Misfolding and aggregation of proteins have a negative impact on all living 
organisms. In recent years, aggregation has been studied in detail due to its 
involvement in neurodegenerative diseases, including Alzheimer's, Parkinson's 
and Huntington's diseases, and type II diabetes--all associated with 
accumulation of amyloid fibrils. This research highlighted the central 
importance of protein homeostasis, or proteostasis for short, defined as the 
cellular state in which the proteome is both stable and functional. It 
implicates an equilibrium between synthesis, folding, trafficking, aggregation, 
disaggregation and degradation. In accordance with the eukaryotic systems, it 
has been documented that protein aggregation also reduces fitness of bacterial 
cells, but although our understanding of the cellular protein quality control 
systems is perhaps most detailed in bacteria, the use of bacterial proteostasis 
as a drug target remains little explored. Here we describe protein aggregation 
as a normal physiological process and its role in bacterial virulence and we 
shed light on how bacteria defend themselves against the toxic threat of 
aggregates. We review the impact of aggregates on bacterial viability and look 
at the ways that bacteria use to maintain a balance between aggregation and 
functionality. The proteostasis in bacteria can be interrupted via 
overexpression of proteins, certain antibiotics such as aminoglycosides, as well 
as antimicrobial peptides--all leading to loss of cell viability. Therefore 
intracellular protein aggregation and disruption of proteostatic balance in 
bacteria open up another strategy that should be explored towards the discovery 
of new antimicrobials.