binding strength. We show that ACE2 oligomerizes spike more strongly for more infectious variants, while exhibiting weaker 1:1 affinity. Furthermore, we find that antibodies use induced oligomerization both as a primary inhibition mechanism and to enhance the effects of receptor-site blocking. Our results suggest that naive affinity measurements are poor predictors of potency, and introduce an antibody-based inhibition mechanism for oligomeric targets. More generally, they point toward a much broader role of induced oligomerization in controlling biomolecular interactions. [ABSTRACT FROM AUTHOR]

Published
2024
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21. Towards in cellulo virus crystallography.

Author

Duyvesteyn, Helen ME, Ginn, Helen M, Pietilä, Maija K, Wagner, Armin, Hattne, Johan, Grimes, Jonathan M, Hirvonen, Elina, Evans, Gwyndaf, Parsy, Marie-Laure, Sauter, Nicholas K, Brewster, Aaron S, Huiskonen, Juha T, Stuart, David I, Sutton, Geoff, and Bamford, Dennis H

Subjects
Escherichia coli, Bacteriophage phi X 174, Cryoelectron Microscopy, Crystallography, X-Ray, Crystallography, X-Ray, Biotechnology, 2.2 Factors relating to physical environment, Infection, Biochemistry and Cell Biology, Other Physical Sciences
Abstract

Viruses are a significant threat to both human health and the economy, and there is an urgent need for novel anti-viral drugs and vaccines. High-resolution viral structures inform our understanding of the virosphere, and inspire novel therapies. Here we present a method of obtaining such structural information that avoids potentially disruptive handling, by collecting diffraction data from intact infected cells. We identify a suitable combination of cell type and virus to accumulate particles in the cells, establish a suitable time point where most cells contain virus condensates and use electron microscopy to demonstrate that these are ordered crystalline arrays of empty capsids. We then use an X-ray free electron laser to provide extremely bright illumination of sub-micron intracellular condensates of bacteriophage phiX174 inside living Escherichia coli at room temperature. We have been able to collect low resolution diffraction data. Despite the limited resolution and completeness of these initial data, due to a far from optimal experimental setup, we have used novel methodology to determine a putative space group, unit cell dimensions, particle packing and likely maturation state of the particles.

Published
2018

27. Risk-free polio vaccine: Recombinant expression systems for production of stabilised virus-like particles

Author

Sherry, Lee, primary, Bahar, Mohammad W, additional, Porta, Claudine, additional, Fox, Helen, additional, Grehan, Keith, additional, Nasta, Veronia, additional, Duyvesteyn, Helen ME, additional, de Colibus, Luigi, additional, Marsian, Johanna, additional, Murdoch, Inga, additional, Ponndorf, Daniel, additional, Kim, Seong-Ryong, additional, Shah, Sachin, additional, Carlyle, Sarah, additional, Swanson, Jessica J, additional, Matthews, Sue, additional, Nicol, Clare, additional, Lomonossoff, George P, additional, Macadam, Andrew J, additional, Fry, Ellizabeth E, additional, Stuart, David I, additional, Stonehouse, Nicola J, additional, and Rowlands, David J, additional

Published
2024
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29. High-speed fixed-target serial virus crystallography

Author

Roedig, Philip, Ginn, Helen M, Pakendorf, Tim, Sutton, Geoff, Harlos, Karl, Walter, Thomas S, Meyer, Jan, Fischer, Pontus, Duman, Ramona, Vartiainen, Ismo, Reime, Bernd, Warmer, Martin, Brewster, Aaron S, Young, Iris D, Michels-Clark, Tara, Sauter, Nicholas K, Kotecha, Abhay, Kelly, James, Rowlands, David J, Sikorsky, Marcin, Nelson, Silke, Damiani, Daniel S, Alonso-Mori, Roberto, Ren, Jingshan, Fry, Elizabeth E, David, Christian, Stuart, David I, Wagner, Armin, and Meents, Alke

