Characterization of amyloid-like properties in bacterial intracellular aggregates

Anna Villar-Pique, Susanna Navarro, Salvador Ventura

Research output: Contribution to journalReview articleResearchpeer-review

3 Citations (Scopus)


Protein aggregation into amyloid conformations is associated with more than 50 different human disorders. Recent studies demonstrate that the expression in bacteria of amyloid proteins results in the formation of intracellular aggregates structurally related to those underlying human diseases. The ease with which prokaryotic organisms can be genetically and biochemically manipulated makes them useful systems for studying how and why protein aggregates inside the cell, providing a tractable environment to rationally model in vivo amyloid formation. In this chapter we present an overview of the methods used to characterize the kinetic, structural, and functional properties of amyloid-like bacterial intracellular aggregates and how they can be employed to screen for lead compounds that might modulate amyloid deposition.
Original languageEnglish
Pages (from-to)99-122
JournalMethods in Molecular Biology
Publication statusPublished - 1 Jan 2015


  • Amyloid
  • Bacteria
  • Inclusion bodies
  • Protein aggregation


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