Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variants

Autor: Quan Yuan, Yali Zhang, Shaojuan Wang, Lizhi Zhou, Xin Chi, Qingbing Zheng, Jason S. McLellan, Ying Gu, Tong Cheng, Sibo Zhang, Shaowei Li, Chuanlai Yang, Tianying Zhang, Yingbin Wang, Jinjin Li, Yuyun Zhang, Hui Sun, Qinjian Zhao, Zheng Zhang, Z. Hong Zhou, Jun Zhang, Minqing Hong, Tingting Deng, Wenhui Xue, Hualong Xiong, Shuo Song, Hai Yu, Tingting Li, Ningshao Xia, Yang Huang, Tingting Chen
Jazyk: angličtina
Rok vydání: 2021
Předmět:
General Physics and Astronomy
Passive
medicine.disease_cause
Antibodies
Viral
Epitope
Mice
Epitopes
Receptors
Monoclonal
Chlorocebus aethiops
Sf9 Cells
Viral
Lung
Multidisciplinary
Chinese hamster ovary cell
Antibodies
Monoclonal
Spike Glycoprotein
Virus
Infectious Diseases
Spike Glycoprotein
Coronavirus
Middle East Respiratory Syndrome Coronavirus
Pneumonia & Influenza
Receptors
Virus
Antibody
Infection
Biotechnology
Middle East respiratory syndrome coronavirus
Science
CHO Cells
Biology
General Biochemistry
Genetics and Molecular Biology
Article
Antibodies
Vaccine Related
Cricetulus
Neutralization Tests
Biodefense
medicine
Animals
Humans
Binding site
Vero Cells
Pandemics
X-ray crystallography
Binding Sites
SARS-CoV-2
Prevention
HEK 293 cells
fungi
Immunization
Passive
COVID-19
General Chemistry
Pneumonia
Virology
Coronavirus
HEK293 Cells
Emerging Infectious Diseases
Good Health and Well Being
Immunization
Viral infection
biology.protein
Vero cell
Protein Multimerization
Broadly Neutralizing Antibodies
Zdroj: Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature communications, vol 12, iss 1
Nature Communications
ISSN: 2041-1723
Popis: The emergence of numerous variants of SARS-CoV-2, the causative agent of COVID-19, has presented new challenges to the global efforts to control the COVID-19 pandemic. Here, we obtain two cross-neutralizing antibodies (7D6 and 6D6) that target Sarbecoviruses’ receptor-binding domain (RBD) with sub-picomolar affinities and potently neutralize authentic SARS-CoV-2. Crystal structures show that both antibodies bind a cryptic site different from that recognized by existing antibodies and highly conserved across Sarbecovirus isolates. Binding of these two antibodies to the RBD clashes with the adjacent N-terminal domain and disrupts the viral spike. Both antibodies confer good resistance to mutations in the currently circulating SARS-CoV-2 variants. Thus, our results have direct relevance to public health as options for passive antibody therapeutics and even active prophylactics. They can also inform the design of pan-sarbecovirus vaccines.
Antibodies (Abs) targeting highly conserved epitopes are important tools against emerging virus variants. Here, the authors characterize Abs that recognize a cryptic epitope in the receptor-binding domain of SARS-CoV-2 spike that is well conserved and show that these Abs can neutralize several variants of concerns.
Databáze: OpenAIRE
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