title: Characterization of amyloid-like properties in bacterial intracellular aggregates.
abstract: 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.
authors.affiliation: Departament de Bioquímica i Biologia Molecular, Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, Cerdanyola del Vallés, 08193, Barcelona, Spain.
authors.forename: Anna
authors.initials: A
authors.lastname: Villar-Pique
authors.forename: Susanna
authors.initials: S
authors.lastname: Navarro
authors.forename: Salvador
authors.initials: S
authors.lastname: Ventura
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D000818:Animals; D001419:Bacteria / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D066329:Protein Aggregates / Q000502:physiology*
chemical_list: D000682:Amyloid; D066329:Protein Aggregates