Structural Mimicry in Microbial and Antimicrobial Amyloids

Nimrod Golan1, Yizhaq Engelberg1, Meytal Landau1,2

  • 1Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel;

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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