Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

9.8K
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,...
9.8K
Biofilms01:29

Biofilms

266
Biofilms are complex communities of microorganisms encased in a self-produced extracellular polysaccharide matrix attached to surfaces. These microbial consortia can include single or multiple species, providing enhanced survival benefits by forming organized, multilayered structures.The formation of biofilms occurs through four key stages: attachment, colonization, development, and dispersal.During attachment, free-swimming planktonic cells adhere to a surface, often facilitated by...
266
Archaeal Cell Wall01:29

Archaeal Cell Wall

205
Archaeal cell walls are structurally and compositionally distinct from their bacterial counterparts, lacking the characteristic peptidoglycan layer found in most bacteria. Instead, archaeal cell walls exhibit remarkable diversity, utilizing materials such as pseudomurein, polysaccharides, and proteins to construct their protective outer layers. This structural flexibility is closely tied to archaea's ecological adaptability.S-Layers: The Common Archaeal Cell WallThe S-layer is the most...
205
Protein Folding01:22

Protein Folding

120.6K
Overview
120.6K
Surface Appendages of Archaea01:23

Surface Appendages of Archaea

142
Archaeal surface appendages are highly specialized structures essential for environmental adaptation, encompassing roles in adhesion, biofilm formation, and motility. Among these appendages, pili and archaella stand out for their distinct morphologies and functionalities, enabling archaea to thrive in diverse and often extreme environments.Pili: Adhesion and Biofilm FormationPili are filamentous structures assembled from pilin protein subunits, primarily contributing to adhesion and biofilm...
142
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

3.5K
Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
3.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Chronic suppression of a multidrug-resistant Pseudomonas aeruginosa in prosthetic joint infection using personalized bacteriophage treatment.

Nature communications·2026
Same author

Structural Insights into Native Intact <i>Mycobacterium abscessus</i> by Conventional and Ultrahigh-field solid-state NMR at 1.2 GHz.

bioRxiv : the preprint server for biology·2026
Same author

Structural defects in amyloid-β fibrils drive secondary nucleation.

Nature communications·2026
Same author

Structural basis of <i>Pseudomonas</i> biofilm-forming functional amyloid FapC formation.

Science advances·2025
Same author

Elucidation of Radical Degradation in Native Biofilms by EPR Sheds Light on Bacterial Resistance and Efficient DNP Solid-state NMR.

bioRxiv : the preprint server for biology·2025
Same author

Ultrasensitive Characterization of Native Bacterial Biofilms via Dynamic Nuclear Polarization-Enhanced Solid-State NMR.

Angewandte Chemie (International ed. in English)·2025

Related Experiment Video

Updated: Sep 6, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.2K

Functional amyloids from bacterial biofilms - structural properties and interaction partners.

Ümit Akbey1, Maria Andreasen2

  • 1Department of Structural Biology, School of Medicine, University of Pittsburgh Pittsburgh PA 15261 USA umitakbey@pitt.edu.

Chemical Science
|June 27, 2022
PubMed
Summary

Functional bacterial amyloids, unlike disease-related ones, form essential biofilm structures and confer antibiotic resistance. Understanding their interactions with host proteins is key to combating infections.

More Related Videos

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

859
Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
15:04

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

6.0K

Related Experiment Videos

Last Updated: Sep 6, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.2K
Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

859
Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
15:04

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

6.0K

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Protein aggregation is linked to neurodegenerative diseases like Alzheimer's and Parkinson's.
  • Functional amyloids, prevalent in bacterial biofilms, serve crucial roles in bacterial survival and antibiotic resistance.
  • Unlike disease-associated amyloids, functional amyloids assemble extracellularly and possess unique structural features.

Purpose of the Study:

  • To review the current knowledge on functional bacterial amyloids.
  • To highlight their structural characteristics and interaction partners.
  • To explore their implications in biofilm formation, antibiotic resistance, and potential links to neurodegenerative diseases.

Main Methods:

  • Literature review of studies on functional bacterial amyloids.
  • Analysis of structural features, including cross-β-sheet and cross-α-sheet folds.
  • Examination of interactions with extracellular matrix components and human proteins.

Main Results:

  • Functional amyloids have distinct structures optimized for assembly and function.
  • They interact with extracellular matrix components like lipids and polymers.
  • Emerging evidence links functional amyloids to disease-related amyloids and neurodegenerative pathologies.

Conclusions:

  • Functional amyloids are dynamic components of bacterial biofilms, not inert structures.
  • Their interactions with host components, including disease-related amyloids, are critical.
  • Understanding these interactions can lead to strategies against biofilm infections and antibiotic resistance.