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Related Concept Videos

Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
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):...
ABC Transporters: Importer01:27

ABC Transporters: Importer

ATP-binding cassette or ABC transporters are a class of ATP-driven pumps that hydrolyze ATP to move solutes across the membrane. They can be grouped into importers and exporters. While exporters are present in all domains of life, importers exist only in bacteria and some plants.
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:
Secondary Active Transport01:55

Secondary Active Transport

One example of how cells use the energy contained in electrochemical gradients is demonstrated by glucose transport into cells. The ion vital to this process is sodium (Na+), which is typically present in higher concentrations extracellularly than in the cytosol. Such a concentration difference is due, in part, to the action of an enzyme “pump” embedded in the cellular membrane that actively expels Na+ from a cell. Importantly, as this pump contributes to the high concentration of...
Secondary Active Transport01:32

Secondary Active Transport

One example of how cells use the energy contained in electrochemical gradients is demonstrated by glucose transport into cells. The ion vital to this process is sodium (Na+), which is typically present in higher concentrations extracellularly than in the cytosol. Such a concentration difference is due, in part, to the action of an enzyme "pump" embedded in the cellular membrane that actively expels Na+ from a cell. Importantly, as this pump contributes to the high concentration of...
ABC Transporters: Exporter01:31

ABC Transporters: Exporter

ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...

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Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments
12:28

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

Published on: October 15, 2016

Autotransporter-based cell surface display in Gram-negative bacteria.

Toon Nicolay1, Jos Vanderleyden, Stijn Spaepen

  • 1Centre of Microbial and Plant Genetics , Leuven , Belgium.

Critical Reviews in Microbiology
|July 17, 2013
PubMed
Summary

Autotransporter technology enables efficient cell surface display of proteins for biotechnology. This method uses a modular system to express heterologous proteins on bacterial surfaces, with potential applications in biocatalysis and vaccines.

Keywords:
AutodisplayType V secretion systembiotechnologyouter membrane proteinpassenger

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Protein Engineering by Yeast Surface Display
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Last Updated: May 9, 2026

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments
12:28

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Published on: October 15, 2016

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates
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Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Area of Science:

  • Microbiology and Biotechnology
  • Molecular Biology
  • Protein Engineering

Background:

  • Cell surface display of proteins is crucial for biotechnological applications like screening, biocatalysis, and vaccine development.
  • Autotransporter secretion systems in Gram-negative bacteria offer a promising platform for protein surface display due to their modular design.

Purpose of the Study:

  • To explore the potential of autotransporter-based systems for heterologous protein surface display.
  • To discuss the critical aspects and applications of autotransporter technology for displaying foreign protein domains on bacterial surfaces.

Main Methods:

  • Utilizing the modular structure of autotransporters by genetically replacing the passenger domain.
  • Constructing an autotransporter-based surface expression module with a promoter, signal peptide, passenger domain, and translocation unit.

Main Results:

  • Autotransporter technology allows for the genetic replacement of passenger domains to display heterologous proteins on the bacterial cell surface.
  • The compatibility of passenger domains with surface translocation remains a key challenge, lacking general determination rules.

Conclusions:

  • Autotransporter systems provide a versatile platform for cell surface display, adaptable for various biotechnological needs.
  • Further research is needed to establish guidelines for ensuring passenger domain compatibility for successful surface translocation and display.