Subjects
Biological Sciences, Infection, Algorithms, Crystallography, X-Ray, Image Enhancement, Image Interpretation, Computer-Assisted, Imaging, Three-Dimensional, Reproducibility of Results, Sample Size, Sensitivity and Specificity, Viruses, Technology, Medical and Health Sciences, Developmental Biology, Biological sciences
Abstract

We report a method for serial X-ray crystallography at X-ray free-electron lasers (XFELs), which allows for full use of the current 120-Hz repetition rate of the Linear Coherent Light Source (LCLS). Using a micropatterned silicon chip in combination with the high-speed Roadrunner goniometer for sample delivery, we were able to determine the crystal structures of the picornavirus bovine enterovirus 2 (BEV2) and the cytoplasmic polyhedrosis virus type 18 polyhedrin, with total data collection times of less than 14 and 10 min, respectively. Our method requires only micrograms of sample and should therefore broaden the applicability of serial femtosecond crystallography to challenging projects for which only limited sample amounts are available. By synchronizing the sample exchange to the XFEL repetition rate, our method allows for most efficient use of the limited beam time available at XFELs and should enable a substantial increase in sample throughput at these facilities.

Published
2017

30. Community prevalence of SARS-CoV-2 in England from April to November, 2020: results from the ONS Coronavirus Infection Survey

Author

Pouwels, Koen B., Walker, A. Sarah, Crook, Derrick, Matthews, Philippa C., Peto, Tim, Pritchard, Emma, Stoesser, Nicole, Vihta, Karina-Doris, Howarth, Alison, Doherty, George, Kavanagh, James, Chau, Kevin K., Hatch, Stephanie B., Ebner, Daniel, Martins Ferreira, Lucas, Christott, Thomas, Marsden, Brian D., Dejnirattisai, Wanwisa, Mongkolsapaya, Juthathip, Hoosdally, Sarah, Cornall, Richard, Stuart, David I., Screaton, Gavin, Eyre, David, Bell, John, Cox, Stuart, Paddon, Kevin, James, Tim, House, Thomas, Newton, John N., Robotham, Julie V., Birrell, Paul, Jordan, Helena, Sheppard, Tim, Athey, Graham, Moody, Dan, Curry, Leigh, Brereton, Pamela, Hay, Jodie, Vansteenhouse, Harper, Bell, Iain, Diamond, Ian, Lambert, Alex, Benton, Pete, Rourke, Emma, Hawkes, Stacey, Henry, Sarah, Scruton, James, Stokes, Peter, Thomas, Tina, Allen, John, Black, Russell, Bovill, Heather, Braunholtz, David, Brown, Dominic, Collyer, Sarah, Crees, Megan, Daglish, Colin, Davies, Byron, Donnarumma, Hannah, Douglas-Mann, Julia, Felton, Antonio, Finselbach, Hannah, Fordham, Eleanor, Ipser, Alberta, Jenkins, Joe, Jones, Joel, Kent, Katherine, Kerai, Geeta, Lloyd, Lina, Masding, Victoria, Osborn, Ellie, Patel, Alpi, Pereira, Elizabeth, Pett, Tristan, Randall, Melissa, Reeve, Donna, Shah, Palvi, Snook, Ruth, Studley, Ruth, Sutherland, Esther, Swinn, Eliza, Thomas, Heledd, Tudor, Anna, Weston, Joshua, Leib, Shayla, Tierney, James, Farkas, Gabor, Cobb, Raf, Van Galen, Folkert, Compton, Lewis, Irving, James, Clarke, John, Mullis, Rachel, Ireland, Lorraine, Airimitoaie, Diana, Nash, Charlotte, Cox, Danielle, Fisher, Sarah, Moore, Zoe, McLean, James, Kerby, Matt, Pouwels, Koen B, Robotham, Julie V, Birrell, Paul J, Gelman, Andrew, Bowers, Nikola, Boreham, Ian, Lewis, James, Bell, John I, Newton, John N, Farrar, Jeremy, and Walker, Ann Sarah

Published
2021
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31. Performance characteristics of five immunoassays for SARS-CoV-2: a head-to-head benchmark comparison

