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Related Experiment Video

Updated: Jan 15, 2026

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Mechano-Locking Strategy for Broad-Spectrum SARS-CoV-2 Neutralization.

Yang Ye1,2, Shijie Chen1,2, Yixiang Zhang3,4

  • 1Kidney Disease Center of the First Affiliated Hospital and Department of Cell Biology, Zhejiang University School of Medicine, Hangzhou, Zhejiang, 310058, China.

Small (Weinheim an Der Bergstrasse, Germany)
|October 7, 2025
PubMed
Summary

Researchers developed a novel mechano-locking strategy using bispecific antibodies (bsAbs) to neutralize viruses like SARS-CoV-2. This approach enhances viral protein stability, offering a mutation-resistant method for developing new antiviral therapies.

Keywords:
SARS‐CoV‐2 spikebispecific antibodiesmechanobiologyneutralizing antibodiessingle‐molecule magnetic tweezers

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Area of Science:

  • Virology
  • Immunology
  • Biophysics

Background:

  • Viral entry relies on surface protein-receptor interactions, a target for conventional neutralization.
  • Rapid viral mutation, as seen in SARS-CoV-2, HIV, and influenza, limits the effectiveness of current antiviral strategies.
  • A new approach is needed to overcome mutation-driven resistance in viral therapeutics.

Purpose of the Study:

  • To propose and validate a novel mechano-locking strategy for viral neutralization.
  • To utilize bispecific antibodies (bsAbs) to stabilize viral spike proteins in their prefusion conformation.
  • To develop mutation-resistant antiviral therapeutics.

Main Methods:

  • SARS-CoV-2 spike protein was used as a model system.
  • Bispecific antibodies (bsAbs) were designed to lock the spike protein, preventing force-induced conformational changes.
  • Pseudoviral assays were employed to assess neutralization efficacy against SARS-CoV-2 variants.
  • Single-molecule magnetic tweezers experiments were conducted to measure mechanical stability.

Main Results:

  • The developed bsAbs showed broad-spectrum neutralization against multiple SARS-CoV-2 variants.
  • bsAbs significantly increased the mechanical force required for spike protein S1-S2 subunit dissociation.
  • This mechano-locking strategy enhanced the mechanical stability of the spike protein.

Conclusions:

  • The mechano-locking strategy provides a mutation-resistant approach to viral neutralization.
  • Stabilizing viral proteins enhances their resistance to conformational changes and mutations.
  • This study introduces a new paradigm for designing biomechanically enhanced antiviral therapeutics applicable to enveloped viruses.