Abstract
An increasing number of proteins are being shown to assemble into amyloid structures, self-seeding fibrillar aggregates that may lead to pathological states or play essential biological functions in organisms. Bacterial cell factories have raised as privileged model systems to understand the mechanisms behind amyloid assembly and the cellular fitness cost associated to the formation of these aggregates. In the near future, these bacterial systems will allow implementing high-throughput screening approaches to identify effective modulators of amyloid aggregation.
Highlights
An increasing number of proteins are being shown to assemble into amyloid structures, self-seeding fibrillar aggregates that may lead to pathological states or play essential biological functions in organisms
A first inflection in the field came along with early reports describing a selective molecular structure inside inclusion bodies (IBs). It has been found a substantial similitude between the properties of these bacterial aggregates and the pathological fibrils linked to amyloidosis
These findings come from independent studies using completely different protein models, not related in sequence or structure, suggesting that the amyloid signature might be a generic feature of bacterial aggregates. High resolution approaches, such as hydrogen/deuterium exchange by NMR or solid-state NMR have been used to study different bacterial IBs, defining their molecular structure at the residue level. These analysis prove that, at least for amyloidogenic proteins, bacterial IBs and fibrils share the same amyloid core
Summary
An increasing number of proteins are being shown to assemble into amyloid structures, self-seeding fibrillar aggregates that may lead to pathological states or play essential biological functions in organisms. A first inflection in the field came along with early reports describing a selective molecular structure inside IBs. It has been found a substantial similitude between the properties of these bacterial aggregates and the pathological fibrils linked to amyloidosis.
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