Related Experiment Video
Updated: Mar 29, 2026

Synthesis of Masarimycin, a Small Molecule Inhibitor of Gram-Positive Bacterial Growth
Published on: January 7, 2022
Antibacterial Activity of Stenotrophomonas maltophilia Endolysin P28 against both Gram-positive and Gram-negative
Hongling Dong1, Chaoyang Zhu1, Jingyi Chen1
1College of Life Sciences, Wuhan University Wuhan, China.
Abstract:
Maltocin P28 is a phage-tail like bacteriocin produced by Stenotrophomonas maltophilia P28. The ORF8 of maltocin P28 gene cluster is predicted to encode an endolysin and we name it endolysin P28. Sequence analysis revealed that it contains the lysozyme_like superfamily conserved domain. Endolysin P28 has the four consensus motifs as that of Escherichia coli phage lambda gpR. In this study, endolysin P28 was expressed in E. coli BL21 (DE3) and purified with a C-terminal oligo-histidine tag. The antibacterial activity of endolysin P28 increased as the temperature rose from 25 to 45°C. Thermostability assays showed that endolysin P28 was stable up to 50°C, while its residual activity was reduced by 55% after treatment at 70°C for 30 min. Acidity and high salinity could enhance its antibacterial activity. Endolysin P28 exhibited a broad antibacterial activity against 14 out of 16 tested Gram-positive and Gram-negative bacteria besides S. maltophilia. Moreover, it could effectively lyse intact Gram-negative bacteria in the absence of ethylenediaminetetraacetic acid as an outer membrane permeabilizer. Therefore, the characteristics of endolysin P28 make it a potential therapeutic agent against multi-drug-resistant pathogens.
Insights
Endolysin P28, derived from Stenotrophomonas maltophilia, shows potent antibacterial activity against various pathogens. This phage-derived enzyme is a promising candidate for developing new antimicrobial therapies.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Maltocin P28 is a bacteriocin from Stenotrophomonas maltophilia P28.
- The ORF8 gene in the maltocin P28 cluster encodes endolysin P28, featuring a lysozyme-like domain and conserved motifs similar to E. coli phage lambda gpR's endolysin.
Purpose of the Study:
- To express, purify, and characterize endolysin P28.
- To evaluate the antibacterial activity and stability of endolysin P28.
- To assess its potential as a therapeutic agent against multi-drug-resistant pathogens.
Main Methods:
- Endolysin P28 was expressed in E. coli BL21 (DE3) and purified using a C-terminal oligo-histidine tag.
- Antibacterial activity was tested across a temperature range (25-70°C) and under varying pH and salinity conditions.
- Thermostability was assessed by measuring residual activity after heat treatment.
- The lytic spectrum against Gram-positive and Gram-negative bacteria was determined.
Main Results:
- Endolysin P28 activity increased with temperature up to 45°C and remained stable up to 50°C.
- Acidity and high salinity enhanced its antibacterial efficacy.
- It demonstrated broad-spectrum activity against 14 of 16 tested bacterial species, including Gram-negative and Gram-positive bacteria.
- Endolysin P28 effectively lysed intact Gram-negative bacteria without requiring ethylenediaminetetraacetic acid.
Conclusions:
- Endolysin P28 exhibits significant antibacterial properties, including broad-spectrum activity and stability under specific conditions.
- Its ability to lyse Gram-negative bacteria without permeabilizers highlights its potential.
- Endolysin P28 is a promising candidate for developing novel therapeutic strategies against multi-drug-resistant bacteria.
Related Concept Videos
Antimicrobial Effectiveness
Inhibitors of Gram-positive Cell Wall Synthesis
Clinical Significance of Antibiotic Resistance
Special Staining Techniques
Antimicrobial Proteins
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...

