Antibody evasion by the P.1 strain of SARS-CoV-2.
Antibody evasion by the P.1 strain of SARS-CoV-2.
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DOI：
10.1016/j.cell.2021.03.055
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发表时间：
2021-05-27
期刊：
影响因子：
64.5
通讯作者：
Screaton GR
中科院分区：
文献类型：
--
作者：
Dejnirattisai W;Zhou D;Supasa P;Liu C;Mentzer AJ;Ginn HM;Zhao Y;Duyvesteyn HME;Tuekprakhon A;Nutalai R;Wang B;López-Camacho C;Slon-Campos J;Walter TS;Skelly D;Costa Clemens SA;Naveca FG;Nascimento V;Nascimento F;Fernandes da Costa C;Resende PC;Pauvolid-Correa A;Siqueira MM;Dold C;Levin R;Dong T;Pollard AJ;Knight JC;Crook D;Lambe T;Clutterbuck E;Bibi S;Flaxman A;Bittaye M;Belij-Rammerstorfer S;Gilbert SC;Carroll MW;Klenerman P;Barnes E;Dunachie SJ;Paterson NG;Williams MA;Hall DR;Hulswit RJG;Bowden TA;Fry EE;Mongkolsapaya J;Ren J;Stuart DI;Screaton GR
终止SARS-CoV-2大流行依赖于全球疫苗接种。目前的疫苗引发对来自早期分离株的病毒刺突的中和抗体应答。然而，出现了具有多个突变的新菌株，包括来自巴西的P.1，来自南非的B.1.351和来自英国的B.1.1.7（尖峰分别有12，10和9个变化）。所有突变的ACE 2结合位点，与P.1和B.1.351有一个几乎相同的三联体（E484 K，K417 N/T，和N501 Y），我们显示赋予类似的增加ACE 2的亲和力。我们发现，令人惊讶的是，P.1对自然获得的或疫苗诱导的抗体应答的抗性显著低于B.1.351，这表明受体结合结构域（RBD）以外的变化影响中和。单克隆抗体（mAb）222中和所有三种变体，尽管与两个ACE 2结合位点突变相互作用。我们通过结构分析解释了这一点，并使用222轻链在很大程度上恢复了对主要类别的公共抗体的中和效力。尽管有类似的RBD突变，但P.1比B.1.351 P.1，B.1.351，和B.1.1.7部分或完全逃避大多数VH 3 - 53抗体mAb 222（VH 3 -53）保留对所有三种变体的中和作用。2来自巴西揭示了较低的阻力，自然感染或疫苗接种产生的抗体相比，另一个类似的变种，B.1.351。单克隆抗体mAb 222能够中和所有三种变体（P.1、B.1.351和B.1.1.7），其轻链能够恢复对广泛抗体组的中和效力。
Terminating the SARS-CoV-2 pandemic relies upon pan-global vaccination. Current vaccines elicit neutralizing antibody responses to the virus spike derived from early isolates. However, new strains have emerged with multiple mutations, including P.1 from Brazil, B.1.351 from South Africa, and B.1.1.7 from the UK (12, 10, and 9 changes in the spike, respectively). All have mutations in the ACE2 binding site, with P.1 and B.1.351 having a virtually identical triplet (E484K, K417N/T, and N501Y), which we show confer similar increased affinity for ACE2. We show that, surprisingly, P.1 is significantly less resistant to naturally acquired or vaccine-induced antibody responses than B.1.351, suggesting that changes outside the receptor-binding domain (RBD) impact neutralization. Monoclonal antibody (mAb) 222 neutralizes all three variants despite interacting with two of the ACE2-binding site mutations. We explain this through structural analysis and use the 222 light chain to largely restore neutralization potency to a major class of public antibodies. Despite similar RBD mutations, P.1 is easier to neutralize than B.1.351 P.1, B.1.351, and B.1.1.7 partially or fully escape most VH3-53 antibodies mAb 222 (VH3-53) retains neutralization against all three variants Neutralization is restored in VH3-53 chimeric antibodies with mAb 222 LC Structural and functional analysis of the P.1 variant of SARS-CoV-2 from Brazil reveals less resistance to antibodies generated from natural infection or vaccination compared to another similar variant, B.1.351. A monoclonal antibody, mAb 222, is able to neutralize all three variants (P.1, B.1.351, and B.1.1.7), with its light chain able to restore neutralization potency to a broad group of antibodies.
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DOI：
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发表时间：
2020-12-31
期刊：
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影响因子：
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发表时间：
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影响因子：
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发表时间：
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