Author

Ainsworth, Mark, Andersson, Monique, Auckland, Kathryn, Baillie, J Kenneth, Barnes, Eleanor, Beer, Sally, Beveridge, Amy, Bibi, Sagida, Blackwell, Luke, Borak, Martyna, Bown, Abbie, Brooks, Tim, Burgess-Brown, Nicola A, Camara, Susana, Catton, Matthew, Chau, Kevin K., Christott, Thomas, Clutterbuck, Elizabeth, Coker, Jesse, Cornall, Richard J, Cox, Stuart, Crawford-Jones, David, Crook, Derrick W, D'Arcangelo, Silvia, Dejnirattsai, Wanwisa, Dequaire, Julie M M, Dimitriadis, Stavros, Dingle, Kate E, Doherty, George, Dold, Christina, Dong, Tao, Dunachie, Susanna J, Ebner, Daniel, Emmenegger, Marc, Espinosa, Alexis, Eyre, David W, Fairhead, Rory, Fassih, Shayan, Feehily, Conor, Felle, Sally, Fernandez-Cid, Alejandra, Fernandez Mendoza, Maria, Foord, Thomas H, Fordwoh, Thomas, Fox McKee, Deborah, Frater, John, Gallardo Sanchez, Veronica, Gent, Nick, Georgiou, Dominique, Groves, Christopher J, Hallis, Bassam, Hammond, Peter M, Hatch, Stephanie B., Harvala, Heli J, Hill, Jennifer, Hoosdally, Sarah J, Horsington, Bryn, Howarth, Alison, James, Tim, Jeffery, Katie, Jones, Elizabeth, Justice, Anita, Karpe, Fredrik, Kavanagh, James, Kim, David S, Kirton, Richard, Klenerman, Paul, Knight, Julian C, Koukouflis, Leonidas, Kwok, Andrew, Leuschner, Ullrich, Levin, Robert, Linder, Aline, Lockett, Teresa, Lumley, Sheila F, Marinou, Spyridoula, Marsden, Brian D, Martinez, Jose, Martins Ferreira, Lucas, Mason, Lara, Matthews, Philippa C, Mentzer, Alexander J, Mobbs, Alexander, Mongkolsapaya, Juthathip, Morrow, Jordan, Mukhopadhyay, Shubhashish M M, Neville, Matthew J, Oakley, Sarah, Oliveira, Marta, Otter, Ashley, Paddon, Kevin, Pascoe, Jordan, Peng, Yanchun, Perez, Elena, Perumal, Prem K, Peto, Timothy E A, Pickford, Hayleah, Ploeg, Rutger J, Pollard, Andrew J, Richardson, Anastasia, Ritter, Thomas G, Roberts, David J, Rodger, Gillian, Rollier, Christine S, Rowe, Cathy, Rudkin, Justine K, Screaton, Gavin, Semple, Malcolm G, Sienkiewicz, Alex, Silva-Reyes, Laura, Skelly, Donal T, Sobrino Diaz, Alberto, Stafford, Lizzie, Stockdale, Lisa, Stoesser, Nicole, Street, Teresa, Stuart, David I, Sweed, Angela, Taylor, Adan, Thraves, Hannah, Tsang, Hoi P, Verheul, Marije K, Vipond, Richard, Walker, Timothy M, Wareing, Susan, Warren, Yolanda, Wells, Charlie, Wilson, Clare, Withycombe, Kate, and Young, Rebecca K

Published
2020
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32. Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient

Author

Zhou, Daming, Duyvesteyn, Helen M. E., Chen, Cheng-Pin, Huang, Chung-Guei, Chen, Ting-Hua, Shih, Shin-Ru, Lin, Yi-Chun, Cheng, Chien-Yu, Cheng, Shu-Hsing, Huang, Yhu-Chering, Lin, Tzou-Yien, Ma, Che, Huo, Jiandong, Carrique, Loic, Malinauskas, Tomas, Ruza, Reinis R., Shah, Pranav N. M., Tan, Tiong Kit, Rijal, Pramila, Donat, Robert F., Godwin, Kerry, Buttigieg, Karen R., Tree, Julia A., Radecke, Julika, Paterson, Neil G., Supasa, Piyada, Mongkolsapaya, Juthathip, Screaton, Gavin R., Carroll, Miles W., Gilbert-Jaramillo, Javier, Knight, Michael L., James, William, Owens, Raymond J., Naismith, James H., Townsend, Alain R., Fry, Elizabeth E., Zhao, Yuguang, Ren, Jingshan, Stuart, David I., and Huang, Kuan-Ying A.

