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Structural Study of SARS-CoV-2 Antibodies Identifies a Broad-Spectrum Antibody That Neutralizes the Omicron Variant by Disassembling the Spike Trimer

Wuqiang Zhan, Xiaolong Tian, Xiang Zhang, Shenghui Xing, Wenping Song, Qianying Liu, Aihua Hao, Yuxia Hu, Meng Zhang, Tianlei Ying, Zhenguo Chen, Fei Lan, Lei Sun

2022Journal of Virology33 citationsDOIOpen Access PDF

Abstract

The emergence of the Omicron strain of SARS-CoV-2 caused higher immune escape, raising unprecedented concerns about the effectiveness of antibody therapies and vaccines. In this study, we identified a SARS-CoV-2 neutralizing antibody, 553-49, which neutralizes all variants by targeting a completely conserved novel epitope. In addition, we revealed that IgG 553-15 neutralizes SARS-CoV-2 by cross-linking virions and that 553-60 functions by blocking receptor binding. Comparison of different receptor binding domain (RBD) epitopes revealed that the 553-49 epitope is hidden in the S trimer and keeps a high degree of conservation during SARS-CoV-2 evolution, making 553-49 a promising therapeutic reagent against the emerging Omicron and future variants of SARS-CoV-2.

Topics & Concepts

BiologyTrimerAntibodyVirologySpike ProteinSpike (software development)Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Broad spectrumCoronavirus disease 2019 (COVID-19)2019-20 coronavirus outbreakComputational biologyGeneticsPhysicsComputer scienceInfectious disease (medical specialty)DiseaseOutbreakNuclear magnetic resonancePathologyChemistrySoftware engineeringMedicineDimerCombinatorial chemistrySARS-CoV-2 and COVID-19 ResearchBacillus and Francisella bacterial researchViral gastroenteritis research and epidemiology
Structural Study of SARS-CoV-2 Antibodies Identifies a Broad-Spectrum Antibody That Neutralizes the Omicron Variant by Disassembling the Spike Trimer | Litcius