We find them here, we find them there: Functional bacterial amyloid |
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Authors: | D Otzen P H Nielsen |
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Institution: | (1) Interdisciplinary Nanoscience Centre, Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus C, Denmark;(2) Department of Biotechnology, Chemistry and Environmental Engineering, Aalborg University, Sohngaardsholmsvej 57, 9000 Aalborg, Denmark |
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Abstract: | Protein amyloid is often deposited in connection with neurodegenerative diseases. Such deposits generally possess three principal drawbacks: cytotoxicity, lack of spatial control in their deposition and structural polymorphism. These are typical features of biologically non-optimized systems which have not been exposed to evolutionary pressure. Nevertheless, Nature uses the cross-beta self-organizing principle in many structural contexts where a strong but pliable material is needed. Functional amyloid is found in humans, invertebrates, fungi and, not least, bacteria, in which amyloid may be the rule rather than the exception. Detailed case studies reveal how directed nucleation can use tailor-made proteins optimized to assume a specific amyloid conformation, leading to remarkably robust assemblies. This makes it highly challenging to purify and analyze the products formed in vivo. We contrast pathogenic and in-vitro-formed amyloid with functional amyloid, paying particular reference to bacterial amyloid, and discuss challenges and perspectives in identifying and characterizing this class of protein. |
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Keywords: | Protein bacteria aggregate CsgA functional amyloid cytotoxicity polymorphism |
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