Human serum from SARS-CoV-2-vaccinated and COVID-19 patients shows reduced binding to the RBD of SARS-CoV-2 Omicron variant.
Human serum from SARS-CoV-2-vaccinated and COVID-19 patients shows reduced binding to the RBD of SARS-CoV-2 Omicron variant.
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DOI：
10.1186/s12916-022-02312-5
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发表时间：
2022-03-03
期刊：
影响因子：
9.3
通讯作者：
Hust M
中科院分区：
文献类型：
--
作者：
Schubert M;Bertoglio F;Steinke S;Heine PA;Ynga-Durand MA;Maass H;Sammartino JC;Cassaniti I;Zuo F;Du L;Korn J;Milošević M;Wenzel EV;Krstanović F;Polten S;Pribanić-Matešić M;Brizić I;Baldanti F;Hammarström L;Dübel S;Šustić A;Marcotte H;Strengert M;Protić A;Piralla A;Pan-Hammarström Q;Čičin-Šain L;Hust M
COVID-19大流行是由β冠状病毒SARS-CoV-2引起的。2021年11月，Omicron变体被发现并立即被归类为关注变体（VOC），因为它在刺突蛋白中显示出比以往任何变体都多的突变，特别是在受体结合结构域（RBD）中。我们分析了Omicron RBD与人血管紧张素转换酶-2受体（ACE 2）的结合，以及与武汉、β或δ RBD变体相比，COVID-19患者或疫苗接种者的人血清的能力。所有RBD均在昆虫细胞中产生。通过ELISA和微量热泳（MST）分析RBD与ACE 2的结合。同样，通过ELISA滴定来自27名COVID-19患者、81名接种疫苗的个体和34名加强接种者的血清，测定来自原始武汉毒株、Beta、Delta和Omicron VOC的RBD。此外，分析了来自2×或3× BNT 162 b2疫苗接种者的血清对真实SARS-CoV-2野生型（D 614 G）、Delta和Omicron的中和效力。令人惊讶的是，Omicron RBD与β和δ相比，与ACE 2的结合稍弱，这表明改善的ACE 2结合不太可能是Omicron进化的驱动因素。与原始武汉毒株相比，抗Omicron RBD的血清抗体滴度显著较低。在2× BNT 162 b2接种者的血清中观察到Omicron RBD结合率降低2.6倍。在我们的设置中，Omicron SARS-CoV-2的中和作用完全减弱。这些结果表明，免疫逃逸集中在中和抗体。然而，加强疫苗接种增加了抗Omicron的抗RBD抗体水平，并且真实Omicron SARS-CoV-2的中和至少部分恢复。这项研究增加了证据，表明目前的疫苗接种方案可能对Omicron变体的效率较低。在线版本包含补充材料，可通过10.1186/s12916-022-02312-5获得。
The COVID-19 pandemic is caused by the betacoronavirus SARS-CoV-2. In November 2021, the Omicron variant was discovered and immediately classified as a variant of concern (VOC), since it shows substantially more mutations in the spike protein than any previous variant, especially in the receptor-binding domain (RBD). We analyzed the binding of the Omicron RBD to the human angiotensin-converting enzyme-2 receptor (ACE2) and the ability of human sera from COVID-19 patients or vaccinees in comparison to Wuhan, Beta, or Delta RBD variants. All RBDs were produced in insect cells. RBD binding to ACE2 was analyzed by ELISA and microscale thermophoresis (MST). Similarly, sera from 27 COVID-19 patients, 81 vaccinated individuals, and 34 booster recipients were titrated by ELISA on RBDs from the original Wuhan strain, Beta, Delta, and Omicron VOCs. In addition, the neutralization efficacy of authentic SARS-CoV-2 wild type (D614G), Delta, and Omicron by sera from 2× or 3× BNT162b2-vaccinated persons was analyzed. Surprisingly, the Omicron RBD showed a somewhat weaker binding to ACE2 compared to Beta and Delta, arguing that improved ACE2 binding is not a likely driver of Omicron evolution. Serum antibody titers were significantly lower against Omicron RBD compared to the original Wuhan strain. A 2.6× reduction in Omicron RBD binding was observed for serum of 2× BNT162b2-vaccinated persons. Neutralization of Omicron SARS-CoV-2 was completely diminished in our setup. These results indicate an immune escape focused on neutralizing antibodies. Nevertheless, a boost vaccination increased the level of anti-RBD antibodies against Omicron, and neutralization of authentic Omicron SARS-CoV-2 was at least partially restored. This study adds evidence that current vaccination protocols may be less efficient against the Omicron variant. The online version contains supplementary material available at 10.1186/s12916-022-02312-5.
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影响因子：
5.8
作者：
Marcotte H;Piralla A;Zuo F;Du L;Cassaniti I;Wan H;Kumagai-Braesh M;Andréll J;Percivalle E;Sammartino JC;Wang Y;Vlachiotis S;Attevall J;Bergami F;Ferrari A;Colaneri M;Vecchia M;Sambo M;Zuccaro V;Asperges E;Bruno R;Oggionni T;Meloni F;Abolhassani H;Bertoglio F;Schubert M;Calzolai L;Varani L;Hust M;Xue Y;Hammarström L;Baldanti F;Pan-Hammarström Q
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Pan-Hammarström Q
影响因子：
7.8
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Ng KW;Faulkner N;Wrobel AG;Gamblin SJ;Kassiotis G
通讯作者：
Kassiotis G
影响因子：
64.5
作者：
Hoffmann M;Krüger N;Schulz S;Cossmann A;Rocha C;Kempf A;Nehlmeier I;Graichen L;Moldenhauer AS;Winkler MS;Lier M;Dopfer-Jablonka A;Jäck HM;Behrens GMN;Pöhlmann S
通讯作者：
Pöhlmann S
影响因子：
5.4
作者：
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通讯作者：
Hahn AS
影响因子：
39
作者：
Butt, Adeel A.;Dargham, Soha R.;Abu-Raddad, Laith J.
通讯作者：
Abu-Raddad, Laith J.