Capsid-like particles decorated with the SARS-CoV-2 receptor-binding domain elicit strong virus neutralization activity

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Capsid-like particles decorated with the SARS-CoV-2 receptor-binding domain elicit strong virus neutralization activity. / Fougeroux, Cyrielle; Goksøyr, Louise; Idorn, Manja; Soroka, Vladislav; Myeni, Sebenzile K; Dagil, Robert; Janitzek, Christoph M; Søgaard, Max; Aves, Kara-Lee; Horsted, Emma W; Erdogan, Sayit Mahmut; Gustavsson, Tobias; Dorosz, Jerzy; Clemmensen, Stine; Fredsgaard, Laurits; Thrane, Susan; Vidal-Calvo, Elena E; Khalifé, Paul; Hulen, Thomas M; Choudhary, Swati; Theisen, Michael; Singh, Susheel K; Garcia-Senosiain, Asier; Van Oosten, Linda; Pijlman, Gorben; Hierzberger, Bettina; Domeyer, Tanja; Nalewajek, Blanka W; Strøbæk, Anette; Skrzypczak, Magdalena; Andersson, Laura F; Buus, Søren; Buus, Anette Stryhn; Christensen, Jan Pravsgaard; Dalebout, Tim J; Iversen, Kasper; Harritshøj, Lene H; Mordmüller, Benjamin; Ullum, Henrik; Reinert, Line S; de Jongh, Willem Adriaan; Kikkert, Marjolein; Paludan, Søren R; Theander, Thor G; Nielsen, Morten A; Salanti, Ali; Sander, Adam F.

In: Nature Communications, Vol. 12, No. 1, 2021, p. 324.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Fougeroux, C, Goksøyr, L, Idorn, M, Soroka, V, Myeni, SK, Dagil, R, Janitzek, CM, Søgaard, M, Aves, K-L, Horsted, EW, Erdogan, SM, Gustavsson, T, Dorosz, J, Clemmensen, S, Fredsgaard, L, Thrane, S, Vidal-Calvo, EE, Khalifé, P, Hulen, TM, Choudhary, S, Theisen, M, Singh, SK, Garcia-Senosiain, A, Van Oosten, L, Pijlman, G, Hierzberger, B, Domeyer, T, Nalewajek, BW, Strøbæk, A, Skrzypczak, M, Andersson, LF, Buus, S, Buus, AS, Christensen, JP, Dalebout, TJ, Iversen, K, Harritshøj, LH, Mordmüller, B, Ullum, H, Reinert, LS, de Jongh, WA, Kikkert, M, Paludan, SR, Theander, TG, Nielsen, MA, Salanti, A & Sander, AF 2021, 'Capsid-like particles decorated with the SARS-CoV-2 receptor-binding domain elicit strong virus neutralization activity', Nature Communications, vol. 12, no. 1, pp. 324. https://doi.org/10.1038/s41467-020-20251-8

APA

Fougeroux, C., Goksøyr, L., Idorn, M., Soroka, V., Myeni, S. K., Dagil, R., Janitzek, C. M., Søgaard, M., Aves, K-L., Horsted, E. W., Erdogan, S. M., Gustavsson, T., Dorosz, J., Clemmensen, S., Fredsgaard, L., Thrane, S., Vidal-Calvo, E. E., Khalifé, P., Hulen, T. M., ... Sander, A. F. (2021). Capsid-like particles decorated with the SARS-CoV-2 receptor-binding domain elicit strong virus neutralization activity. Nature Communications, 12(1), 324. https://doi.org/10.1038/s41467-020-20251-8

Vancouver

Fougeroux C, Goksøyr L, Idorn M, Soroka V, Myeni SK, Dagil R et al. Capsid-like particles decorated with the SARS-CoV-2 receptor-binding domain elicit strong virus neutralization activity. Nature Communications. 2021;12(1):324. https://doi.org/10.1038/s41467-020-20251-8

