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针对 SARS-CoV-2 受体结合域的隐匿性位点特异性抗体可以保留对刺突变异体的功能性结合亲和力。

Cryptic-site-specific antibodies to the SARS-CoV-2 receptor binding domain can retain functional binding affinity to spike variants.

机构信息

Center for Human Systems Immunology, Duke University, Durham, North Carolina, USA.

Department of Surgery, Duke University, Durham, North Carolina, USA.

出版信息

J Virol. 2023 Dec 21;97(12):e0107023. doi: 10.1128/jvi.01070-23. Epub 2023 Nov 29.

DOI:10.1128/jvi.01070-23
PMID:38019013
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10746274/
Abstract

Multiple SARS-CoV-2 variants of concern have emerged and caused a significant number of infections and deaths worldwide. These variants of concern contain mutations that might significantly affect antigen-targeting by antibodies. It is therefore important to further understand how antibody binding and neutralization are affected by the mutations in SARS-CoV-2 variants. We highlighted how antibody epitope specificity can influence antibody binding to SARS-CoV-2 spike protein variants and neutralization of SARS-CoV-2 variants. We showed that weakened spike binding and neutralization of Beta (B.1.351) and Omicron (BA.1) variants compared to wildtype are not universal among the panel of antibodies and identified antibodies of a specific binding footprint exhibiting consistent enhancement of spike binding and retained neutralization to Beta variant. These data and analysis can inform how antigen-targeting by antibodies might evolve during a pandemic and prepare for potential future sarbecovirus outbreaks.

摘要

多种关注的 SARS-CoV-2 变体已经出现,并在全球范围内导致了大量感染和死亡。这些关注的变体包含可能显著影响抗体靶向抗原的突变。因此,进一步了解抗体结合和中和如何受到 SARS-CoV-2 变体突变的影响非常重要。我们强调了抗体表位特异性如何影响抗体与 SARS-CoV-2 刺突蛋白变体的结合和对 SARS-CoV-2 变体的中和。我们表明,与野生型相比,Beta(B.1.351)和奥密克戎(BA.1)变体的刺突结合减弱和中和作用并非所有抗体都普遍存在,并确定了具有特定结合特征的抗体,其刺突结合得到一致增强,对 Beta 变体的中和作用保持不变。这些数据和分析可以告知在大流行期间抗体对抗原的靶向作用如何演变,并为潜在的未来沙贝科病毒爆发做好准备。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/0ce024ac82dc/jvi.01070-23.f006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/e211e1880fa9/jvi.01070-23.f001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/4c219e4eb978/jvi.01070-23.f002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/ffad7c0cd9fc/jvi.01070-23.f003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/e12cb4a3bc51/jvi.01070-23.f004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/e84f5525968d/jvi.01070-23.f005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/0ce024ac82dc/jvi.01070-23.f006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/e211e1880fa9/jvi.01070-23.f001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/4c219e4eb978/jvi.01070-23.f002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/ffad7c0cd9fc/jvi.01070-23.f003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/e12cb4a3bc51/jvi.01070-23.f004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/e84f5525968d/jvi.01070-23.f005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9e71/10746274/0ce024ac82dc/jvi.01070-23.f006.jpg

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