Published
2020
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33. Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2

Author

Huo, Jiandong, Le Bas, Audrey, Ruza, Reinis R., Duyvesteyn, Helen M. E., Mikolajek, Halina, Malinauskas, Tomas, Tan, Tiong Kit, Rijal, Pramila, Dumoux, Maud, Ward, Philip N., Ren, Jingshan, Zhou, Daming, Harrison, Peter J., Weckener, Miriam, Clare, Daniel K., Vogirala, Vinod K., Radecke, Julika, Moynié, Lucile, Zhao, Yuguang, Gilbert-Jaramillo, Javier, Knight, Michael L., Tree, Julia A., Buttigieg, Karen R., Coombes, Naomi, Elmore, Michael J., Carroll, Miles W., Carrique, Loic, Shah, Pranav N. M., James, William, Townsend, Alain R., Stuart, David I., Owens, Raymond J., and Naismith, James H.

Published
2020
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34. Structure of CPV17 polyhedrin determined by the improved analysis of serial femtosecond crystallographic data.

Author

Ginn, Helen M, Messerschmidt, Marc, Ji, Xiaoyun, Zhang, Hanwen, Axford, Danny, Gildea, Richard J, Winter, Graeme, Brewster, Aaron S, Hattne, Johan, Wagner, Armin, Grimes, Jonathan M, Evans, Gwyndaf, Sauter, Nicholas K, Sutton, Geoff, and Stuart, David I

Subjects
Animals, Culicidae, Reoviridae, Viral Structural Proteins, Crystallography, Protein Conformation, Genetic Vectors, Models, Molecular, Image Processing, Computer-Assisted, Models, Molecular, Image Processing, Computer-Assisted, Generic Health Relevance
Abstract

The X-ray free-electron laser (XFEL) allows the analysis of small weakly diffracting protein crystals, but has required very many crystals to obtain good data. Here we use an XFEL to determine the room temperature atomic structure for the smallest cytoplasmic polyhedrosis virus polyhedra yet characterized, which we failed to solve at a synchrotron. These protein microcrystals, roughly a micron across, accrue within infected cells. We use a new physical model for XFEL diffraction, which better estimates the experimental signal, delivering a high-resolution XFEL structure (1.75 Å), using fewer crystals than previously required for this resolution. The crystal lattice and protein core are conserved compared with a polyhedrin with less than 10% sequence identity. We explain how the conserved biological phenotype, the crystal lattice, is maintained in the face of extreme environmental challenge and massive evolutionary divergence. Our improved methods should open up more challenging biological samples to XFEL analysis.

Published
2015

35. A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses

Author

Tan, Tiong Kit, Rijal, Pramila, Rahikainen, Rolle, Keeble, Anthony H., Schimanski, Lisa, Hussain, Saira, Harvey, Ruth, Hayes, Jack W. P., Edwards, Jane C., McLean, Rebecca K., Martini, Veronica, Pedrera, Miriam, Thakur, Nazia, Conceicao, Carina, Dietrich, Isabelle, Shelton, Holly, Ludi, Anna, Wilsden, Ginette, Browning, Clare, Zagrajek, Adrian K., Bialy, Dagmara, Bhat, Sushant, Stevenson-Leggett, Phoebe, Hollinghurst, Philippa, Tully, Matthew, Moffat, Katy, Chiu, Chris, Waters, Ryan, Gray, Ashley, Azhar, Mehreen, Mioulet, Valerie, Newman, Joseph, Asfor, Amin S., Burman, Alison, Crossley, Sylvia, Hammond, John A., Tchilian, Elma, Charleston, Bryan, Bailey, Dalan, Tuthill, Tobias J., Graham, Simon P., Duyvesteyn, Helen M. E., Malinauskas, Tomas, Huo, Jiandong, Tree, Julia A., Buttigieg, Karen R., Owens, Raymond J., Carroll, Miles W., Daniels, Rodney S., McCauley, John W., Stuart, David I., Huang, Kuan-Ying A., Howarth, Mark, and Townsend, Alain R.

