Multifunctional Amyloids in the Biology of Gram-Positive Bacteria

Author: mycolabadmin
2020-12-17
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Summary

This research explores how bacteria use special proteins called amyloids to perform various important functions. These proteins can form strong fibers that help bacteria stick together and survive in challenging environments. Understanding how these proteins work is crucial for addressing bacterial infections and developing new therapeutic strategies. Impacts on everyday life: – Helps explain how bacteria form resistant communities that can cause infections – Provides insights for developing new antibacterial treatments – Improves understanding of food contamination and preservation – Contributes to development of new biomaterials – Advances knowledge of bacterial survival in medical and industrial settings

Background

Amyloids were historically associated with misfolded proteins causing neurological disorders, but are now recognized as widely distributed functional proteins in prokaryotes and eukaryotes. They are involved in various biological processes including protection, surface interactions, and detoxification. Despite differences in amino acid sequences, amyloids share a conserved quaternary structure of cross-β strands that self-assemble into fibers through nucleation-dependent processes.

Objective

This review examines the current knowledge and latest findings of different bacterial amyloid systems, with particular emphasis on gram-positive bacteria. It explores their contribution to bacterial multicellularity, microbe-host interactions, and how cross-seeding between different bacterial amyloids can diversify their functionality in microbial biology.

Results

The review identifies and characterizes multiple functional amyloid systems in gram-positive bacteria including: chaplins and rodlins in Streptomyces coelicolor, phenol soluble modulins (PSMs) in Staphylococci, adhesin P1 and WapA in Streptococcus mutans, listeriolysin O in Listeria monocytogenes, and the TasA system in Bacillus species. Each system shows unique assembly mechanisms and specific biological functions while maintaining common amyloid characteristics.

Conclusion

Gram-positive bacteria possess diverse amyloid systems with unique protein components and polymerization processes. Beyond their structural role in biofilms, these proteins serve multiple functions in bacterial physiology and host interactions. Cross-seeding between different amyloids represents a potential mechanism for interspecies communication and community structure development. Further research is needed to fully understand the impact of these proteins on bacterial ecology.

Published in:Microorganisms,
Study Type:Review,
Source: 10.3390/microorganisms8122020