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Related Concept Videos

Operons02:09

Operons

Prokaryotes can control gene expression through operons—DNA sequences consisting of regulatory elements and clustered, functionally related protein-coding genes. Operons use a single promoter sequence to initiate transcription of a gene cluster (i.e., a group of structural genes) into a single mRNA molecule. The terminator sequence ends transcription. An operator sequence, located between the promoter and structural genes, prohibits the operon’s transcriptional activity if bound by a repressor...
Inducible Operons: lac Operon01:25

Inducible Operons: lac Operon

The lac operon in Escherichia coli is a model for understanding inducible gene regulation and metabolic flexibility. It integrates local control by lactose and global regulation through catabolite repression, enabling E. coli to preferentially metabolize glucose when available and switch to lactose utilization when glucose is scarce.Structure and Function of the lac OperonThe lac operon contains three structural genes: lacZ (β-galactosidase), lacY (lactose permease), and lacA (thiogalactoside...
Coordination of Gene Expression Processes in Bacteria01:29

Coordination of Gene Expression Processes in Bacteria

The DNA replication, transcription, and translation processes are intricately coupled in bacteria, allowing efficient gene expression and rapid protein synthesis. While this physical and functional coordination is advantageous, it introduces challenges that bacteria overcome through specific regulatory mechanisms.Coupling of Replication, Transcription, and TranslationThe coupling of replication, transcription, and translation is a hallmark of bacterial gene expression. As the replisome unwinds...
Production of Pharmaceuticals01:30

Production of Pharmaceuticals

Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...
Gram-negative Bacterial Protein Secretion Systems01:17

Gram-negative Bacterial Protein Secretion Systems

Gram-negative bacteria utilize sophisticated protein secretion systems to transport proteins across their double-membrane envelope into the extracellular environment or host cells. Based on their mechanism of action, these systems are classified into one-step and two-step pathways.One-Step Secretion Systems (Types I, III, IV, and VI)One-step secretion systems bypass the periplasm entirely, forming a continuous channel that spans both the inner and outer membranes:Type I Secretion System (T1SS):...

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Related Experiment Video

Updated: May 26, 2026

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
05:58

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells

Published on: February 24, 2026

Heterologous protein expression by Lactococcus lactis.

Julio Villatoro-Hernández1, Oscar P Kuipers, Odila Saucedo-Cárdenas

  • 1Department of Molecular Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands.

Methods in Molecular Biology (Clifton, N.J.)
|December 14, 2011
PubMed
Summary

Lactococcus lactis, a safe lactic acid bacterium (LAB), serves as an efficient cell factory for producing medical proteins. Its nonpathogenic nature allows for in vivo mucosal delivery, expanding therapeutic applications beyond inflammatory bowel diseases.

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Area of Science:

  • Microbiology
  • Biotechnology
  • Protein Expression

Background:

  • Lactic acid bacteria (LAB) like Lactococcus lactis are nonpathogenic and non-colonizing, making them suitable for in vivo applications.
  • Previous clinical trials using L. lactis for inflammatory bowel diseases demonstrate its safety and therapeutic potential.
  • The ability to engineer LAB for producing therapeutic proteins offers a novel approach in medicine.

Purpose of the Study:

  • To detail the utilization of Lactococcus lactis as a cell factory for producing heterologous proteins with medical relevance.
  • To explore the expression, localization, and detection of these therapeutically important proteins within L. lactis.
  • To establish a standardized protocol for sample processing to facilitate protein detection.

Main Methods:

  • Engineering Lactococcus lactis strains for the expression of heterologous proteins.
  • Investigating the subcellular localization of the expressed heterologous proteins within L. lactis.
  • Developing and applying a standardized protocol for cell and cell-free fraction processing.
  • Utilizing detection methods to identify the targeted heterologous protein expressed by L. lactis.

Main Results:

  • Demonstrated successful heterologous protein expression in Lactococcus lactis.
  • Characterized the subcellular localization of expressed proteins.
  • Validated a standardized protocol for protein detection in processed samples.
  • Confirmed the potential of L. lactis as a viable platform for therapeutic protein production.

Conclusions:

  • Lactococcus lactis is a safe and effective cell factory for producing medically relevant heterologous proteins.
  • The established methods enable reliable detection and characterization of these proteins.
  • This platform holds promise for developing new therapeutic strategies for various diseases beyond inflammatory bowel diseases.