IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-31193-8.html
   My bibliography  Save this article

SpySwitch enables pH- or heat-responsive capture and release for plug-and-display nanoassembly

Author

Listed:
  • Susan K. Vester

    (University of Oxford)

  • Rolle Rahikainen

    (University of Oxford
    Tampere University)

  • Irsyad N. A. Khairil Anuar

    (University of Oxford
    LiliumX Ltd, WE.306 Westbourne Studios)

  • Rory A. Hills

    (University of Oxford)

  • Tiong Kit Tan

    (University of Oxford)

  • Mark Howarth

    (University of Oxford)

Abstract

Proteins can be empowered via SpyTag for anchoring and nanoassembly, through covalent bonding to SpyCatcher partners. Here we generate a switchable version of SpyCatcher, allowing gentle purification of SpyTagged proteins. We introduce numerous histidines adjacent to SpyTag’s binding site, giving moderate pH-dependent release. After phage-based selection, our final SpySwitch allows purification of SpyTag- and SpyTag003-fusions from bacterial or mammalian culture by capture at neutral pH and release at pH 5, with purity far beyond His-tag methods. SpySwitch is also thermosensitive, capturing at 4 °C and releasing at 37 °C. With flexible choice of eluent, SpySwitch-purified proteins can directly assemble onto multimeric scaffolds. 60-mer multimerization enhances immunogenicity and we use SpySwitch to purify receptor-binding domains from SARS-CoV-2 and 11 other sarbecoviruses. For these receptor-binding domains we determine thermal resilience (for mosaic vaccine development) and cross-recognition by antibodies. Antibody EY6A reacts across all tested sarbecoviruses, towards potential application against new coronavirus pandemic threats.

Suggested Citation

  • Susan K. Vester & Rolle Rahikainen & Irsyad N. A. Khairil Anuar & Rory A. Hills & Tiong Kit Tan & Mark Howarth, 2022. "SpySwitch enables pH- or heat-responsive capture and release for plug-and-display nanoassembly," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-31193-8
    DOI: 10.1038/s41467-022-31193-8
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-31193-8
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-022-31193-8?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Jun Lan & Jiwan Ge & Jinfang Yu & Sisi Shan & Huan Zhou & Shilong Fan & Qi Zhang & Xuanling Shi & Qisheng Wang & Linqi Zhang & Xinquan Wang, 2020. "Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor," Nature, Nature, vol. 581(7807), pages 215-220, May.
    2. Tyler N. Starr & Nadine Czudnochowski & Zhuoming Liu & Fabrizia Zatta & Young-Jun Park & Amin Addetia & Dora Pinto & Martina Beltramello & Patrick Hernandez & Allison J. Greaney & Roberta Marzi & Will, 2021. "SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape," Nature, Nature, vol. 597(7874), pages 97-102, September.
    3. Ryo Matsunaga & Saeko Yanaka & Satoru Nagatoishi & Kouhei Tsumoto, 2013. "Hyperthin nanochains composed of self-polymerizing protein shackles," Nature Communications, Nature, vol. 4(1), pages 1-10, October.
    4. Cyrielle Fougeroux & Louise Goksøyr & Manja Idorn & Vladislav Soroka & Sebenzile K. Myeni & Robert Dagil & Christoph M. Janitzek & Max Søgaard & Kara-Lee Aves & Emma W. Horsted & Sayit Mahmut Erdoğan , 2021. "Capsid-like particles decorated with the SARS-CoV-2 receptor-binding domain elicit strong virus neutralization activity," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    5. Christopher O. Barnes & Claudia A. Jette & Morgan E. Abernathy & Kim-Marie A. Dam & Shannon R. Esswein & Harry B. Gristick & Andrey G. Malyutin & Naima G. Sharaf & Kathryn E. Huey-Tubman & Yu E. Lee &, 2020. "SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies," Nature, Nature, vol. 588(7839), pages 682-687, December.
    6. Tiong Kit Tan & Pramila Rijal & Rolle Rahikainen & Anthony H. Keeble & Lisa Schimanski & Saira Hussain & Ruth Harvey & Jack W. P. Hayes & Jane C. Edwards & Rebecca K. McLean & Veronica Martini & Miria, 2021. "A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    Full references (including those not matched with items on IDEAS)

