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Towards revealing the structure of bacterial inclusion bodies Wang LPrion 2009[Jul]; 3 (3): 139-45Protein aggregation is a widely observed phenomenon in human diseases, biopharmaceutical production, and biological research. Protein aggregates are generally classified as highly ordered, such as amyloid fibrils, or amorphous, such as bacterial inclusion bodies. Amyloid fibrils are elongated filaments with diameters of 6-12 nm, they are comprised of residue-specific cross-beta structure, and display characteristic properties, such as binding with amyloid-specific dyes. Amyloid fibrils are associated with dozens of human pathological conditions, including Alzheimer disease and prion diseases. Distinguished from amyloid fibrils, bacterial inclusion bodies display apparent amorphous morphology. Inclusion bodies are formed during high-level recombinant protein production, and formation of inclusion bodies is a major concern in biotechnology. Despite of the distinctive morphological difference, bacterial inclusion bodies have been found to have some amyloid-like properties, suggesting that they might contain structures similar to amyloid-like fibrils. Recent structural data further support this hypothesis, and this review summarizes the latest progress towards revealing the structural details of bacterial inclusion bodies.|Alzheimer Disease/metabolism[MESH]|Amino Acid Sequence[MESH]|Amyloid/*chemistry[MESH]|Animals[MESH]|Bacterial Proteins/chemistry[MESH]|Escherichia coli/*metabolism[MESH]|Humans[MESH]|Inclusion Bodies/chemistry/*metabolism[MESH]|Magnetic Resonance Spectroscopy[MESH]|Mice[MESH]|Microscopy, Electron/methods[MESH]|Models, Biological[MESH]|Molecular Sequence Data[MESH]|Prion Diseases/metabolism[MESH]|Protein Binding[MESH]|Protein Structure, Secondary[MESH]|Recombinant Proteins/chemistry[MESH]|Spectroscopy, Fourier Transform Infrared[MESH]|X-Ray Diffraction[MESH] |
