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Related Experiment Video

Updated: Sep 12, 2025

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Domain Interactions in a Chimeric Dual-domain Lysin Lead to Broad Bactericidal Activity.

Fen Hu1, Xiaomei Zhang2, Zhou Gong3

  • 1Key Laboratory of Ministry of Education for Gastrointestinal Cancer, School of Basic Medical Sciences, Fujian Medical University, Fuzhou 350002, China; State Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.

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|August 6, 2025
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Summary

Engineered chimeric lysins like ClyR show broad-spectrum activity against resistant bacteria. Inter-domain interactions within ClyR are key to its enhanced bactericidal mechanism and expanded host range.

Keywords:
SH3bantimicrobial resistancebactericidal host rangelysinpeptidoglycan hydrolase

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Phage-derived lysins are promising antimicrobial agents against multidrug-resistant bacteria.
  • Engineering lysins for a broad host range is crucial for their therapeutic potential.
  • The chimeric lysin ClyR, combining PlyCAC and PlySb domains, demonstrated an expanded host range previously.

Purpose of the Study:

  • To elucidate the mechanism behind ClyR's expanded bactericidal activity.
  • To analyze the structural and dynamic properties of the chimeric lysin ClyR.
  • To understand the role of inter-domain interactions in ClyR's function.

Main Methods:

  • X-ray diffraction to determine the crystal structure of PlySb.
  • Biophysical techniques including X-ray diffraction, cross-linking coupled mass spectrometry (CXMS), and small-angle X-ray scattering (SAXS) for ClyR structure analysis.
  • Mutagenesis and biochemical assays to investigate the functional impact of inter-domain interactions.

Main Results:

  • The crystal structure of PlySb was solved.
  • ClyR was found to possess a dynamic conformation influenced by inter-domain interactions.
  • These interactions were shown to modulate ClyR's bactericidal activity.

Conclusions:

  • The study provides structural and mechanistic insights into the chimeric lysin ClyR.
  • Inter-domain interactions are identified as critical modulators of ClyR's broad-spectrum antimicrobial activity.
  • Findings enhance understanding of how chimeric lysin structure influences host range and therapeutic efficacy.