ArticleAMB Express2019
External lysis of Escherichia coli by a bacteriophage endolysin modified with hydrophobic amino acids.
Article in AMB Express, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 48 citations in OpenAlex.
- Evaluation of the Therapeutic Effect of a Bovine-DerivedMicroorganisms · 2026Article
- Polycationic nanopeptide-fused endolysins for the control of Mannheimia haemolytica.Applied microbiology and biotechnology · 2026Article
- Antimicrobial Activity of LysX and LysP Endolysins AgainstPlants (Basel, Switzerland) · 2026Article
- Review
- Phage-derived proteins: Advancing food safety through biocontrol and detection of foodborne pathogens.Comprehensive reviews in food science and food safety · 2025Review
- Endolysins and membrane-active peptides: innovative engineering strategies against gram-negative bacteria.Frontiers in microbiology · 2025Review
- Research Progress on Strategies for Improving the Enzyme Properties of Bacteriophage Endolysins.Journal of microbiology and biotechnology · 2024Review
- Review
- Role of hypothetical protein PA1-LRP in antibacterial activity of endolysin from a newFrontiers in microbiology · 2024Article
- Antibacterial activity of vB_AbaM_PhT2 phage hydrophobic amino acid fusion endolysin, combined with colistin against Acinetobacter baumannii.Scientific reports · 2023Article
- Beyond antibiotics: phage-encoded lysins against Gram-negative pathogens.Frontiers in microbiology · 2023Review
- Motility increase of adherent invasiveFrontiers in microbiology · 2022Article
- Isolation ofFrontiers in microbiology · 2022Article
- Endolysin, a Promising Solution against Antimicrobial Resistance.Antibiotics (Basel, Switzerland) · 2021Review
- Current Status of Endolysin-Based Treatments against Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2021Review
- Bacteriophage Technology and Modern Medicine.Antibiotics (Basel, Switzerland) · 2021Review
- Engineered endolysin-based "artilysins" for controlling the gram-negative pathogen Helicobacter pylori.AMB Express · 2021Article
- Mycobacteriophages as Potential Therapeutic Agents against Drug-Resistant Tuberculosis.International journal of molecular sciences · 2021Review
- Predicting Cell Wall Lytic Enzymes Using Combined Features.Frontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Drug-resistant bacteria are a serious threat to global public health. Gram-positive bacterial endolysin preparations have been successfully used to fight Gram-positive bacteria as a novel antimicrobial replacement strategy. However, Gram-negative bacterial phage endolysins cannot be applied directly to destroy Gram-negative strains due to the externally inaccessible peptidoglycan layer of the cell wall; this has seriously hampered the development of endolysin-like antibiotics against Gram-negative bacteria. In this study, 3-12 hydrophobic amino acids were successively added to the C-terminus of Escherichia coli phage endolysin Lysep3 to create five different hydrophobic-modified endolysins. Compared with endogenous Lysep3, endolysins modified with hydrophobic amino acids surprisingly could kill E. coli from outside of the cell at the appropriate pH and endolysin concentration. The lysis ability of modified endolysins were enhanced with increasing numbers of hydrophobic amino acids at the C-terminus of endolysin. Thus, these findings demonstrate that the enhancement of hydrophobicity at the C-terminus enables the endolysin to act upon E. coli from the outside, representing a novel method of lysing Gram-negative antibiotic-resistant bacteria.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.