ArticleApplied and environmental microbiology2010
Characterization of a novel LysM domain from Lactobacillus fermentum bacteriophage endolysin and its use as an anchor to display heterologous proteins on the surfaces of lactic acid bacteria.
Article in Applied and environmental microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 73 citations in OpenAlex.
- Identification of a novel bacteriophage attachment site into ffs, the 4.5S non-coding RNA component of the signal recognition particle.Scientific reports · 2025Article
- Genomic Characterisation of Limosilactobacillus fermentum CRL2085 Unveiling Probiotic Traits for Application in Cattle Feed.Environmental microbiology reports · 2025Article
- Bacterial Systems as a Precision Delivery Platform of Therapeutic Peptides for Cancer Therapy.Polymer science & technology (Washington, D.C.) · 2025Review
- Natural peptidoglycan nanoparticles enable rapid antigen purification and potent delivery of plant-derived vaccines.Plant communications · 2025Article
- Surface Display of Avian H5 and H9 Hemagglutinin Antigens on Non-Genetically ModifiedMicroorganisms · 2025Article
- Degradation of beechwood xylan using food-grade bacteria-like particles displaying β-xylosidase from Limosilactobacillus fermentum.Bioresources and bioprocessing · 2025Article
- Harnessing flagellin ofApplied and environmental microbiology · 2025Article
- Isolation and Characterization of aJournal of microbiology and biotechnology · 2025Article
- Endolysins: a new antimicrobial agent against antimicrobial resistance. Strategies and opportunities in overcoming the challenges of endolysins against Gram-negative bacteria.Frontiers in pharmacology · 2024Review
- Characterization of Lactobacilli Phage Endolysins and Their Functional Domains-Potential Live Biotherapeutic Testing Reagents.Viruses · 2023Article
- Whole genome sequence analysis of bacteriophage P1 that infects the Lactobacillus plantarum.Virus genes · 2022Article
- Engineered bacteria as drug delivery vehicles: Principles and prospects.Engineering microbiology · 2022Review
- A novel, non-GMO surface display in Limosilactobacillus fermentum mediated by cell surface hydrolase without anchor motif.BMC microbiology · 2022Article
- Expanding the Database of Signal-Anchor-Release Domain Endolysins Through Metagenomics.Probiotics and antimicrobial proteins · 2022Article
- Expanding natural transformation to improve beneficial lactic acid bacteria.FEMS microbiology reviews · 2022Article
- Characterization of antibacterial activity of a N-acetylmuramoyl-L-alanine amidase produced by Latilactobacillus sakei isolated from salami.World journal of microbiology & biotechnology · 2021Article
- Strategies to display heterologous proteins on the cell surface of lactic acid bacteria using as anchor the C-terminal domain of Lactobacillus acidophilus SlpA.World journal of microbiology & biotechnology · 2020Article
- Identification and characterization of a moonlighting protein-enolase for surface display in Streptococcus thermophilus.Microbial cell factories · 2020Article
- Safety Aspects of Genetically Modified Lactic Acid Bacteria.Microorganisms · 2020Review
- A SH3_5 Cell Anchoring Domain for Non-recombinant Surface Display on Lactic Acid Bacteria.Frontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The endolysin Lyb5, from Lactobacillus fermentum temperate bacteriophage phiPYB5, showed a broad lytic spectrum against Gram-positive as well as Gram-negative bacteria. Sequence analysis revealed that the C terminus of the endolysin Lyb5 (Ly5C) contained three putative lysin motif (LysM) repeat regions, implying that Ly5C was involved in bacterial cell wall binding. To investigate the potential of Ly5C for surface display, green fluorescent protein (GFP) was fused to Ly5C at its N or C terminus and the resulting fusion proteins were expressed in Escherichia coli. After being mixed with various cells in vitro, GFP was successfully displayed on the surfaces of Lactococcus lactis, Lactobacillus casei, Lb. brevis, Lb. plantarum, Lb. fermentum, Lb. delbrueckii, Lb. helveticus, and Streptococcus thermophilus cells. Increases in the fluorescence intensities of chemically pretreated L. lactis and Lb. casei cells compared to those of nonpretreated cells suggested that the peptidoglycan was the binding ligand for Ly5C. Moreover, the pH and concentration of sodium chloride were optimized to enhance the binding capacity of GFP-Ly5C, and high-intensity fluorescence of cells was observed under optimal conditions. All results suggested that Ly5C was a novel anchor for constructing a surface display system for lactic acid bacteria (LAB). To demonstrate the applicability of the Ly5C-mediated surface display system, beta-galactosidase (beta-Gal) from Paenibacillus sp. strain K1, replacing GFP, was functionally displayed on the surfaces of LAB cells via Ly5C. The success in surface display of GFP and beta-Gal opened up the feasibility of employing the cell wall anchor of bacteriophage endolysin for surface display in LAB.
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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.