Evidence map›Paper›PMID 40733665›Full record

ArticleVaccines2025

Characterization of the Binding and Inhibition Mechanisms of a Novel Neutralizing Monoclonal Antibody Targeting the Stem Helix Region in the S2 Subunit of the Spike Protein of SARS-CoV-2.

Selene Si Ern Tan, Ee Hong Tam, Kah Man Lai, Yanjun Wu, Tianshu Xiao, Yee-Joo Tan

Abstract read
In one paragraph

Article in Vaccines, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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.

Selene Si Ern TanInfectious Diseases Translational Research Programme, Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117545, Singapore.ORCID 0009-0009-5166-6164
Ee Hong TamSchool of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore.ORCID 0009-0008-6904-1149
Kah Man LaiInfectious Diseases Translational Research Programme, Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117545, Singapore.
Yanjun WuSchool of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore.ORCID 0009-0007-3861-5712
Tianshu XiaoSchool of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore.ORCID 0000-0003-1287-1228
Yee-Joo TanInfectious Diseases Translational Research Programme, Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117545, Singapore.ORCID 0000-0002-2278-4497

Funding

Ministry of Education RG36/24Ministry of Education T2EP30121-0012Ministry of Health PREPARE-OC-VT-2024-003
6 · The paper itself

Abstract

BACKGROUND/

objectivesFor viral entry into host cells, the spike (S) protein of coronavirus (CoV) uses its S1 domain to bind to the host receptor and S2 domain to mediate the fusion between virion and cellular membranes. The S1 domain acquired multiple mutations as the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) evolved to give rise to Variant of Concerns (VOCs) but the S2 domain has limited changes. In particular, the stem helix in S2 did not change significantly and it is fairly well-conserved across multiple beta-CoVs. In this study, we generated a murine mAb 7B2 binding to the stem helix of SARS-CoV-2.

methodsMAb 7B2 was isolated from immunized mouse and its neutralization activity was evaluated using microneutralization, plaque reduction and cell-cell fusion assays. Bio-layer interferometry was used to measure binding affinity and AlphaFold3 was used to model the antibody-antigen interface.

resultsMAb 7B2 has lower virus neutralizing and membrane block activities when compared to a previously reported stem helix-binding human mAb S2P6. Alanine scanning and AlphaFold3 modeling reveals that residues K1149 and D1153 in S form a network of polar interactions with the heavy chain of 7B2. Conversely, S2P6 binding to S is not affected by alanine substitution at K1149 and D1153 as indicated by the high ipTM scores in the predicted S2P6-stem helix structure.

conclusionsOur detailed characterization of the mechanism of inhibition of 7B2 reveals its distinctive binding model from S2P6 and yields insights on multiple neutralizing and highly conserved epitopes in the S2 domain which could be key components for pan-CoV vaccine development.

Indexed as

monoclonal antibodiesSARS-CoV-2spike protein

Identifiers

PMID40733665
PMCPMC12299175

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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.