Published
2021
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36. Publisher Correction: Bispecific repurposed medicines targeting the viral and immunological arms of COVID-19

Author

Redhead, Martin A., Owen, C. David, Brewitz, Lennart, Collette, Amelia H., Lukacik, Petra, Strain-Damerell, Claire, Robinson, Sean W., Collins, Patrick M., Schäfer, Philipp, Swindells, Mark, Radoux, Chris J., Hopkins, Iva Navratilova, Fearon, Daren, Douangamath, Alice, von Delft, Frank, Malla, Tika R., Vangeel, Laura, Vercruysse, Thomas, Thibaut, Jan, Leyssen, Pieter, Nguyen, Tu-Trinh, Hull, Mitchell, Tumber, Anthony, Hallett, David J., Schofield, Christopher J., Stuart, David I., Hopkins, Andrew L., and Walsh, Martin A.

Published
2021
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39. Bispecific repurposed medicines targeting the viral and immunological arms of COVID-19

Author

Redhead, Martin A., Owen, C. David, Brewitz, Lennart, Collette, Amelia H., Lukacik, Petra, Strain-Damerell, Claire, Robinson, Sean W., Collins, Patrick M., Schäfer, Philipp, Swindells, Mark, Radoux, Chris J., Hopkins, Iva Navratilova, Fearon, Daren, Douangamath, Alice, von Delft, Frank, Malla, Tika R., Vangeel, Laura, Vercruysse, Thomas, Thibaut, Jan, Leyssen, Pieter, Nguyen, Tu-Trinh, Hull, Mitchell, Tumber, Anthony, Hallett, David J., Schofield, Christopher J., Stuart, David I., Hopkins, Andrew L., and Walsh, Martin A.

Published
2021
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41. COVID-19 therapeutics: stewardship in England and considerations for antimicrobial resistance

Author

Bou-Antoun, Sabine, primary, Rokadiya, Sakib, additional, Ashiru-Oredope, Diane, additional, Demirjian, Alicia, additional, Sherwood, Emma, additional, Ellaby, Nicholas, additional, Gerver, Sarah, additional, Grossi, Carlota, additional, Harman, Katie, additional, Hartman, Hassan, additional, Lochen, Alessandra, additional, Ragonnet-Cronin, Manon, additional, Squire, Hanna, additional, Sutton, J Mark, additional, Thelwall, Simon, additional, Tree, Julia, additional, Bahar, Mohammad W, additional, Stuart, David I, additional, Brown, Colin S, additional, Chand, Meera, additional, and Hopkins, Susan, additional

Published
2023
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42. Snapshots from Cryo-ET of active SARS-CoV-2 virions

Author

Fukuhara, Hideo, primary, Dokainish, Hisham M., additional, Kita, Shunsuke, additional, Tabata, Koshiro, additional, Takasu, Akira, additional, Huiskonen, Juha T., additional, Anraku, Yuki, additional, Senda, Toshiya, additional, Stuart, David I., additional, Sasaki, Michihito, additional, Orba, Yasuko, additional, Suzuki, Yasuhiko, additional, Sawa, Hirofumi, additional, and Maenaka, Katsumi, additional

Published
2023
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45. Glycogen Phosphorylase b

Author

Johnson, Louise N., primary, Hajdu, Janos, additional, Acharya, K. Ravindra, additional, Stuart, David I., additional, McLaughlin, Paul J., additional, Oikonomakos, Nikos G., additional, and Barford, David, additional

Published
2020
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