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中和抗体对 SARS-CoV-2 受体结合域的识别。

Recognition of the SARS-CoV-2 receptor binding domain by neutralizing antibodies.

机构信息

Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.

Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA; Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA; Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.

出版信息

Biochem Biophys Res Commun. 2021 Jan 29;538:192-203. doi: 10.1016/j.bbrc.2020.10.012. Epub 2020 Oct 10.

DOI:10.1016/j.bbrc.2020.10.012
PMID:33069360
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7547570/
Abstract

Immediately from the outset of the COVID-19 pandemic, researchers from diverse biomedical and biological disciplines have united to study the novel pandemic virus, SARS-CoV-2. The antibody response to SARS-CoV-2 has been a major focus of COVID-19 research due to its clinical relevance and importance in vaccine and therapeutic development. Isolation and characterization of antibodies to SARS-CoV-2 have been accumulating at an unprecedented pace. Most of the SARS-CoV-2 neutralizing antibodies to date target the spike (S) protein receptor binding domain (RBD), which engages the host receptor ACE2 for viral entry. Here we review the binding sites and molecular features of monoclonal antibodies that target the SARS-CoV-2 RBD, including a few that also cross-neutralize SARS-CoV.

摘要

从 COVID-19 大流行一开始,来自不同生物医学和生物学领域的研究人员就联合起来研究这种新型的大流行病毒 SARS-CoV-2。由于 SARS-CoV-2 抗体在疫苗和治疗开发中的临床相关性和重要性,针对 SARS-CoV-2 的抗体反应一直是 COVID-19 研究的重点。针对 SARS-CoV-2 的抗体的分离和鉴定正在以前所未有的速度积累。迄今为止,大多数 SARS-CoV-2 中和抗体都针对刺突(S)蛋白受体结合域(RBD),该域与宿主受体 ACE2 结合以实现病毒进入。在这里,我们回顾了针对 SARS-CoV-2 RBD 的单克隆抗体的结合位点和分子特征,包括一些也能中和 SARS-CoV 的抗体。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/9c750eeed6f8/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/7d4ea894a9c2/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/4c37fce43611/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/94846fb4b225/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/7edebdeebc97/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/fc59b6519655/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/24dd2d1bc5e2/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/9c750eeed6f8/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/7d4ea894a9c2/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/4c37fce43611/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/94846fb4b225/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/7edebdeebc97/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/fc59b6519655/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/24dd2d1bc5e2/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/29e8/7908065/9c750eeed6f8/gr7.jpg

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