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Claudia L. Driscoll & Anthony H. Keeble & Mark R. Howarth, 2024. "SpyMask enables combinatorial assembly of bispecific binders," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Kuan-Ying A. Huang & Xiaorui Chen & Arpita Mohapatra & Hong Thuy Vy Nguyen & Lisa Schimanski & Tiong Kit Tan & Pramila Rijal & Susan K. Vester & Rory A. Hills & Mark Howarth & Jennifer R. Keeffe & Ale, 2023. "Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Yin-Feng Kang & Cong Sun & Jing Sun & Chu Xie & Zhen Zhuang & Hui-Qin Xu & Zheng Liu & Yi-Hao Liu & Sui Peng & Run-Yu Yuan & Jin-Cun Zhao & Mu-Sheng Zeng, 2022. "Quadrivalent mosaic HexaPro-bearing nanoparticle vaccine protects against infection of SARS-CoV-2 variants," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Leire Campos-Mata & Benjamin Trinité & Andrea Modrego & Sonia Tejedor Vaquero & Edwards Pradenas & Anna Pons-Grífols & Natalia Rodrigo Melero & Diego Carlero & Silvia Marfil & César Santiago & Dàlia R, 2024. "A monoclonal antibody targeting a large surface of the receptor binding motif shows pan-neutralizing SARS-CoV-2 activity," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    3. Kuan-Ying A. Huang & Xiaorui Chen & Arpita Mohapatra & Hong Thuy Vy Nguyen & Lisa Schimanski & Tiong Kit Tan & Pramila Rijal & Susan K. Vester & Rory A. Hills & Mark Howarth & Jennifer R. Keeffe & Ale, 2023. "Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. Tingting Li & Xiaojian Han & Chenjian Gu & Hangtian Guo & Huajun Zhang & Yingming Wang & Chao Hu & Kai Wang & Fengjiang Liu & Feiyang Luo & Yanan Zhang & Jie Hu & Wang Wang & Shenglong Li & Yanan Hao , 2021. "Potent SARS-CoV-2 neutralizing antibodies with protective efficacy against newly emerged mutational variants," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    5. Andrew C. Hunt & Bastian Vögeli & Ahmed O. Hassan & Laura Guerrero & Weston Kightlinger & Danielle J. Yoesep & Antje Krüger & Madison DeWinter & Michael S. Diamond & Ashty S. Karim & Michael C. Jewett, 2023. "A rapid cell-free expression and screening platform for antibody discovery," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    6. Mingxi Li & Yifei Ren & Zhen Qin Aw & Bo Chen & Ziqing Yang & Yuqing Lei & Lin Cheng & Qingtai Liang & Junxian Hong & Yiling Yang & Jing Chen & Yi Hao Wong & Jing Wei & Sisi Shan & Senyan Zhang & Jiwa, 2022. "Broadly neutralizing and protective nanobodies against SARS-CoV-2 Omicron subvariants BA.1, BA.2, and BA.4/5 and diverse sarbecoviruses," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    7. Timothy J. C. Tan & Zongjun Mou & Ruipeng Lei & Wenhao O. Ouyang & Meng Yuan & Ge Song & Raiees Andrabi & Ian A. Wilson & Collin Kieffer & Xinghong Dai & Kenneth A. Matreyek & Nicholas C. Wu, 2023. "High-throughput identification of prefusion-stabilizing mutations in SARS-CoV-2 spike," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    8. Shawn B. Egri & Xue Wang & Marco A. Díaz-Salinas & Jeremy Luban & Natalya V. Dudkina & James B. Munro & Kuang Shen, 2023. "Detergent modulates the conformational equilibrium of SARS-CoV-2 Spike during cryo-EM structural determination," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    9. Romain Rouet & Jake Y. Henry & Matt D. Johansen & Meghna Sobti & Harikrishnan Balachandran & David B. Langley & Gregory J. Walker & Helen Lenthall & Jennifer Jackson & Stephanie Ubiparipovic & Ohan Ma, 2023. "Broadly neutralizing SARS-CoV-2 antibodies through epitope-based selection from convalescent patients," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    10. Chunyan Wang & Emma L. Hesketh & Tatiana M. Shamorkina & Wentao Li & Peter J. Franken & Dubravka Drabek & Rien Haperen & Sarah Townend & Frank J. M. Kuppeveld & Frank Grosveld & Neil A. Ranson & Joost, 2022. "Antigenic structure of the human coronavirus OC43 spike reveals exposed and occluded neutralizing epitopes," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    11. Jun-Yu Si & Yuan-Mei Chen & Ye-Hui Sun & Meng-Xue Gu & Mei-Ling Huang & Lu-Lu Shi & Xiao Yu & Xiao Yang & Qing Xiong & Cheng-Bao Ma & Peng Liu & Zheng-Li Shi & Huan Yan, 2024. "Sarbecovirus RBD indels and specific residues dictating multi-species ACE2 adaptiveness," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    12. Christian Hentrich & Mateusz Putyrski & Hanh Hanuschka & Waldemar Preis & Sarah-Jane Kellmann & Melissa Wich & Manuel Cavada & Sarah Hanselka & Victor S. Lelyveld & Francisco Ylera, 2024. "Engineered reversible inhibition of SpyCatcher reactivity enables rapid generation of bispecific antibodies," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    13. Zhiqiang Ku & Xuping Xie & Jianqing Lin & Peng Gao & Bin Wu & Abbas El Sahili & Hang Su & Yang Liu & Xiaohua Ye & Eddie Yongjun Tan & Xin Li & Xuejun Fan & Boon Chong Goh & Wei Xiong & Hannah Boyd & A, 2022. "Engineering SARS-CoV-2 specific cocktail antibodies into a bispecific format improves neutralizing potency and breadth," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    14. Hannah McClymont & Wenbiao Hu, 2021. "Weather Variability and COVID-19 Transmission: A Review of Recent Research," IJERPH, MDPI, vol. 18(2), pages 1-19, January.
    15. Haisheng Yu & Banghui Liu & Yudi Zhang & Xijie Gao & Qian Wang & Haitao Xiang & Xiaofang Peng & Caixia Xie & Yaping Wang & Peiyu Hu & Jingrong Shi & Quan Shi & Pingqian Zheng & Chengqian Feng & Guofan, 2023. "Somatically hypermutated antibodies isolated from SARS-CoV-2 Delta infected patients cross-neutralize heterologous variants," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    16. Wenkai Han & Ningning Chen & Xinzhou Xu & Adil Sahil & Juexiao Zhou & Zhongxiao Li & Huawen Zhong & Elva Gao & Ruochi Zhang & Yu Wang & Shiwei Sun & Peter Pak-Hang Cheung & Xin Gao, 2023. "Predicting the antigenic evolution of SARS-COV-2 with deep learning," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    17. Seoryeong Park & Jaewon Choi & Yonghee Lee & Jinsung Noh & Namphil Kim & JinAh Lee & Geummi Cho & Sujeong Kim & Duck Kyun Yoo & Chang Kyung Kang & Pyoeng Gyun Choe & Nam Joong Kim & Wan Beom Park & Se, 2024. "An ancestral SARS-CoV-2 vaccine induces anti-Omicron variants antibodies by hypermutation," Nature Communications, Nature, vol. 15(1), pages 1-9, December.
    18. Ioannis Kontoyiannis & Lambros Mertzanis & Athina Panotopoulou & Ioannis Papageorgiou & Maria Skoularidou, 2022. "Bayesian context trees: Modelling and exact inference for discrete time series," Journal of the Royal Statistical Society Series B, Royal Statistical Society, vol. 84(4), pages 1287-1323, September.
    19. Biao Zhou & Runhong Zhou & Bingjie Tang & Jasper Fuk-Woo Chan & Mengxiao Luo & Qiaoli Peng & Shuofeng Yuan & Hang Liu & Bobo Wing-Yee Mok & Bohao Chen & Pui Wang & Vincent Kwok-Man Poon & Hin Chu & Ch, 2022. "A broadly neutralizing antibody protects Syrian hamsters against SARS-CoV-2 Omicron challenge," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    20. Nikhil Kumar Tulsian & Raghuvamsi Venkata Palur & Xinlei Qian & Yue Gu & Bhuvaneshwari D/O Shunmuganathan & Firdaus Samsudin & Yee Hwa Wong & Jianqing Lin & Kiren Purushotorman & Mary McQueen Kozma & , 2023. "Defining neutralization and allostery by antibodies against COVID-19 variants," Nature Communications, Nature, vol. 14(1), pages 1-23, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-31193-8. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.