![]() In humans, protein aggregation has been found associated with numerous protein misfolding diseases ( Stirling et al., 2003 Gregersen et al., 2006) such as Huntington ( Jimenez-Sanchez et al., 2017), Alzheimer ( De Strooper and Karran, 2016), and Parkinson’s diseases ( Kalia and Lang, 2015). These proteins are generally expressed from foreign or mutated genes without proper post-translational modifications and/or folding ( Tsumoto et al., 2003). Inclusion bodies (IBs) are nuclear, cytoplasmic, or periplasmic aggregates of bio-macromolecules, mostly proteins. Additionally, the unique features of protein inclusion bodies, the mechanism and influencing factors of their formation, and their potential advantages will also be discussed. These approaches will be comprehensively highlighted with some of the new developments in this review. coli, altering expression vectors, and modifying the proteins of interest. To overcome this hurdle, different strategies have been developed through adjusting growth conditions, engineering host strains of E. However, the formation of inclusion bodies is a frequently encountered challenge for producing soluble and functional recombinant proteins. Recombinant proteins are becoming increasingly important for industrial applications, where Escherichia coli is the most widely used bacterial host for their production. 3Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON, Canada.2Department of Biology, University of Waterloo, Waterloo, ON, Canada.1Guelph Research and Development Centre, Agriculture and Agri-Food Canada, Guelph, ON, Canada.Hassan 1, Nadine Abraham 1,3, Xiu-Zhen Li 1 and Ting Zhou 1* ![]() Arshpreet Bhatwa 1,2, Weijun Wang 1, Yousef I. ![]()
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