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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

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Updated: Jun 12, 2026

Methods for Detecting Cytotoxic Amyloids Following Infection of Pulmonary Endothelial Cells by Pseudomonas aeruginosa
07:27

Methods for Detecting Cytotoxic Amyloids Following Infection of Pulmonary Endothelial Cells by Pseudomonas aeruginosa

Published on: July 12, 2018

Functional amyloid in Pseudomonas.

Morten S Dueholm1, Steen V Petersen1, Mads Sønderkær1

  • 1Centre for Insoluble Protein Structures, Interdisciplinary Nanoscience Center (iNANO), Department of Molecular Biology, University of Aarhus (iNANO), 8000 Aarhus C, DenmarkDepartment of Biotechnology, Chemistry, and Environmental Engineering, Aalborg University, 9000 Aalborg, DenmarkDepartments of Medical BiochemistryMedical MicrobiologyMolecular Biology, University of Aarhus (iNANO), 8000 Aarhus C, Denmark.

Molecular Microbiology
|June 25, 2010
PubMed
Summary
This summary is machine-generated.

Researchers discovered a new functional amyloid protein, fapC, in Pseudomonas biofilms. This finding advances understanding of microbial amyloid structures and their role in biofilm architecture.

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Published on: May 22, 2018

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Amyloids are prevalent in microbial biofilms, contributing to their structure, but specific amyloid proteins remain largely uncharacterized.
  • Understanding these microbial amyloids is crucial for deciphering biofilm formation and architecture.

Purpose of the Study:

  • To identify and characterize a novel functional amyloid protein from a Pseudomonas strain.
  • To elucidate the genetic basis and structural features of this newly discovered amyloid.

Main Methods:

  • Purification and structural verification of the amyloid protein.
  • Partial sequencing (MS/MS) and whole-genome sequencing to identify the amyloid subunit gene (fapC).
  • Analysis of conserved motifs and residue importance for amyloid formation.
  • Heterologous expression of the fapA-F operon in Escherichia coli.

Main Results:

  • Discovery and purification of a novel functional amyloid protein, fapC, from a Pseudomonas fluorescens group strain.
  • Identification of the fapC gene, encoding the major amyloid fibril subunit, featuring a unique repeat motif lacking aromatic residues.
  • Demonstration that glutamine and asparagine residues are critical for amyloid formation, conserved across different amyloid types.
  • Confirmation that the fapA-F operon, including fapC, is involved in biofilm formation, as shown by heterologous expression in E. coli.

Conclusions:

  • A novel functional amyloid, fapC, has been identified in Pseudomonas, contributing to biofilm architecture.
  • The fapC amyloid structure highlights the non-essential role of aromatic residues and the importance of glutamine/asparagine residues in amyloid formation.
  • The conserved fapA-F operon plays a significant role in Pseudomonas biofilm development.