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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
Cell Biology
Issue Date: Oct-2020
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.
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.
ISSN: 1545-9993
DOI: 10.1038/s41594-020-0478-5
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