REVIEW: Pathogenesis-Associated Bacterial Amyloids: The Network of Interactions

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Haidar Fayoud^1,2, Mikhail V. Belousov^1,2, Kirill S. Antonets^1,2, Anton A. Nizhnikov^1,2,a*

¹Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia

²All-Russia Research Institute for Agricultural Microbiology, 196608 St. Petersburg, Russia

^* To whom correspondence should be addressed.

Received: September 13, 2024; Revised: October 20, 2024; Accepted: October 21, 2024

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Amyloids are protein fibrils with a characteristic cross-β structure that is responsible for the unusual resistance of amyloids to various physical and chemical factors, as well as numerous pathogenic and functional consequences of amyloidogenesis. The greatest diversity of functional amyloids was identified in bacteria. The majority of bacterial amyloids are involved in virulence and pathogenesis either via facilitating formation of biofilms and adaptation of bacteria to colonization of a host organism or through direct regulation of toxicity. Recent studies have shown that, beside their commonly known activity, amyloids may be involved in the spatial regulation of proteome by modulating aggregation of other amyloidogenic proteins with multiple functional or pathological effects. Although the studies on the role of microbiome-produced amyloids in the development of amyloidoses in humans and animals have only been started, it is clear that humans as holobionts contain amyloids encoded not only by the host genome, but also by microorganisms that constitute the microbiome. Amyloids acquired from external sources (e.g., food) can interact with holobiont amyloids and modulate the effects of bacterial and host amyloids, thus adding another level of complexity to the holobiont-associated amyloid network. In this review, we described bacterial amyloids directly or indirectly involved in disease pathogenesis in humans and discussed the significance of bacterial amyloids in the three-component network of holobiont-associated amyloids.

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KEY WORDS: amyloid, protein aggregate, bacteria, fibril, virulence, pathogenesis, human, cross-seeding, beta-sheet, infection, amyloid network, holobiont

DOI: 10.1134/S0006297924120022

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