Evidence map›Paper›PMID 42698763›Full record

ArticleBiosafety and health2026

Receptor-mimicking antibodies retain neutralization of recent SARS-CoV-2 variants.

Qi Tang, Liyuan Hu, Minxiang Xie, Ran Zhan, Qiao Wang, Rong Zhang

Abstract read
In one paragraph

Article in Biosafety and health, 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

6 authors.

Qi TangKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Liyuan HuKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Minxiang XieKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Ran ZhanKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Qiao WangKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.
Rong ZhangKey Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ongoing evolution of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has compromised the efficacy of many neutralizing antibodies. Receptor-mimicking antibodies, whose binding modes partially resemble those of angiotensin-converting enzyme 2 (ACE2), are of particular interest as they recognize functionally constrained regions of the receptor-binding domain (RBD). However, whether these antibodies retain activity against newly emerged SARS-CoV-2 variants remains unclear. In this study, two representative receptor-mimicking antibodies, VIR-7229 and S2K146, were evaluated alongside S2H13, another RBD-targeting antibody. VIR-7229 and S2K146 retained neutralizing activity better than S2H13, with VIR-7229 showing the greatest retention. VIR-7229 potently neutralized the Wuhan-Hu-1, BA.1, XBB.1.5, and BA.2.86 variants and exhibited reduced yet considerable neutralizing activity against KP.3.1.1, XEC, and XEC.25.1. Enzyme-linked immunosorbent assay (ELISA) and biolayer interferometry further demonstrated that VIR-7229 maintained strong binding to spike proteins from recent variants. Computational structural analysis suggested that mutations in these variants may weaken VIR-7229 binding to the RBD but do not fully disrupt the antibody-RBD interface. These findings indicate that VIR-7229 retains considerable neutralizing activity and robust spike recognition against recent SARS-CoV-2 variants, likely through recognition of a functional interface involved in ACE2 binding. This study supports further evaluation of receptor-mimicking antibodies and may inform the design of candidate immunogens against evolving SARS-CoV-2 variants.

Indexed as

Receptor-mimicking antibodySevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Spike protein

Identifiers

PMID42698763
PMCPMC13541768

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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.