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TitleA non-ACE2 competing human single-domain antibody confers broad neutralization against SARS-CoV-2 and circulating variants.
Journal, issue, pagesSignal Transduct Target Ther, Vol. 6, Issue 1, Page 378, Year 2021
Publish dateNov 3, 2021
AuthorsZhenlin Yang / Yulu Wang / Yujia Jin / Yuanfei Zhu / Yanling Wu / Cheng Li / Yu Kong / Wenping Song / Xiaolong Tian / Wuqiang Zhan / Ailing Huang / Shanshan Zhou / Shuai Xia / Xiaoxu Tian / Chao Peng / Cuicui Chen / Yibing Shi / Gaowei Hu / Shujuan Du / Yuyan Wang / Youhua Xie / Shibo Jiang / Lu Lu / Lei Sun / Yuanlin Song / Tianlei Ying /
PubMed AbstractThe current COVID-19 pandemic has heavily burdened the global public health system and may keep simmering for years. The frequent emergence of immune escape variants have spurred the search for ...The current COVID-19 pandemic has heavily burdened the global public health system and may keep simmering for years. The frequent emergence of immune escape variants have spurred the search for prophylactic vaccines and therapeutic antibodies that confer broad protection against SARS-CoV-2 variants. Here we show that the bivalency of an affinity maturated fully human single-domain antibody (n3113.1-Fc) exhibits exquisite neutralizing potency against SARS-CoV-2 pseudovirus, and confers effective prophylactic and therapeutic protection against authentic SARS-CoV-2 in the host cell receptor angiotensin-converting enzyme 2 (ACE2) humanized mice. The crystal structure of n3113 in complex with the receptor-binding domain (RBD) of SARS-CoV-2, combined with the cryo-EM structures of n3113 and spike ecto-domain, reveals that n3113 binds to the side surface of up-state RBD with no competition with ACE2. The binding of n3113 to this novel epitope stabilizes spike in up-state conformations but inhibits SARS-CoV-2 S mediated membrane fusion, expanding our recognition of neutralization by antibodies against SARS-CoV-2. Binding assay and pseudovirus neutralization assay show no evasion of recently prevalent SARS-CoV-2 lineages, including Alpha (B.1.1.7), Beta (B.1.351), Gamma (P.1), and Delta (B.1.617.2) for n3113.1-Fc with Y58L mutation, demonstrating the potential of n3113.1-Fc (Y58L) as a promising candidate for clinical development to treat COVID-19.
External linksSignal Transduct Target Ther / PubMed:34732694 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.27 - 3.7 Å
Structure data

32038

7vnc

EMDB-32038, PDB-7vnc:
Structure of the SARS-CoV-2 spike glycoprotein in complex with a human single domain antibody n3113 (UDD-state, state 1)
Method: EM (single particle) / Resolution: 3.7 Å

32039

7vnd

EMDB-32039, PDB-7vnd:
Structure of the SARS-CoV-2 spike glycoprotein in complex with a human single domain antibody n3113 (UUD-state, state 2)
Method: EM (single particle) / Resolution: 3.6 Å

32040

7vne

EMDB-32040, PDB-7vne:
Structure of the SARS-CoV-2 spike glycoprotein in complex with a human single domain antibody n3113.1 (UUU-state)
Method: EM (single particle) / Resolution: 3.5 Å

PDB-7vnb:
Crystal structure of the SARS-CoV-2 RBD in complex with a human single domain antibody n3113
Method: X-RAY DIFFRACTION / Resolution: 2.27 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / SARS-CoV-2 / nanobody / ANTIVIRAL PROTEIN

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