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Proteins adopt functionally active conformations after type III secretion.

Kevin James Metcalf1,2, James Lea Bevington1, Sandy Lisette Rosales3

  • 1Department of Chemical and Biomolecular Engineering, University of California, Berkeley, CA, 94720, USA.

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|December 25, 2016
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Summary
This summary is machine-generated.

Bacterial secretion systems enable protein production by allowing proteins to fold correctly in the extracellular space. This strategy simplifies purification and improves efficiency for diverse protein targets.

Keywords:
Protein foldingProtein secretionT3SS

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Area of Science:

  • Microbiology
  • Biotechnology
  • Protein Engineering

Background:

  • Bacterial secretion simplifies protein purification by releasing proteins extracellularly.
  • Traditional methods require cell lysis, complicating protein recovery.
  • The type III secretion system (T3SS) translocates proteins but requires unfolding.

Purpose of the Study:

  • To evaluate the efficacy of T3SS for producing correctly folded heterologous proteins.
  • To characterize and quantify protein folding after secretion via T3SS.
  • To identify factors influencing extracellular protein folding.

Main Methods:

  • Assayed function of secreted beta-lactamase, alkaline phosphatase, and a single-chain variable fragment.
  • Analyzed structural and chemical features of secreted proteins.
  • Investigated the impact of NaCl concentration on folding efficiency.

Main Results:

  • Secreted enzymes and antibody fragment refolded correctly and were functional extracellularly.
  • Essential protein features like multimerization and disulfide bonds formed post-secretion.
  • Extracellular NaCl concentration influenced folding efficiency in a protein-dependent manner.

Conclusions:

  • Secreted proteins can achieve active conformations extracellularly through post-translational modifications.
  • Protein refolding propensity varies and is sensitive to the extracellular environment.
  • Strategies exist to control bacterial secretion and ensure correct folding of target proteins.