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Related Experiment Video

Updated: Feb 22, 2026

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Antibody Screening and Binding Prediction Analysis Targeting Stx2.

Jilei Wu1, Chenghua Liu2, Fenghao Peng2

  • 1College of Biotechnology, Jiangsu University of Science and Technology, Zhenjiang 212000, China.

Antibodies (Basel, Switzerland)
|February 20, 2026
PubMed
Summary
This summary is machine-generated.

Two monoclonal antibodies, YG12-1 and YG12-2, show promise in neutralizing Shiga toxin 2 (Stx2), a key factor in severe E. coli infections. While YG12-2 binds more strongly, YG12-1 demonstrates superior protective effects, highlighting complex antibody efficacy.

Keywords:
Escherichia coli O157:H7 infectionImmuneBuilderShiga toxin type 2 (Stx2)human monoclonal antibodystructural prediction

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Area of Science:

  • Immunology
  • Microbiology
  • Structural Biology

Background:

  • Shiga toxin (Stx), particularly Stx2, produced by enterohemorrhagic Escherichia coli (EHEC), is a potent exotoxin causing severe conditions like hemolytic uremic syndrome (HUS).
  • Current therapeutic options for Stx2-induced complications are limited, necessitating the development of novel treatment strategies.

Purpose of the Study:

  • To identify and characterize human monoclonal antibodies targeting Shiga toxin 2 (Stx2).
  • To evaluate the structural and functional properties of Stx2-neutralizing antibodies for potential therapeutic applications.

Main Methods:

  • Phage display library screening to identify human monoclonal antibodies YG12-1 and YG12-2.
  • Integrated computational modeling (ImmuneBuilder, Rosetta) and experimental validation (ELISA, SPR) to assess antibody-antigen interactions.
  • In vivo efficacy assessment using a murine model of acute peritoneal infection.

Main Results:

  • Structural analysis revealed YG12-2 has superior binding affinity to Stx2 due to longer CDRH3 topology and enhanced electrostatic complementarity.
  • Despite higher binding affinity, YG12-1 exhibited greater protective activity in a murine infection model.
  • A non-linear correlation between antibody affinity and in vivo efficacy was observed, influenced by epitope accessibility and pharmacokinetics.

Conclusions:

  • Monoclonal antibodies YG12-1 and YG12-2 represent a potential therapeutic strategy against Stx2-mediated E. coli O157:H7 infections.
  • Functional efficacy in vivo is a critical determinant of therapeutic success, beyond simple binding affinity.