ArticleMicrobial cell factories2014
Expanding the recombinant protein quality in Lactococcus lactis.
Article in Microbial cell factories, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Exploring the therapeutic potential of recombinant bovine β-defensins for antimicrobial and anti-inflammatory functions in sepsis management.Veterinary research · 2025Article
- Evaluating Host Defense Peptides: A Comparative Analysis of Synthetic Peptides and Recombinant Concatemers.Biomolecules · 2025Article
- CRISPR-Cas9 in the Tailoring of Genetically Engineered Animals.Current issues in molecular biology · 2025Review
- Evaluation of the Immunogenicity of a Pool of RecombinantVeterinary sciences · 2025Article
- Lactiplantibacillus plantarum: a new example of inclusion body producing bacteria.Microbial cell factories · 2023Article
- Potential of Oral Nanoparticles Containing Cytokines as Intestinal Mucosal Immunostimulants in Pigs: A Pilot Study.Animals : an open access journal from MDPI · 2022Article
- Prospective bacterial and fungal sources of hyaluronic acid: A review.Computational and structural biotechnology journal · 2022Review
- Immune Responses to Orally Administered RecombinantViruses · 2021Article
- Combination of an engineered Lactococcus lactis expressing CXCL12 with light-emitting diode yellow light as a treatment for scalded skin in mice.Microbial biotechnology · 2021Article
- Selecting Subpopulations of High-Quality Protein Conformers among Conformational Mixtures of Recombinant Bovine MMP-9 Solubilized from Inclusion Bodies.International journal of molecular sciences · 2021Article
- Nisin M: a Bioengineered Nisin A Variant That Retains Full Induction Capacity but Has Significantly Reduced Antimicrobial Activity.Applied and environmental microbiology · 2020Article
- Engineering Biology to Construct Microbial Chassis for the Production of Difficult-to-Express Proteins.International journal of molecular sciences · 2020Review
- A new approach to obtain pure and active proteins from Lactococcus lactis protein aggregates.Scientific reports · 2018Article
- A New Broad Range Plasmid for DNA Delivery in Eukaryotic Cells Using Lactic Acid Bacteria: In Vitro and In Vivo Assays.Molecular therapy. Methods & clinical development · 2017Article
- Functional inclusion bodies produced in the yeast Pichia pastoris.Microbial cell factories · 2016Article
- Living biointerfaces based on non-pathogenic bacteria support stem cell differentiation.Scientific reports · 2016Article
- Recombinant pharmaceuticals from microbial cells: a 2015 update.Microbial cell factories · 2016Review
- Implementation of the agmatine-controlled expression system for inducible gene expression in Lactococcus lactis.Microbial cell factories · 2015Article
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundEscherichia coli has been a main host for the production of recombinant proteins of biomedical interest, but conformational stress responses impose severe bottlenecks that impair the production of soluble, proteolytically stable versions of many protein species. In this context, emerging Generally Recognized As Safe (GRAS) bacterial hosts provide alternatives as cell factories for recombinant protein production, in which limitations associated to the use of Gram-negative microorganisms might result minimized. Among them, Lactic Acid Bacteria and specially Lactococcus lactis are Gram-positive GRAS organisms in which recombinant protein solubility is generically higher and downstream facilitated, when compared to E. coli. However, deep analyses of recombinant protein quality in this system are still required to completely evaluate its performance and potential for improvement.
resultsWe have explored here the conformational quality (through specific fluorescence emission) and solubility of an aggregation-prone GFP variant (VP1GFP) produced in L. lactis. In this context, our results show that parameters such as production time, culture conditions and growth temperature have a dramatic impact not only on protein yield, but also on protein solubility and conformational quality, that are particularly favored under fermentative metabolism.
conclusionsMetabolic regime and cultivation temperature greatly influence solubility and conformational quality of an aggregation-prone protein in L. lactis. Specifically, the present study proves that anaerobic growth is the optimal condition for recombinant protein production purposes. Besides, growth temperature plays an important role regulating both protein solubility and conformational quality. Additionally, our results also prove the great versatility for the manipulation of this bacterial system regarding the improvement of functionality, yield and quality of recombinant proteins in this species. These findings not only confirm L. lactis as an excellent producer of recombinant proteins but also reveal room for significant improvement by the exploitation of external protein quality modulators.
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