Gen Li, Zhongcheng Zhou, Peng Du, Meixing Yu, Ning Li, Xinxin Xiong, Hong Huang, Zhihai Liu, Qinjin Dai, Jie Zhu, Chengbin Guo, Shanyun Wu, Daniel T Baptista-Hon, Man Miao, Lam Wai Ming, Yong Wu, Fanxin Zeng, Charlotte L Zhang, Edward D Zhang, Haifeng Song, Jianghai Liu, Johnson Yiu-Nam Lau, Andy P Xiang, Kang Zhang
{"title":"印度 B.1.617 株中的 SARS-CoV-2 穗状 L452R-E484Q 变体显示免疫血清的中和活性显著降低。","authors":"Gen Li, Zhongcheng Zhou, Peng Du, Meixing Yu, Ning Li, Xinxin Xiong, Hong Huang, Zhihai Liu, Qinjin Dai, Jie Zhu, Chengbin Guo, Shanyun Wu, Daniel T Baptista-Hon, Man Miao, Lam Wai Ming, Yong Wu, Fanxin Zeng, Charlotte L Zhang, Edward D Zhang, Haifeng Song, Jianghai Liu, Johnson Yiu-Nam Lau, Andy P Xiang, Kang Zhang","doi":"10.1093/pcmedi/pbab016","DOIUrl":null,"url":null,"abstract":"<p><p>To assess the impact of the key non-synonymous amino acid substitutions in the RBD of the spike protein of SARS-CoV-2 variant B.1.617.1 (dominant variant identified in the current India outbreak) on the infectivity and neutralization activities of the immune sera, L452R and E484Q (L452R-E484Q variant), pseudotyped virus was constructed (with the D614G background). The impact on binding with the neutralizing antibodies was also assessed with an ELISA assay. Pseudotyped virus carrying a L452R-E484Q variant showed a comparable infectivity compared with D614G. However, there was a significant reduction in the neutralization activity of the immune sera from non-human primates vaccinated with a recombinant receptor binding domain (RBD) protein, convalescent patients, and healthy vaccinees vaccinated with an mRNA vaccine. In addition, there was a reduction in binding of L452R-E484Q-D614G protein to the antibodies of the immune sera from vaccinated non-human primates. These results highlight the interplay between infectivity and other biologic factors involved in the natural evolution of SARS-CoV-2. Reduced neutralization activities against the L452R-E484Q variant will have an impact on health authority planning and implications for the vaccination strategy/new vaccine development.</p>","PeriodicalId":33608,"journal":{"name":"Precision Clinical Medicine","volume":null,"pages":null},"PeriodicalIF":5.1000,"publicationDate":"2021-07-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8385834/pdf/","citationCount":"0","resultStr":"{\"title\":\"The SARS-CoV-2 spike L452R-E484Q variant in the Indian B.1.617 strain showed significant reduction in the neutralization activity of immune sera.\",\"authors\":\"Gen Li, Zhongcheng Zhou, Peng Du, Meixing Yu, Ning Li, Xinxin Xiong, Hong Huang, Zhihai Liu, Qinjin Dai, Jie Zhu, Chengbin Guo, Shanyun Wu, Daniel T Baptista-Hon, Man Miao, Lam Wai Ming, Yong Wu, Fanxin Zeng, Charlotte L Zhang, Edward D Zhang, Haifeng Song, Jianghai Liu, Johnson Yiu-Nam Lau, Andy P Xiang, Kang Zhang\",\"doi\":\"10.1093/pcmedi/pbab016\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>To assess the impact of the key non-synonymous amino acid substitutions in the RBD of the spike protein of SARS-CoV-2 variant B.1.617.1 (dominant variant identified in the current India outbreak) on the infectivity and neutralization activities of the immune sera, L452R and E484Q (L452R-E484Q variant), pseudotyped virus was constructed (with the D614G background). The impact on binding with the neutralizing antibodies was also assessed with an ELISA assay. Pseudotyped virus carrying a L452R-E484Q variant showed a comparable infectivity compared with D614G. However, there was a significant reduction in the neutralization activity of the immune sera from non-human primates vaccinated with a recombinant receptor binding domain (RBD) protein, convalescent patients, and healthy vaccinees vaccinated with an mRNA vaccine. In addition, there was a reduction in binding of L452R-E484Q-D614G protein to the antibodies of the immune sera from vaccinated non-human primates. These results highlight the interplay between infectivity and other biologic factors involved in the natural evolution of SARS-CoV-2. 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The SARS-CoV-2 spike L452R-E484Q variant in the Indian B.1.617 strain showed significant reduction in the neutralization activity of immune sera.
To assess the impact of the key non-synonymous amino acid substitutions in the RBD of the spike protein of SARS-CoV-2 variant B.1.617.1 (dominant variant identified in the current India outbreak) on the infectivity and neutralization activities of the immune sera, L452R and E484Q (L452R-E484Q variant), pseudotyped virus was constructed (with the D614G background). The impact on binding with the neutralizing antibodies was also assessed with an ELISA assay. Pseudotyped virus carrying a L452R-E484Q variant showed a comparable infectivity compared with D614G. However, there was a significant reduction in the neutralization activity of the immune sera from non-human primates vaccinated with a recombinant receptor binding domain (RBD) protein, convalescent patients, and healthy vaccinees vaccinated with an mRNA vaccine. In addition, there was a reduction in binding of L452R-E484Q-D614G protein to the antibodies of the immune sera from vaccinated non-human primates. These results highlight the interplay between infectivity and other biologic factors involved in the natural evolution of SARS-CoV-2. Reduced neutralization activities against the L452R-E484Q variant will have an impact on health authority planning and implications for the vaccination strategy/new vaccine development.
期刊介绍：
Precision Clinical Medicine (PCM) is an international, peer-reviewed, open access journal that provides timely publication of original research articles, case reports, reviews, editorials, and perspectives across the spectrum of precision medicine. The journal's mission is to deliver new theories, methods, and evidence that enhance disease diagnosis, treatment, prevention, and prognosis, thereby establishing a vital communication platform for clinicians and researchers that has the potential to transform medical practice. PCM encompasses all facets of precision medicine, which involves personalized approaches to diagnosis, treatment, and prevention, tailored to individual patients or patient subgroups based on their unique genetic, phenotypic, or psychosocial profiles. The clinical conditions addressed by the journal include a wide range of areas such as cancer, infectious diseases, inherited diseases, complex diseases, and rare diseases.
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