Protective efficacy of Ad26.COV2.S against SARS-CoV-2 B.1.351 in macaques
The emergence of SARS-CoV-2 variants that partially evade neutralizing antibodies poses a threat to the efficacy of current COVID-19 vaccines 1 , 2 . The Ad26.COV2.S vaccine expresses a stabilized spike protein from the WA1/2020 strain of SARS-CoV-2, and has recently demonstrated protective efficacy...
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| Published in | Nature (London) Vol. 596; no. 7872; pp. 423 - 427 |
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| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
19.08.2021
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | The emergence of SARS-CoV-2 variants that partially evade neutralizing antibodies poses a threat to the efficacy of current COVID-19 vaccines
1
,
2
. The Ad26.COV2.S vaccine expresses a stabilized spike protein from the WA1/2020 strain of SARS-CoV-2, and has recently demonstrated protective efficacy against symptomatic COVID-19 in humans in several geographical regions—including in South Africa, where 95% of sequenced viruses in cases of COVID-19 were the B.1.351 variant
3
. Here we show that Ad26.COV2.S elicits humoral and cellular immune responses that cross-react with the B.1.351 variant and protects against B.1.351 challenge in rhesus macaques. Ad26.COV2.S induced lower binding and neutralizing antibodies against B.1.351 as compared to WA1/2020, but elicited comparable CD8 and CD4 T cell responses against the WA1/2020, B.1.351, B.1.1.7, P.1 and CAL.20C variants. B.1.351 infection of control rhesus macaques resulted in higher levels of virus replication in bronchoalveolar lavage and nasal swabs than did WA1/2020 infection. Ad26.COV2.S provided robust protection against both WA1/2020 and B.1.351, although we observed higher levels of virus in vaccinated macaques after B.1.351 challenge. These data demonstrate that Ad26.COV2.S provided robust protection against B.1.351 challenge in rhesus macaques. Our findings have important implications for vaccine control of SARS-CoV-2 variants of concern.
SARS-CoV-2 challenge of rhesus macaques demonstrates that the Ad26.COV2.S vaccine induces robust protection against both the WA1/2020 isolate and the B.1.351 variant of concern. |
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| AbstractList | The emergence of SARS-CoV-2 variants that partially evade neutralizing antibodies poses a threat to the efficacy of current COVID-19 vaccines.sup.1,2. The Ad26.COV2.S vaccine expresses a stabilized spike protein from the WA1/2020 strain of SARS-CoV-2, and has recently demonstrated protective efficacy against symptomatic COVID-19 in humans in several geographical regions--including in South Africa, where 95% of sequenced viruses in cases of COVID-19 were the B.1.351 variant.sup.3. Here we show that Ad26.COV2.S elicits humoral and cellular immune responses that cross-react with the B.1.351 variant and protects against B.1.351 challenge in rhesus macaques. Ad26.COV2.S induced lower binding and neutralizing antibodies against B.1.351 as compared to WA1/2020, but elicited comparable CD8 and CD4 T cell responses against the WA1/2020, B.1.351, B.1.1.7, P.1 and CAL.20C variants. B.1.351 infection of control rhesus macaques resulted in higher levels of virus replication in bronchoalveolar lavage and nasal swabs than did WA1/2020 infection. Ad26.COV2.S provided robust protection against both WA1/2020 and B.1.351, although we observed higher levels of virus in vaccinated macaques after B.1.351 challenge. These data demonstrate that Ad26.COV2.S provided robust protection against B.1.351 challenge in rhesus macaques. Our findings have important implications for vaccine control of SARS-CoV-2 variants of concern. SARS-CoV-2 challenge of rhesus macaques demonstrates that the Ad26.COV2.S vaccine induces robust protection against both the WA1/2020 isolate and the B.1.351 variant of concern. The emergence of SARS-CoV-2 variants that partially evade neutralizing antibodies poses a threat to the efficacy of current COVID-19 vaccines 1 , 2 . The Ad26.COV2.S vaccine expresses a stabilized spike protein from the WA1/2020 strain of SARS-CoV-2, and has recently demonstrated