Inclusion Bodies in the Study of Amyloid Aggregation

Anna Villar-Piqué, Salvador Ventura

Research output: Chapter in BookChapterResearchpeer-review

Abstract

© 2014 by John Wiley & Sons, Inc. All rights reserved. This chapter illustrates how an increasing number of studies are taking advantage of the amyloid-like nature of the intracellular aggregates formed in bacteria for a number of different purposes, ranging from the mechanistic analysis of the process of protein aggregation in an in vivo-like environment, to the identification of novel antiamyloidogenic compounds. Protein aggregation is also a major bottleneck during the biotechnological production and purification of proteins, hindering the commercialization of protein-based drugs. Despite it having been observed recurrently that recombinant protein expression in bacterial hosts often leads to aggregation of the target protein into compact aggregated structures known as inclusion bodies (IBs). The IBs formed by different and unrelated proteins shared similar conformational properties, suggesting for the first time that the presence of amyloid-like features could be a common characteristic of bacterial protein deposits.
Original languageEnglish
Title of host publicationProtein Aggregation in Bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells
Pages93-116
Number of pages23
Volume9781118448526
DOIs
Publication statusPublished - 14 Apr 2014

Keywords

  • Amyloid aggregation
  • Bacteria
  • Biotechnological production
  • Inclusion bodies (IBs)
  • Protein-based drugs

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