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Updated: Sep 7, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Structural Mimicry in Microbial and Antimicrobial Amyloids
Nimrod Golan1, Yizhaq Engelberg1, Meytal Landau1,2
1Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel;
Abstract:
The remarkable variety of microbial species of human pathogens and microbiomes generates significant quantities of secreted amyloids, which are structured protein fibrils that serve diverse functions related to virulence and interactions with the host. Human amyloids are associated largely with fatal neurodegenerative and systemic aggregation diseases, and current research has put forward the hypothesis that the interspecies amyloid interactome has physiological and pathological significance. Moreover, functional and molecular-level connections between antimicrobial activity and amyloid structures suggest a neuroimmune role for amyloids that are otherwise known to be pathological. Compared to the extensive structural information that has been accumulated for human amyloids, high-resolution structures of microbial and antimicrobial amyloids are only emerging. These recent structures reveal both similarities and surprising departures from the typical amyloid motif, in accordance with their diverse activities, and advance the discovery of novel antivirulence and antimicrobial agents. In addition, the structural information has led researchers to postulate that amyloidogenic sequences are natural targets for structural mimicry, for instance in host-microbe interactions. Microbial amyloid research could ultimately be used to fight aggressive infections and possibly processes leading to autoimmune and neurodegenerative diseases.
Insights
Microbial amyloids, protein fibrils from microbes, have diverse roles in host interactions and disease. Their structures are key to understanding and developing new antimicrobial and antivirulence agents.
Area of Science:
- Microbiology
- Biochemistry
- Structural Biology
Background:
- Microbial pathogens and microbiomes produce secreted amyloids with roles in virulence and host interactions.
- Human amyloids are linked to neurodegenerative diseases, but interspecies amyloid interactions may also be significant.
- Amyloid structures show connections to antimicrobial activity and neuroimmune functions.
Purpose of the Study:
- To explore the structural diversity and functional significance of microbial and antimicrobial amyloids.
- To compare microbial amyloids with human amyloids and identify novel therapeutic targets.
- To investigate the potential of amyloidogenic sequences in host-microbe interactions and disease.
Main Methods:
- Analysis of emerging high-resolution structures of microbial and antimicrobial amyloids.
- Comparison of structural features between microbial and human amyloids.
- Postulation of amyloidogenic sequences as targets for structural mimicry.
Main Results:
- Recent structures reveal similarities and differences between microbial and human amyloids.
- Microbial amyloids exhibit diverse activities, distinct from typical amyloid motifs.
- Structural insights support the role of amyloids in host-microbe interactions.
Conclusions:
- Microbial amyloid structures are crucial for understanding their diverse functions.
- Research into microbial amyloids can lead to novel antivirulence and antimicrobial agents.
- Targeting microbial amyloids may offer therapeutic strategies for infections and diseases.
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