protective efficacy against symptomatic COVID-19 in humans in several geographical regions—including in South Africa, where 95% of sequenced viruses in cases of COVID-19 were the B.1.351 variant 3 . Here we show that Ad26.COV2.S elicits humoral and cellular immune responses that cross-react with the B.1.351 variant and protects against B.1.351 challenge in rhesus macaques. Ad26.COV2.S induced lower binding and neutralizing antibodies against B.1.351 as compared to WA1/2020, but elicited comparable CD8 and CD4 T cell responses against the WA1/2020, B.1.351, B.1.1.7, P.1 and CAL.20C variants. B.1.351 infection of control rhesus macaques resulted in higher levels of virus replication in bronchoalveolar lavage and nasal swabs than did WA1/2020 infection. Ad26.COV2.S provided robust protection against both WA1/2020 and B.1.351, although we observed higher levels of virus in vaccinated macaques after B.1.351 challenge. These data demonstrate that Ad26.COV2.S provided robust protection against B.1.351 challenge in rhesus macaques. Our findings have important implications for vaccine control of SARS-CoV-2 variants of concern. SARS-CoV-2 challenge of rhesus macaques demonstrates that the Ad26.COV2.S vaccine induces robust protection against both the WA1/2020 isolate and the B.1.351 variant of concern. The emergence of SARS-CoV-2 variants that partially evade neutralizing antibodies poses a threat to the efficacy of current COVID-19 vaccines.sup.1,2. The Ad26.COV2.S vaccine expresses a stabilized spike protein from the WA1/2020 strain of SARS-CoV-2, and has recently demonstrated protective efficacy against symptomatic COVID-19 in humans in several geographical regions--including in South Africa, where 95% of sequenced viruses in cases of COVID-19 were the B.1.351 variant.sup.3. Here we show that Ad26.COV2.S elicits humoral and cellular immune responses that cross-react with the B.1.351 variant and protects against B.1.351 challenge in rhesus macaques. Ad26.COV2.S induced lower binding and neutralizing antibodies against B.1.351 as compared to WA1/2020, but elicited comparable CD8 and CD4 T cell responses against the WA1/2020, B.1.351, B.1.1.7, P.1 and CAL.20C variants. B.1.351 infection of control rhesus macaques resulted in higher levels of virus replication in bronchoalveolar lavage and nasal swabs than did WA1/2020 infection. Ad26.COV2.S provided robust protection against both WA1/2020 and B.1.351, although we observed higher levels of virus in vaccinated macaques after B.1.351 challenge. These data demonstrate that Ad26.COV2.S provided robust protection against B.1.351 challenge in rhesus macaques. Our findings have important implications for vaccine control of SARS-CoV-2 variants of concern. The emergence of SARS-CoV-2 variants that partially evade neutralizing antibodies poses a threat to the efficacy of current COVID-19 vaccines1,2. The Ad26.COV2.S vaccine expresses a stabilized spike protein from the WA1/2020 strain of SARS-CoV-2, and has recently demonstrated protective efficacy against symptomatic COVID-19 in humans in several geographical regions-including in South Africa, where 95% of sequenced viruses in cases of COVID-19 were the B.1.351 variant3. Here we show that Ad26.COV2.S elicits humoral and cellular immune responses that cross-react with the B.1.351 variant and protects against B.1.351 challenge in rhesus macaques. Ad26.COV2.S induced lower binding and neutralizing antibodies against B.1.351 as compared to WA1/2020, but elicited comparable CD8 and CD4 T cell responses against the WA1/2020, B.1.351, B.1.1.7, P.1 and CAL.20C variants. B.1.351 infection of control rhesus macaques resulted in higher levels of virus replication in bronchoalveolar lavage and nasal swabs than did WA1/2020 infection. Ad26.COV2.S provided robust protection against both WA1/2020 and B.1.351, although we observed higher levels of virus in vaccinated macaques after B.1.351 challenge. These data demonstrate that Ad26.COV2.S provided robust protection against B.1.351 challenge in rhesus macaques. Our findings have important implications for vaccine control of SARS-CoV-2 variants of concern.The emergence of SARS-CoV-2 variants that partially evade neutralizing antibodies poses