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Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41594-020-0478-5
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dc.titleA thermostable, closed SARS-CoV-2 spike protein trimer
dc.contributor.authorXiong, Xiaoli
dc.contributor.authorQu, Kun
dc.contributor.authorCiazynska, Katarzyna A
dc.contributor.authorHosmillo, Myra
dc.contributor.authorCarter, Andrew P
dc.contributor.authorEbrahimi, Soraya
dc.contributor.authorKe, Zunlong
dc.contributor.authorScheres, Sjors HW
dc.contributor.authorBergamaschi, Laura
dc.contributor.authorGrice, Guinevere L
dc.contributor.authorZhang, Ying
dc.contributor.authorNathan, James A
dc.contributor.authorBaker, Stephen
dc.contributor.authorJames, Leo C
dc.contributor.authorBaxendale, Helen E
dc.contributor.authorGoodfellow, Ian
dc.contributor.authorDoffinger, Rainer
dc.contributor.authorBriggs, John AG
dc.contributor.authorBradley, John
dc.contributor.authorLyons, Paul A
dc.contributor.authorSmith, Kenneth GC
dc.contributor.authorToshner, Mark
dc.contributor.authorElmer, Anne
dc.contributor.authorRibeiro, Carla
dc.contributor.authorKourampa, Jenny
dc.contributor.authorJose, Sherly
dc.contributor.authorKennet, Jane
dc.contributor.authorRowlands, Jane
dc.contributor.authorMeadows, Anne
dc.contributor.authorO'Brien, Criona
dc.contributor.authorRastall, Rebecca
dc.contributor.authorCrucusio, Cherry
dc.contributor.authorHewitt, Sarah
dc.contributor.authorPrice, Jane
dc.contributor.authorCalder, Jo
dc.contributor.authorCanna, Laura
dc.contributor.authorBucke, Ashlea
dc.contributor.authorTordesillas, Hugo
dc.contributor.authorHarris, Julie
dc.contributor.authorRuffolo, Valentina
dc.contributor.authorDomingo, Jason
dc.contributor.authorGraves, Barbara
dc.contributor.authorButcher, Helen
dc.contributor.authorCaputo, Daniela
dc.contributor.authorLe Gresley, Emma
dc.contributor.authorDunmore, Benjamin J
dc.contributor.authorMartin, Jennifer
dc.contributor.authorLegchenko, Ekaterina
dc.contributor.authorTreacy, Carmen
dc.contributor.authorHuang, Christopher
dc.contributor.authorWood, Jennifer
dc.contributor.authorSutcliffe, Rachel
dc.contributor.authorHodgson, Josh
dc.contributor.authorShih, Joy
dc.contributor.authorGraf, Stefan
dc.contributor.authorTong, Zhen
dc.contributor.authorMescia, Federica
dc.contributor.authorTilly, Tobias
dc.contributor.authorO'Donnell, Ciara
dc.contributor.authorHunter, Kelvin
dc.contributor.authorPointon, Linda
dc.contributor.authorPond, Nicole
dc.contributor.authorWylot, Marta
dc.contributor.authorJones, Emma
dc.contributor.authorFawke, Stuart
dc.contributor.authorBullman, Ben
dc.contributor.authorBergamaschi, Laura
dc.contributor.authorTurner, Lori
dc.contributor.authorJarvis, Isobel
dc.contributor.authorOmarjee, Ommar
dc.contributor.authorDe Sa, Aloka
dc.contributor.authorMarsden, Joe
dc.contributor.authorBetancourt, Ariana
dc.contributor.authorPerera, Marianne
dc.contributor.authorEpping, Maddie
dc.contributor.authorRichoz, Nathan
dc.contributor.authorBower, Georgie
dc.contributor.authorSharma, Rahul
dc.contributor.authorNice, Francesca
dc.contributor.authorHuhn, Oisin
dc.contributor.authorStark, Hannah
dc.contributor.authorWalker, Neil
dc.contributor.authorStirrups, Kathy
dc.contributor.authorOvington, Nigel
dc.contributor.authorDewhust, Eleanor
dc.contributor.authorLi, Emily
dc.contributor.authorPapadia, Sofia
dc.date.accessioned2024-04-02T04:02:16Z
dc.date.available2024-04-02T04:02:16Z
dc.date.issued2020-10
dc.identifier.citationXiong, 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
dc.identifier.issn1545-9993
dc.identifier.issn1545-9985
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/247695
dc.description.abstractThe 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.
dc.language.isoen
dc.publisherNATURE PORTFOLIO
dc.sourceElements
dc.subjectScience & Technology
dc.subjectLife Sciences & Biomedicine
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectCell Biology
dc.subjectBEAM-INDUCED MOTION
dc.subjectCRYO-EM
dc.subjectCORONAVIRUS
dc.subjectVACCINE
dc.typeArticle
dc.date.updated2024-04-01T09:21:05Z
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1038/s41594-020-0478-5
dc.description.sourcetitleNATURE STRUCTURAL & MOLECULAR BIOLOGY
dc.description.volume27
dc.description.issue10
dc.description.page934-941
dc.published.statePublished
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