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Related Concept Videos

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization10:13

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization

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Here we present a protocol to produce gram-negative Escherichia coli (E. coli) spheroplasts and gram-positive Bacillus megaterium (B. megaterium) protoplasts to clearly visualize and rapidly characterize peptide-bacteria interactions. This provides a systematic method to define membrane localizing and translocating...
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Evaluation of Antimicrobial Activities of Nanoparticles and Nanostructured Surfaces In Vitro11:52

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We introduce four methods to evaluate the antimicrobial activities of nanoparticles and nanostructured surfaces using in vitro techniques. These methods can be adapted to study the interactions of different nanoparticles and nanostructured surfaces with a broad range of microbial...
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Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids11:56

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The protocol presents the Escherichia coli-based selective pressure incorporation of non-canonical amino acids (ncAAs) into the lactococcal antimicrobial peptide nisin. Its properties can be changed during recombinant expression via substitution with desired ncAAs in defined growth media. Resulting changes in bioactivity are mapped by growth inhibition assays and fluorescence...
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Application of the Intelligent High-Throughput Antimicrobial Sensitivity Testing/Phage Screening System and Lar Index of Antimicrobial Resistance09:59

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Here we introduce the principle, structure, and instruction of the intelligent high-throughput antimicrobial sensitivity testing/phage screening system. Its application is illustrated by using Salmonella isolated from poultry in Shandong, China, as an example. The Lar index is calculated, and its significance in evaluating antimicrobial resistance is discussed...
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Here we present a method to select for novel variants of the E. coli biotin-protein ligase BirA that biotinylates a specific target peptide. The protocol describes the construction of a plasmid for the bacterial display of the target peptide, generation of a BirA library, selection and characterization of BirA...
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Related Experiment Video

Updated: Jan 19, 2026

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization
10:13

Production and Visualization of Bacterial Spheroplasts and Protoplasts to Characterize Antimicrobial Peptide Localization

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Antagonizing Vancomycin Resistance in Enterococcus by Surface Localized Antimicrobial Display-Derived Peptides.

Yuan Liu1,2, Yuqian Jia1, Kangni Yang1

  • 1Institute of Comparative Medicine, College of Veterinary Medicine, Yangzhou University, No. 88 University South Road, Yangzhou, Jiangsu 225009, China.

ACS Infectious Diseases
|September 12, 2019
PubMed
Summary

Novel cationic peptides combat vancomycin-resistant Enterococci (VRE). SLAY peptide 1/2 shows moderate activity and synergizes with vancomycin, restoring its efficacy and preventing resistance. This offers new hope against VRE infections.

Keywords:
antibiotic adjuvantbacterial resistancevancomycin-resistant bacteria

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Related Experiment Videos

Last Updated: Jan 19, 2026

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Area of Science:

  • Antimicrobial drug discovery
  • Molecular microbiology
  • Infectious disease research

Background:

  • Vancomycin-resistant Enterococci (VRE) pose a significant threat due to a limited therapeutic pipeline.
  • Novel strategies are urgently needed to combat VRE infections.

Purpose of the Study:

  • To investigate surface localized antimicrobial display (SLAY)-derived cationic peptides as a potential treatment for VRE.
  • To evaluate the antibacterial activity and synergistic potential of SLAY peptides with vancomycin.

Main Methods:

  • Determined the antibacterial spectrum and minimal inhibitory concentration (MIC) of SLAY peptide 1/2 against Enterococci.
  • Assessed synergistic activity between SLAY-P1 and vancomycin against VRE.
  • Conducted mechanistic studies on the inhibition of the vanRS two-component system.
  • Evaluated efficacy in a Galleria mellonella infection model.

Main Results:

  • SLAY peptide 1/2 exhibited moderate bactericidal activity against Enterococcus (MIC: 2-8 μg/mL).
  • Significant synergy was observed between SLAY-P1 and vancomycin against VRE.
  • SLAY-P1 inhibited vanRS transcription, restoring vancomycin activity and cell wall precursor accumulation.
  • Combination therapy prevented vancomycin resistance emergence and improved survival in Galleria mellonella.

Conclusions:

  • SLAY-derived cationic peptides demonstrate antibacterial activity against VRE.
  • SLAY-P1 effectively reverses vancomycin resistance in Enterococcus by targeting the vanRS system.
  • These peptides represent promising candidates for developing novel therapies against vancomycin-resistant pathogens.