a threat to the efficacy of current COVID-19 vaccines1,2. The Ad26.COV2.S vaccine expresses a stabilized spike protein from the WA1/2020 strain of SARS-CoV-2, and has recently demonstrated protective efficacy against symptomatic COVID-19 in humans in several geographical regions-including in South Africa, where 95% of sequenced viruses in cases of COVID-19 were the B.1.351 variant3. Here we show that Ad26.COV2.S elicits humoral and cellular immune responses that cross-react with the B.1.351 variant and protects against B.1.351 challenge in rhesus macaques. Ad26.COV2.S induced lower binding and neutralizing antibodies against B.1.351 as compared to WA1/2020, but elicited comparable CD8 and CD4 T cell responses against the WA1/2020, B.1.351, B.1.1.7, P.1 and CAL.20C variants. B.1.351 infection of control rhesus macaques resulted in higher levels of virus replication in bronchoalveolar lavage and nasal swabs than did WA1/2020 infection. Ad26.COV2.S provided robust protection against both WA1/2020 and B.1.351, although we observed higher levels of virus in vaccinated macaques after B.1.351 challenge. These data demonstrate that Ad26.COV2.S provided robust protection against B.1.351 challenge in rhesus macaques. Our findings have important implications for vaccine control of SARS-CoV-2 variants of concern. The emergence of SARS-CoV-2 variants that partially evade neutralizing antibodies poses a threat to the efficacy of current COVID-19 vaccines . The Ad26.COV2.S vaccine expresses a stabilized spike protein from the WA1/2020 strain of SARS-CoV-2, and has recently demonstrated protective efficacy against symptomatic COVID-19 in humans in several geographical regions-including in South Africa, where 95% of sequenced viruses in cases of COVID-19 were the B.1.351 variant . Here we show that Ad26.COV2.S elicits humoral and cellular immune responses that cross-react with the B.1.351 variant and protects against B.1.351 challenge in rhesus macaques. Ad26.COV2.S induced lower binding and neutralizing antibodies against B.1.351 as compared to WA1/2020, but elicited comparable CD8 and CD4 T cell responses against the WA1/2020, B.1.351, B.1.1.7, P.1 and CAL.20C variants. B.1.351 infection of control rhesus macaques resulted in higher levels of virus replication in bronchoalveolar lavage and nasal swabs than did WA1/2020 infection. Ad26.COV2.S provided robust protection against both WA1/2020 and B.1.351, although we observed higher levels of virus in vaccinated macaques after B.1.351 challenge. These data demonstrate that Ad26.COV2.S provided robust protection against B.1.351 challenge in rhesus macaques. Our findings have important implications for vaccine control of SARS-CoV-2 variants of concern. The emergence of SARS-CoV-2 variants that partially evade neutralizing antibodies poses a threat to the efficacy of current COVID-19 vaccines1,2. The Ad26.COV2.S vaccine expresses a stabilized spike protein from the WA1/2020 strain of SARS-CoV-2, and has recently demonstrated protective efficacy against symptomatic COVID-19 in humans in several geographical regions-including in South Africa, where 95% of sequenced viruses in cases of COVID-19 were the B.1.351 variant3. Here we show that Ad26.COV2.S elicits humoral and cellular immune responses that cross-react with the B.1.351 variant and protects against B.1.351 challenge in rhesus macaques. Ad26.COV2.S induced lower binding and neutralizing antibodies against B.1.351 as compared to WA1/2020, but elicited comparable CD8 and CD4 T cell responses against the WA1/2020, B.1.351, B.1.1.7, P.1 and CAL.20C variants. B.1.351 infection of control rhesus macaques resulted in higher levels of virus replication in bronchoalveolar lavage and nasal swabs than did WA1/2020 infection. Ad26.COV2.S provided robust protection against both WA1/2020 and B.1.351, although we observed higher levels of virus in vaccinated macaques after B.1.351 challenge. These data demonstrate that Ad26.COV2.S provided robust protection against B.1.351 challenge in rhesus macaques. Our findings have important implications for vaccine control of SARS-CoV-2 variants of concern. The emergence of SARS-CoV-2 variants that partially evade neutralizing antibodies