Author

Fougeroux, Cyrielle ; Goksøyr, Louise ; Idorn, Manja ; Soroka, Vladislav ; Myeni, Sebenzile K ; Dagil, Robert ; Janitzek, Christoph M ; Søgaard, Max ; Aves, Kara-Lee ; Horsted, Emma W ; Erdogan, Sayit Mahmut ; Gustavsson, Tobias ; Dorosz, Jerzy ; Clemmensen, Stine ; Fredsgaard, Laurits ; Thrane, Susan ; Vidal-Calvo, Elena E ; Khalifé, Paul ; Hulen, Thomas M ; Choudhary, Swati ; Theisen, Michael ; Singh, Susheel K ; Garcia-Senosiain, Asier ; Van Oosten, Linda ; Pijlman, Gorben ; Hierzberger, Bettina ; Domeyer, Tanja ; Nalewajek, Blanka W ; Strøbæk, Anette ; Skrzypczak, Magdalena ; Andersson, Laura F ; Buus, Søren ; Buus, Anette Stryhn ; Christensen, Jan Pravsgaard ; Dalebout, Tim J ; Iversen, Kasper ; Harritshøj, Lene H ; Mordmüller, Benjamin ; Ullum, Henrik ; Reinert, Line S ; de Jongh, Willem Adriaan ; Kikkert, Marjolein ; Paludan, Søren R ; Theander, Thor G ; Nielsen, Morten A ; Salanti, Ali ; Sander, Adam F. / Capsid-like particles decorated with the SARS-CoV-2 receptor-binding domain elicit strong virus neutralization activity. In: Nature Communications. 2021 ; Vol. 12, No. 1. pp. 324.

Bibtex

@article{142c1c583ba5495bad00021bfd0f9fe3,
title = "Capsid-like particles decorated with the SARS-CoV-2 receptor-binding domain elicit strong virus neutralization activity",
abstract = "The rapid development of a SARS-CoV-2 vaccine is a global priority. Here, we develop two capsid-like particle (CLP)-based vaccines displaying the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein. RBD antigens are displayed on AP205 CLPs through a split-protein Tag/Catcher, ensuring unidirectional and high-density display of RBD. Both soluble recombinant RBD and RBD displayed on CLPs bind the ACE2 receptor with nanomolar affinity. Mice are vaccinated with soluble RBD or CLP-displayed RBD, formulated in Squalene-Water-Emulsion. The RBD-CLP vaccines induce higher levels of serum anti-spike antibodies than the soluble RBD vaccines. Remarkably, one injection with our lead RBD-CLP vaccine in mice elicits virus neutralization antibody titers comparable to those found in patients that had recovered from COVID-19. Following booster vaccinations, the virus neutralization titers exceed those measured after natural infection, at serum dilutions above 1:10,000. Thus, the RBD-CLP vaccine is a highly promising candidate for preventing COVID-19.",
author = "Cyrielle Fougeroux and Louise Goks{\o}yr and Manja Idorn and Vladislav Soroka and Myeni, {Sebenzile K} and Robert Dagil and Janitzek, {Christoph M} and Max S{\o}gaard and Kara-Lee Aves and Horsted, {Emma W} and Erdogan, {Sayit Mahmut} and Tobias Gustavsson and Jerzy Dorosz and Stine Clemmensen and Laurits Fredsgaard and Susan Thrane and Vidal-Calvo, {Elena E} and Paul Khalif{\'e} and Hulen, {Thomas M} and Swati Choudhary and Michael Theisen and Singh, {Susheel K} and Asier Garcia-Senosiain and {Van Oosten}, Linda and Gorben Pijlman and Bettina Hierzberger and Tanja Domeyer and Nalewajek, {Blanka W} and Anette Str{\o}b{\ae}k and Magdalena Skrzypczak and Andersson, {Laura F} and S{\o}ren Buus and Buus, {Anette Stryhn} and Christensen, {Jan Pravsgaard} and Dalebout, {Tim J} and Kasper Iversen and Harritsh{\o}j, {Lene H} and Benjamin Mordm{\"u}ller and Henrik Ullum and Reinert, {Line S} and {de Jongh}, {Willem Adriaan} and Marjolein Kikkert and Paludan, {S{\o}ren R} and Theander, {Thor G} and Nielsen, {Morten A} and Ali Salanti and Sander, {Adam F}",
year = "2021",
doi = "10.1038/s41467-020-20251-8",
language = "English",
volume = "12",
pages = "324",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Capsid-like particles decorated with the SARS-CoV-2 receptor-binding domain elicit strong virus neutralization activity

