Bacterial inclusion bodies contain amyloid-like structure

Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can be composed of native globular molecules, suc...

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Bibliographic Details
Published in:PLoS biology 2008-08, Vol.6 (8), p.e195-e195
Main Authors: Wang, Lei, Maji, Samir K, Sawaya, Michael R, Eisenberg, David, Riek, Roland
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amyloid - metabolism
Animals
Antigens, Bacterial - genetics
Bacteria
Bacterial Proteins - genetics
Biochemistry
Biophysics
Biotechnology
Bone Morphogenetic Protein 2
Bone Morphogenetic Proteins - genetics
Diabetes
E coli
Enzymes
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli - ultrastructure
Experiments
Humans
Inclusion Bodies - metabolism
Inclusion Bodies - ultrastructure
Microbiology
Molecular Sequence Data
Molecular weight
Myelin Proteins
Myelin-Associated Glycoprotein - genetics
Myelin-Oligodendrocyte Glycoprotein
Neurological Disorders
NMR
Nuclear magnetic resonance
Parkinson's disease
Prokaryotes
Protein folding
Protein Structure, Secondary
Rats
Transforming Growth Factor beta - genetics
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Summary:Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can be composed of native globular molecules, such as the hemoglobin molecules in sickle-cell fibrils, or can be reorganized beta-sheet-rich aggregates, termed amyloid-like fibrils. Amyloid fibrils are associated with several pathological conditions in humans, including Alzheimer disease and diabetes type II. We studied the structure of bacterial inclusion bodies, which have been believed to belong to the amorphous class of aggregates. We demonstrate that all three in vivo-derived inclusion bodies studied are amyloid-like and comprised of amino-acid sequence-specific cross-beta structure. These findings suggest that inclusion bodies are structured, that amyloid formation is an omnipresent process both in eukaryotes and prokaryotes, and that amino acid sequences evolve to avoid the amyloid conformation.
ISSN:1545-7885
1544-9173
1545-7885
DOI:10.1371/journal.pbio.0060195