ArticleApplied and environmental microbiology2008
System using tandem repeats of the cA peptidoglycan-binding domain from Lactococcus lactis for display of both N- and C-terminal fusions on cell surfaces of lactic acid bacteria.
Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 42 citations in OpenAlex.
- A novel bacterium-like particles platform displaying antigens by new anchoring proteins induces efficacious immune responses.Frontiers in microbiology · 2024Article
- Recent advances in genetic tools for engineering probiotic lactic acid bacteria.Bioscience reports · 2023Article
- Progress of Molecular Display Technology UsingMicroorganisms · 2023Review
- Article
- Surface display of hirame novirhabdovirus (HIRRV) G protein in Lactococcus lactis and its immune protection in flounder (Paralichthys olivaceus).Microbial cell factories · 2019Article
- Immobilization of β-Galactosidases on theCatalysts (Basel, Switzerland) · 2019Article
- Screening for New Surface Anchoring Domains forFrontiers in microbiology · 2019Article
- Functional and structural characterization of a novel putative cysteine protease cell wall-modifying multi-domain enzyme selected from a microbial metagenome.Scientific reports · 2016Article
- Display of recombinant proteins at the surface of lactic acid bacteria: strategies and applications.Microbial cell factories · 2016Review
- Improvement of LysM-mediated surface display of designed ankyrin repeat proteins (DARPins) in recombinant and nonrecombinant strains of Lactococcus lactis and Lactobacillus Species.Applied and environmental microbiology · 2015Article
- Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications.Applied microbiology and biotechnology · 2014Review
- A genetically engineered protein domain binding to bacterial murein, archaeal pseudomurein, and fungal chitin cell wall material.Applied microbiology and biotechnology · 2012Article
- Murein and pseudomurein cell wall binding domains of bacteria and archaea--a comparative view.Applied microbiology and biotechnology · 2011Review
- Heterologous protein display on the cell surface of lactic acid bacteria mediated by the s-layer protein.Microbial cell factories · 2011Article
- Identification of candidate carrier proteins for surface display on Lactococcus lactis by theoretical and experimental analyses of the surface proteome.Applied and environmental microbiology · 2011Article
- Engineered lactic acid bacterium Lactococcus lactis capable of binding antibodies and tumor necrosis factor alpha.Applied and environmental microbiology · 2010Article
- Display of both N- and C-terminal target fusion proteins on the Aspergillus oryzae cell surface using a chitin-binding module.Applied microbiology and biotechnology · 2010Article
- 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.Applied and environmental microbiology · 2010Article
- Effects of L1-ORF2 fragments on green fluorescent protein gene expression.Genetics and molecular biology · 2009Article
- Surface display of heterologous proteins in Bacillus thuringiensis using a peptidoglycan hydrolase anchor.Microbial cell factories · 2009Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here, we established a system for displaying heterologous protein to the C terminus of the peptidoglycan-binding domain (cA domain) of AcmA (a major autolysin from Lactococcus lactis). Western blot and flow cytometric analyses revealed that the fusion proteins (cA-AmyA) of the cA domain and alpha-amylase from Streptococcus bovis 148 (AmyA) are efficiently expressed and successfully displayed on the surfaces of L. lactis cells. AmyA was also displayed on the cell surface while retaining its activity. Moreover, with an increase in the number of cA domains, the quantity of cA-AmyA fusion proteins displayed on the cell surface increased. When three repeats of the cA domain were used as an anchor protein, 82% of alpha-amylase activity was detected on the cells. The raw starch-degrading activity of AmyA was significantly higher when AmyA was fused to the C terminus of the cA domain than when it was fused to the N terminus. In addition, cA-AmyA fusion proteins were successfully displayed on the cell surfaces of Lactobacillus plantarum and Lactobacillus casei.
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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.