Evidence map›Paper›PMID 42530330›Full record

ArticleJournal of virology2026

ACE2-fused nanobody targeting a cryptic RBD epitope broadly neutralizes SARS-like viruses.

Weihong Zeng, Guanying Zhang, Huan Ma, Lijun Xiong, Mingshi Xu, Shanshan Wang, Xiaoxue Huang, Shi Chen, Xiangyang Chi, Sandra Chiu and 1 more

Abstract read
In one paragraph

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

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Weihong Zeng *School of Biomedical and Environmental Engineering, Hefei Institute of Technology, Hefei, Anhui, China.ORCID 0000-0003-3853-3630
Guanying Zhang *National Key Laboratory of Advanced Biotechnology, Academy of Military Medical Sciences, Beijing, China.
Huan Ma *Laboratory of Structural Immunology, State Key Laboratory of Immune Response and Immunotherapy, Institute of Advanced Technology, University of Science and Technology of China, Hefei, Anhui, China.ORCID 0000-0002-4668-0107
Lijun XiongSchool of Biomedical and Environmental Engineering, Hefei Institute of Technology, Hefei, Anhui, China.
Mingshi XuSchool of Biomedical and Environmental Engineering, Hefei Institute of Technology, Hefei, Anhui, China.
Shanshan WangSchool of Biomedical and Environmental Engineering, Hefei Institute of Technology, Hefei, Anhui, China.
Xiaoxue HuangLaboratory of Structural Immunology, State Key Laboratory of Immune Response and Immunotherapy, Institute of Advanced Technology, University of Science and Technology of China, Hefei, Anhui, China.
Shi ChenLaboratory of Structural Immunology, State Key Laboratory of Immune Response and Immunotherapy, Institute of Advanced Technology, University of Science and Technology of China, Hefei, Anhui, China.
Xiangyang ChiNational Key Laboratory of Advanced Biotechnology, Academy of Military Medical Sciences, Beijing, China.ORCID 0000-0002-0580-5997
Sandra ChiuDivision of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, China.ORCID 0000-0001-9034-5755
Tengchuan JinLaboratory of Structural Immunology, State Key Laboratory of Immune Response and Immunotherapy, Institute of Advanced Technology, University of Science and Technology of China, Hefei, Anhui, China.ORCID 0000-0002-1395-188X

Funding

Anhui Provincial Higher Education Quality Engineering Project 2024aijy571Hefei Institute of Technology Talent Scientific Research Fund Project 2025KY24Hefei Municipal Key Technology Research and Development Program 2025SKJGGHLG010National Natural Science Foundation of China 32100745, 82272301Strategic Priority Research Program of the Chinese Academy of Sciences XDB0490000, XDB0940301USTC Research Funds of the Double First-Class Initiative YD9100002056
6 · The paper itself

Abstract

The SARS-CoV-2 (SARS2) and SARS-CoV (SARS1) viruses pose significant threats due to their high mutation rates and potential for cross-species transmission, which has rendered many antibodies ineffective. To counter potential future emergences of novel SARS-like viruses, it is imperative to develop nanobodies with broad-spectrum neutralizing capacity. Here, we employed an alternating immunization strategy in alpacas using SARS1 and SARS2 RBDs to generate cross-reactive nanobodies. Four crossing-binding nanobodies (aSR29, aSR196, aSR347, and aSR348) were identified, exhibiting high affinities for SARS1/SARS2 RBDs and Omicron subvariants. Structural analysis revealed that aSR29 targets a cryptic, highly conserved epitope at the inner base of the RBD, a region shielded from conventional antibodies by steric hindrance, efficiently neutralizing SARS1, SARS2, and multiple Variants of Concern (VOCs), including XBB.1.5 and BQ.1.1. Building on this unique binding mode, we engineered a bispecific fusion protein, aSR29-ACE2-Fc. This construct synergistically combines high-affinity RBD binding with the steric blockade of viral attachment, resulting in a 33-fold increase in neutralization potency against SARS2 and enhanced resilience against immune escape. Our findings validate an efficient strategy for eliciting broad-spectrum nanobodies and demonstrate the therapeutic potential of VHH-ACE2 fusion proteins against current and future SARS-like viruses.IMPORTANCEThe continued evolution of SARS-CoV-2 has rendered most existing antibodies ineffective, highlighting the urgent need for broad-spectrum countermeasures against current and future SARS-like viruses. Here, we developed an alternating immunization strategy to generate nanobodies that target a hidden, highly conserved region on the viral spike protein. One such nanobody, aSR29, potently neutralizes diverse variants, including XBB.1.5 and BQ.1.1. By fusing aSR29 with the viral receptor ACE2, we created a bispecific molecule that blocks viral entry through two independent mechanisms, achieving a 33-fold increase in neutralization potency. This work provides a practical and scalable strategy for pandemic preparedness, demonstrating that engineered nanobody-ACE2 fusions can serve as effective broad-spectrum therapeutics against emerging SARS-like viruses.

Indexed as

Angiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralEpitopesSARS-CoV-2Severe acute respiratory syndrome-related coronavirusSingle-Domain AntibodiesSpike Glycoprotein, CoronavirusAnimalsCamelids, New WorldCross ReactionsHumansNeutralization TestsAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralEpitopesSingle-Domain AntibodiesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2 fusion proteinalternating immunizationconserved RBD epitopenanobodiesSARS-like coronaviruses

Identifiers

PMID42530330
PMCPMC13483450

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.