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https://doi.org/10.1038/s41594-020-0478-5
| Title: | A thermostable, closed SARS-CoV-2 spike protein trimer | Authors: | Xiong, Xiaoli Qu, Kun Ciazynska, Katarzyna A Hosmillo, Myra Carter, Andrew P Ebrahimi, Soraya Ke, Zunlong Scheres, Sjors HW Bergamaschi, Laura Grice, Guinevere L Zhang, Ying Nathan, James A Baker, Stephen James, Leo C Baxendale, Helen E Goodfellow, Ian Doffinger, Rainer Briggs, John AG Bradley, John Lyons, Paul A Smith, Kenneth GC Toshner, Mark Elmer, Anne Ribeiro, Carla Kourampa, Jenny Jose, Sherly Kennet, Jane Rowlands, Jane Meadows, Anne O'Brien, Criona Rastall, Rebecca Crucusio, Cherry Hewitt, Sarah Price, Jane Calder, Jo Canna, Laura Bucke, Ashlea Tordesillas, Hugo Harris, Julie Ruffolo, Valentina Domingo, Jason Graves, Barbara Butcher, Helen Caputo, Daniela Le Gresley, Emma Dunmore, Benjamin J Martin, Jennifer Legchenko, Ekaterina Treacy, Carmen Huang, Christopher Wood, Jennifer Sutcliffe, Rachel Hodgson, Josh Shih, Joy Graf, Stefan Tong, Zhen Mescia, Federica Tilly, Tobias O'Donnell, Ciara Hunter, Kelvin Pointon, Linda Pond, Nicole Wylot, Marta Jones, Emma Fawke, Stuart Bullman, Ben Bergamaschi, Laura Turner, Lori Jarvis, Isobel Omarjee, Ommar De Sa, Aloka Marsden, Joe Betancourt, Ariana Perera, Marianne Epping, Maddie Richoz, Nathan Bower, Georgie Sharma, Rahul Nice, Francesca Huhn, Oisin Stark, Hannah Walker, Neil Stirrups, Kathy Ovington, Nigel Dewhust, Eleanor Li, Emily Papadia, Sofia |
Keywords: | Science & Technology Life Sciences & Biomedicine Biochemistry & Molecular Biology Biophysics Cell Biology BEAM-INDUCED MOTION CRYO-EM CORONAVIRUS VACCINE |
Issue Date: | Oct-2020 | Publisher: | NATURE PORTFOLIO | Citation: | Xiong, Xiaoli, Qu, Kun, Ciazynska, Katarzyna A, Hosmillo, Myra, Carter, Andrew P, Ebrahimi, Soraya, Ke, Zunlong, Scheres, Sjors HW, Bergamaschi, Laura, Grice, Guinevere L, Zhang, Ying, Nathan, James A, Baker, Stephen, James, Leo C, Baxendale, Helen E, Goodfellow, Ian, Doffinger, Rainer, Briggs, John AG, Bradley, John, Lyons, Paul A, Smith, Kenneth GC, Toshner, Mark, Elmer, Anne, Ribeiro, Carla, Kourampa, Jenny, Jose, Sherly, Kennet, Jane, Rowlands, Jane, Meadows, Anne, O'Brien, Criona, Rastall, Rebecca, Crucusio, Cherry, Hewitt, Sarah, Price, Jane, Calder, Jo, Canna, Laura, Bucke, Ashlea, Tordesillas, Hugo, Harris, Julie, Ruffolo, Valentina, Domingo, Jason, Graves, Barbara, Butcher, Helen, Caputo, Daniela, Le Gresley, Emma, Dunmore, Benjamin J, Martin, Jennifer, Legchenko, Ekaterina, Treacy, Carmen, Huang, Christopher, Wood, Jennifer, Sutcliffe, Rachel, Hodgson, Josh, Shih, Joy, Graf, Stefan, Tong, Zhen, Mescia, Federica, Tilly, Tobias, O'Donnell, Ciara, Hunter, Kelvin, Pointon, Linda, Pond, Nicole, Wylot, Marta, Jones, Emma, Fawke, Stuart, Bullman, Ben, Bergamaschi, Laura, Turner, Lori, Jarvis, Isobel, Omarjee, Ommar, De Sa, Aloka, Marsden, Joe, Betancourt, Ariana, Perera, Marianne, Epping, Maddie, Richoz, Nathan, Bower, Georgie, Sharma, Rahul, Nice, Francesca, Huhn, Oisin, Stark, Hannah, Walker, Neil, Stirrups, Kathy, Ovington, Nigel, Dewhust, Eleanor, Li, Emily, Papadia, Sofia (2020-10). A thermostable, closed SARS-CoV-2 spike protein trimer. NATURE STRUCTURAL & MOLECULAR BIOLOGY 27 (10) : 934-941. ScholarBank@NUS Repository. https://doi.org/10.1038/s41594-020-0478-5 | Abstract: | The spike (S) protein of SARS-CoV-2 mediates receptor binding and cell entry and is the dominant target of the immune system. It exhibits substantial conformational flexibility. It transitions from closed to open conformations to expose its receptor-binding site and, subsequently, from prefusion to postfusion conformations to mediate fusion of viral and cellular membranes. S-protein derivatives are components of vaccine candidates and diagnostic assays, as well as tools for research into the biology and immunology of SARS-CoV-2. Here we have designed mutations in S that allow the production of thermostable, disulfide-bonded S-protein trimers that are trapped in the closed, prefusion state. Structures of the disulfide-stabilized and non-disulfide-stabilized proteins reveal distinct closed and locked conformations of the S trimer. We demonstrate that the designed, thermostable, closed S trimer can be used in serological assays. This protein has potential applications as a reagent for serology, virology and as an immunogen. | Source Title: | NATURE STRUCTURAL & MOLECULAR BIOLOGY | URI: | https://scholarbank.nus.edu.sg/handle/10635/247695 | ISSN: | 1545-9993 1545-9985 |
DOI: | 10.1038/s41594-020-0478-5 |
| Appears in Collections: | Staff Publications Elements |
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