poses a threat to the efficacy of current COVID-19 vaccines 1,2 . The Ad26.COV2.S vaccine expresses a stabilized spike protein from the WA1/2020 strain of SARS-CoV-2, and has recently demonstrated protective efficacy against symptomatic COVID-19 in humans in several geographical regions—including in South Africa, where 95% of sequenced viruses in cases of COVID-19 were the B.1.351 variant 3 . Here we show that Ad26.COV2.S elicits humoral and cellular immune responses that cross-react with the B.1.351 variant and protects against B.1.351 challenge in rhesus macaques. Ad26.COV2.S induced lower binding and neutralizing antibodies against B.1.351 as compared to WA1/2020, but elicited comparable CD8 and CD4 T cell responses against the WA1/2020, B.1.351, B.1.1.7, P.1 and CAL.20C variants. B.1.351 infection of control rhesus macaques resulted in higher levels of virus replication in bronchoalveolar lavage and nasal swabs than did WA1/2020 infection. Ad26.COV2.S provided robust protection against both WA1/2020 and B.1.351, although we observed higher levels of virus in vaccinated macaques after B.1.351 challenge. These data demonstrate that Ad26.COV2.S provided robust protection against B.1.351 challenge in rhesus macaques. Our findings have important implications for vaccine control of SARS-CoV-2 variants of concern. |
| Audience | Academic |
| Author | Atyeo, Caroline Chandrashekar, Abishek Flinchbaugh, Zack Brown, Renita Liu, Jinyan Mercado, Noe B. Hope, David L. Valentin, Daniel Schuitemaker, Hanneke Jacob-Dolan, Catherine Pessaint, Laurent Chang, Aiquan Alter, Galit Zahn, Roland Teow, Elyse Nampanya, Felix Bauer, Katherine Yu, Jingyou Martinot, Amanda J. Sanborn, Owen Bueno-Wilkerson, Deandre Barouch, Dan H. Bondzie, Esther A. Giffin, Victoria M. Martinez, David R. Cook, Anthony Andersen, Hanne Lewis, Mark G. Gardner, Sarah Patel, Shivani Wan, Huahua Wegmann, Frank Baric, Ralph S. Anioke, Tochi Nkolola, Joseph Hayes, Tammy McMahan, Katherine Tostanoski, Lisa H. Sellers, Daniel |
| Author_xml | – sequence: 1 givenname: Jingyou surname: Yu fullname: Yu, Jingyou organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 2 givenname: Lisa H. orcidid: 0000-0001-9255-5684 surname: Tostanoski fullname: Tostanoski, Lisa H. organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 3 givenname: Noe B. orcidid: 0000-0001-7769-7326 surname: Mercado fullname: Mercado, Noe B. organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 4 givenname: Katherine surname: McMahan fullname: McMahan, Katherine organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 5 givenname: Jinyan surname: Liu fullname: Liu, Jinyan organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 6 givenname: Catherine orcidid: 0000-0001-6641-0342 surname: Jacob-Dolan fullname: Jacob-Dolan, Catherine organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School, Harvard Medical School – sequence: 7 givenname: Abishek orcidid: 0000-0001-7821-5552 surname: Chandrashekar fullname: Chandrashekar, Abishek organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 8 givenname: Caroline surname: Atyeo fullname: Atyeo, Caroline organization: Harvard Medical School, Ragon Institute of MGH, MIT and Harvard – sequence: 9 givenname: David R. surname: Martinez fullname: Martinez, David R. organization: University of North Carolina at Chapel Hill – sequence: 10 givenname: Tochi surname: Anioke fullname: Anioke, Tochi organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 11 givenname: Esther A. surname: Bondzie fullname: Bondzie, Esther A. organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 12 givenname: Aiquan surname: Chang fullname: Chang, Aiquan organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School, Harvard Medical School – sequence: 13 givenname: Sarah surname: Gardner fullname: Gardner, Sarah organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 14 givenname: Victoria M. orcidid: 0000-0002-9783-302X surname: Giffin fullname: Giffin, Victoria M. organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 15 givenname: David L. orcidid: 0000-0001-5654-1744 surname: Hope fullname: Hope, David L. organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 16 givenname: Felix