AU - Fougeroux, Cyrielle

AU - Goksøyr, Louise

AU - Idorn, Manja

AU - Soroka, Vladislav

AU - Myeni, Sebenzile K

AU - Dagil, Robert

AU - Janitzek, Christoph M

AU - Søgaard, Max

AU - Aves, Kara-Lee

AU - Horsted, Emma W

AU - Erdogan, Sayit Mahmut

AU - Gustavsson, Tobias

AU - Dorosz, Jerzy

AU - Clemmensen, Stine

AU - Fredsgaard, Laurits

AU - Thrane, Susan

AU - Vidal-Calvo, Elena E

AU - Khalifé, Paul

AU - Hulen, Thomas M

AU - Choudhary, Swati

AU - Theisen, Michael

AU - Singh, Susheel K

AU - Garcia-Senosiain, Asier

AU - Van Oosten, Linda

AU - Pijlman, Gorben

AU - Hierzberger, Bettina

AU - Domeyer, Tanja

AU - Nalewajek, Blanka W

AU - Strøbæk, Anette

AU - Skrzypczak, Magdalena

AU - Andersson, Laura F

AU - Buus, Søren

AU - Buus, Anette Stryhn

AU - Christensen, Jan Pravsgaard

AU - Dalebout, Tim J

AU - Iversen, Kasper

AU - Harritshøj, Lene H

AU - Mordmüller, Benjamin

AU - Ullum, Henrik

AU - Reinert, Line S

AU - de Jongh, Willem Adriaan

AU - Kikkert, Marjolein

AU - Paludan, Søren R

AU - Theander, Thor G

AU - Nielsen, Morten A

AU - Salanti, Ali

AU - Sander, Adam F

PY - 2021

Y1 - 2021

N2 - The rapid development of a SARS-CoV-2 vaccine is a global priority. Here, we develop two capsid-like particle (CLP)-based vaccines displaying the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein. RBD antigens are displayed on AP205 CLPs through a split-protein Tag/Catcher, ensuring unidirectional and high-density display of RBD. Both soluble recombinant RBD and RBD displayed on CLPs bind the ACE2 receptor with nanomolar affinity. Mice are vaccinated with soluble RBD or CLP-displayed RBD, formulated in Squalene-Water-Emulsion. The RBD-CLP vaccines induce higher levels of serum anti-spike antibodies than the soluble RBD vaccines. Remarkably, one injection with our lead RBD-CLP vaccine in mice elicits virus neutralization antibody titers comparable to those found in patients that had recovered from COVID-19. Following booster vaccinations, the virus neutralization titers exceed those measured after natural infection, at serum dilutions above 1:10,000. Thus, the RBD-CLP vaccine is a highly promising candidate for preventing COVID-19.

AB - The rapid development of a SARS-CoV-2 vaccine is a global priority. Here, we develop two capsid-like particle (CLP)-based vaccines displaying the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein. RBD antigens are displayed on AP205 CLPs through a split-protein Tag/Catcher, ensuring unidirectional and high-density display of RBD. Both soluble recombinant RBD and RBD displayed on CLPs bind the ACE2 receptor with nanomolar affinity. Mice are vaccinated with soluble RBD or CLP-displayed RBD, formulated in Squalene-Water-Emulsion. The RBD-CLP vaccines induce higher levels of serum anti-spike antibodies than the soluble RBD vaccines. Remarkably, one injection with our lead RBD-CLP vaccine in mice elicits virus neutralization antibody titers comparable to those found in patients that had recovered from COVID-19. Following booster vaccinations, the virus neutralization titers exceed those measured after natural infection, at serum dilutions above 1:10,000. Thus, the RBD-CLP vaccine is a highly promising candidate for preventing COVID-19.

U2 - 10.1038/s41467-020-20251-8

DO - 10.1038/s41467-020-20251-8

M3 - Journal article

C2 - 33436573

VL - 12

SP - 324

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

ER -

ID: 255401135