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TitleRational identification of potent and broad sarbecovirus-neutralizing antibody cocktails from SARS convalescents.
Journal, issue, pagesCell Rep, Vol. 41, Issue 12, Page 111845, Year 2022
Publish dateDec 20, 2022
AuthorsYunlong Cao / Fanchong Jian / Zhiying Zhang / Ayijiang Yisimayi / Xiaohua Hao / Linlin Bao / Fei Yuan / Yuanling Yu / Shuo Du / Jing Wang / Tianhe Xiao / Weiliang Song / Ying Zhang / Pulan Liu / Ran An / Peng Wang / Yao Wang / Sijie Yang / Xiao Niu / Yuhang Zhang / Qingqing Gu / Fei Shao / Yaling Hu / Weidong Yin / Aihua Zheng / Youchun Wang / Chuan Qin / Ronghua Jin / Junyu Xiao / Xiaoliang Sunney Xie /
PubMed AbstractSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron sublineages have escaped most receptor-binding domain (RBD)-targeting therapeutic neutralizing antibodies (NAbs), which proves ...Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron sublineages have escaped most receptor-binding domain (RBD)-targeting therapeutic neutralizing antibodies (NAbs), which proves that previous NAb drug screening strategies are deficient against the fast-evolving SARS-CoV-2. Better broad NAb drug candidate selection methods are needed. Here, we describe a rational approach for identifying RBD-targeting broad SARS-CoV-2 NAb cocktails. Based on high-throughput epitope determination, we propose that broad NAb drugs should target non-immunodominant RBD epitopes to avoid herd-immunity-directed escape mutations. Also, their interacting antigen residues should focus on sarbecovirus conserved sites and associate with critical viral functions, making the antibody-escaping mutations less likely to appear. Following these criteria, a featured non-competing antibody cocktail, SA55+SA58, is identified from a large collection of broad sarbecovirus NAbs isolated from SARS-CoV-2-vaccinated SARS convalescents. SA55+SA58 potently neutralizes ACE2-utilizing sarbecoviruses, including circulating Omicron variants, and could serve as broad SARS-CoV-2 prophylactics to offer long-term protection, especially for individuals who are immunocompromised or with high-risk comorbidities.
External linksCell Rep / PubMed:36493787 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.48 - 4.08 Å
Structure data

32728

7wrj

EMDB-32728, PDB-7wrj:
Local CryoEM structure of the SARS-CoV-2 S6P(B.1.1.529) in complex with BD55-4637 Fab
Method: EM (single particle) / Resolution: 4.08 Å

32737

7wry

EMDB-32737, PDB-7wry:
Local structure of BD55-3546 Fab and SARS-COV2 Delta RBD complex
Method: EM (single particle) / Resolution: 3.28 Å

33552

7y0w

EMDB-33552, PDB-7y0w:
Local structure of BD55-5514 and BD55-5840 Fab and Omicron BA.1 RBD complex
Method: EM (single particle) / Resolution: 3.42 Å

PDB-7y0c:
Crystal structure of BD55-1403 and SARS-CoV-2 Omicron RBD
Method: X-RAY DIFFRACTION / Resolution: 2.94 Å

PDB-7y0v:
The co-crystal structure of BA.1-RBD with Fab-5549
Method: X-RAY DIFFRACTION / Resolution: 2.48 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
  • sars coronavirus b012
KeywordsVIRAL PROTEIN / antibody / complex / SARS-COV2 Delta RBD / VIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / Omicron variants / VIRAL PROTEIN-IMMUNE SYSTEM complex / BA.1-RBD

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