surname: Nampanya fullname: Nampanya, Felix organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 17 givenname: Joseph surname: Nkolola fullname: Nkolola, Joseph organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 18 givenname: Shivani orcidid: 0000-0003-3475-1016 surname: Patel fullname: Patel, Shivani organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 19 givenname: Owen surname: Sanborn fullname: Sanborn, Owen organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 20 givenname: Daniel surname: Sellers fullname: Sellers, Daniel organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 21 givenname: Huahua orcidid: 0000-0001-6958-9464 surname: Wan fullname: Wan, Huahua organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School – sequence: 22 givenname: Tammy orcidid: 0000-0002-8397-696X surname: Hayes fullname: Hayes, Tammy organization: Tufts University Cummings School of Veterinary Medicine – sequence: 23 givenname: Katherine surname: Bauer fullname: Bauer, Katherine organization: Tufts University Cummings School of Veterinary Medicine – sequence: 24 givenname: Laurent surname: Pessaint fullname: Pessaint, Laurent organization: Bioqual – sequence: 25 givenname: Daniel surname: Valentin fullname: Valentin, Daniel organization: Bioqual – sequence: 26 givenname: Zack surname: Flinchbaugh fullname: Flinchbaugh, Zack organization: Bioqual – sequence: 27 givenname: Renita surname: Brown fullname: Brown, Renita organization: Bioqual – sequence: 28 givenname: Anthony surname: Cook fullname: Cook, Anthony organization: Bioqual – sequence: 29 givenname: Deandre surname: Bueno-Wilkerson fullname: Bueno-Wilkerson, Deandre organization: Bioqual – sequence: 30 givenname: Elyse surname: Teow fullname: Teow, Elyse organization: Bioqual – sequence: 31 givenname: Hanne orcidid: 0000-0003-1103-9608 surname: Andersen fullname: Andersen, Hanne organization: Bioqual – sequence: 32 givenname: Mark G. orcidid: 0000-0001-7852-0135 surname: Lewis fullname: Lewis, Mark G. organization: Bioqual – sequence: 33 givenname: Amanda J. orcidid: 0000-0001-6237-6191 surname: Martinot fullname: Martinot, Amanda J. organization: Tufts University Cummings School of Veterinary Medicine – sequence: 34 givenname: Ralph S. orcidid: 0000-0001-6827-8701 surname: Baric fullname: Baric, Ralph S. organization: University of North Carolina at Chapel Hill – sequence: 35 givenname: Galit orcidid: 0000-0002-7680-9215 surname: Alter fullname: Alter, Galit organization: Ragon Institute of MGH, MIT and Harvard – sequence: 36 givenname: Frank orcidid: 0000-0002-9821-1492 surname: Wegmann fullname: Wegmann, Frank organization: Janssen Vaccines & Prevention – sequence: 37 givenname: Roland orcidid: 0000-0003-2822-6231 surname: Zahn fullname: Zahn, Roland organization: Janssen Vaccines & Prevention – sequence: 38 givenname: Hanneke orcidid: 0000-0001-8563-2266 surname: Schuitemaker fullname: Schuitemaker, Hanneke organization: Janssen Vaccines & Prevention – sequence: 39 givenname: Dan H. orcidid: 0000-0001-5127-4659 surname: Barouch fullname: Barouch, Dan H. email: dbarouch@bidmc.harvard.edu organization: Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School, Harvard Medical School, Ragon Institute of MGH, MIT and Harvard |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/34161961$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | The Author(s) 2021 2021. The Author(s). COPYRIGHT 2021 Nature Publishing Group Copyright Nature Publishing Group Aug 19, 2021 |
| Copyright_xml | – notice: The Author(s) 2021 – notice: 2021. The Author(s). – notice: COPYRIGHT 2021 Nature Publishing Group – notice: Copyright Nature Publishing Group Aug 19, 2021 |
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| DOI | 10.1038/s41586-021-03732-8 |
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| Title | Protective efficacy of Ad26.COV2.S against SARS-CoV-2 B.1.351 in macaques |
| URI | https://link.springer.com/article/10.1038/s41586-021-03732-8 https://www.ncbi.nlm.nih.gov/pubmed/34161961 https://www.proquest.com/docview/2563500581 https://www.proquest.com/docview/2544878457 https://pubmed.ncbi.nlm.nih.gov/PMC8373608 |
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