Heterologous Expression Systems for Plant Defensin Expression: Examples of Success and Pitfalls

Curr Protein Pept Sci. 2017;18(4):391-399. doi: 10.2174/1389203717666160625070414.

Abstract

Defensins are a superfamily of antimicrobial peptides, present in vertebrates, invertebrates, fungi and plants, suggesting that they appeared prior to the divergence in eukaryotes. The destitution of toxicity to mammalian cells of plant defensins has led to a new research ground, i.e., their potential medical use against human infectious diseases. Isolating defensins from natural sources, like plant tissues, can be time-consuming, labor intensive and usually present low yields. Strategies for large-scale production of purified active defensins have been employed using heterologous expression systems (HES) for defensin production, usually based in E. coli system. Like any other technology, HES present limitations and drawbacks demanding a careful experimental design prior the system selection. This review is proposed to discuss some of the major concerns when choosing to heterologously express plant defensins, with special attention on bacterial expression systems.

Keywords: E. coli; antimicrobial peptides; carrier protein; fusion; inclusion bodies; secretion signal.

Publication types

  • Review

MeSH terms

  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / metabolism*
  • Cloning, Molecular / methods*
  • Databases, Genetic
  • Defensins / biosynthesis
  • Defensins / genetics*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Genetic Vectors / chemistry
  • Genetic Vectors / metabolism
  • Inclusion Bodies / chemistry
  • Pichia / genetics
  • Pichia / metabolism
  • Plant Proteins / biosynthesis
  • Plant Proteins / genetics*
  • Plants / chemistry*
  • Plants / genetics
  • Plants / metabolism
  • Protein Folding
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / genetics
  • Reverse Genetics / methods

Substances

  • Anti-Infective Agents
  • Defensins
  • Plant Proteins
  • Recombinant Proteins