Evidence map›Paper›PMID 42824800›Full record

ArticleAntibody therapeutics2026

An IgG-like fusion protein comprising an anti-spike S2 antibody and ACE2 exhibits potent and broad neutralization against SARS-CoV-2 and variants of concern.

Zhizhong Wei, Ximing Liu, Kailun Wang, Lan Chen, Xia Xiao, Yinyan Sun, Wei Wang, Yizhe Chen, Linqiang Fang, Yonghe Qi and 8 more

Abstract read
In one paragraph

Article in Antibody therapeutics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

18 authors.

Zhizhong WeiPeking University-Tsinghua University-National Institute of Biological Sciences Joint Graduate Program, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Ximing LiuNational Institute of Biological Sciences, Beijing 102206, China.
Kailun WangNational Institute of Biological Sciences, Beijing 102206, China.
Lan ChenNHC Key Laboratory of System Biology of Pathogens, Christophe Mérieux Laboratory National Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 102629, China.
Xia XiaoNHC Key Laboratory of System Biology of Pathogens, Christophe Mérieux Laboratory National Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 102629, China.
Yinyan SunNational Institute of Biological Sciences, Beijing 102206, China.
Wei WangNational Institute of Biological Sciences, Beijing 102206, China.
Yizhe ChenNational Institute of Biological Sciences, Beijing 102206, China.
Linqiang FangNational Institute of Biological Sciences, Beijing 102206, China.
Yonghe QiNational Institute of Biological Sciences, Beijing 102206, China.
Fang YangNational Institute of Biological Sciences, Beijing 102206, China.
Xinyan HaoNational Institute of Biological Sciences, Beijing 102206, China.
Ruihua FanNational Institute of Biological Sciences, Beijing 102206, China.
Sanduo ZhengNational Institute of Biological Sciences, Beijing 102206, China.
Lili RenNHC Key Laboratory of System Biology of Pathogens, Christophe Mérieux Laboratory National Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 102629, China.
Wenhui LiNational Institute of Biological Sciences, Beijing 102206, China.
Xinxin TianNational Institute of Biological Sciences, Beijing 102206, China.ORCID https://orcid.org/0000-0001-9118-7154
Jianhua SuiNational Institute of Biological Sciences, Beijing 102206, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: The continuous evolution of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) highlights the value of broad-spectrum antiviral strategies. Antibody-engineering approaches targeting conserved regions of the Spike protein may enhance neutralizing potency and breadth. Methods: A human antibody (P23) against the Spike protein of SARS-CoV-2 was identified using a human antibody phage display library panning and screening for binding affinity and breadth against multiple coronavirus Spike proteins using surface plasmon resonance (SPR). The epitope of P23 was characterized using the S1 and S2 subunits of SARS-CoV-2 Spike protein and hydrogen-deuterium exchange mass spectrometry (HDX-MS). An IgG-like bispecific fusion protein (Bs-ACE2-P23) was engineered by fusing the extracellular domain (ECD) of human angiotensin-converting enzyme 2 (ACE2) to the N-terminus of the P23 heavy chain (HC). Neutralizing activity was evaluated against both pseudotyped and authentic SARS-CoV-2 variants. Results: P23 cross-bound Spike proteins from SARS-CoV-2 wild type (WT), D614G and JN.1 variants, Pangolin-CoV, Bat coronavirus RaTG13, and SARS-CoV-1, recognizing an epitope on the S2 subunit adjacent to the fusion peptide (FP). While P23 was ineffective against D614G-containing SARS-CoV-2 variants, Bs-ACE2-P23 exhibited markedly enhanced neutralization potency. This bispecific architecture also improved the neutralizing activity of another FP-targeting antibody. Conclusion: We developed a bispecific fusion protein with potent broad-spectrum neutralizing activity against SARS-CoV-2 variants. This architecture provides a promising strategy for next-generation coronavirus biologics.

Indexed as

ACE2broad neutralization antibodyIgG-like bispecific fusion proteinSARS-CoV-2spike protein

Identifiers

PMID42824800
PMCPMC13628130

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