Related Experiment Video

Updated: Jun 1, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
08:12

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel β-sheet structure

Abbi Engel1, Frank Shewmaker, Herman K Edskes

  • 1Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830, USA.

Biochemistry
|June 4, 2011
PubMed

Insights

The prion domain of Candida albicans Ure2p forms infectious amyloid in yeast, unlike Candida glabrata Ure2p. This amyloid structure transmits the prion state, [URE3alb], to yeast cells expressing only C. albicans Ure2p.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Mycology

Background:

  • Prions are infectious proteins that can propagate their misfolded state.
  • Ure2p is a protein in yeast that can form prions.
  • The prion-forming ability of Ure2p varies between yeast species.

Purpose of the Study:

  • To investigate why Ure2p from Candida albicans forms prions in Saccharomyces cerevisiae, while Ure2p from Candida glabrata does not.
  • To characterize the structural basis of prion formation and infectivity for Candida albicans Ure2p.

Main Methods:

  • Comparative analysis of Ure2p N-terminal domains from different Candida species.
  • Amyloid formation assays.
  • Prion infectivity transmission experiments in Saccharomyces cerevisiae.
  • Solid-state nuclear magnetic resonance (ssNMR) spectroscopy of selectively labeled Ure2p fragments.

Main Results:

  • The N-terminal prion domain of Candida albicans Ure2p forms infectious amyloid structures.
  • This amyloid structure is capable of transmitting the [URE3alb] prion state to Saccharomyces cerevisiae.
  • The infectious amyloid exhibits an in-register parallel β-sheet structure, similar to other known yeast prions.
  • The N-terminal domain of Candida glabrata Ure2p does not readily form amyloid, and any formed amyloid is not infectious.

Conclusions:

  • The N-terminal prion domain of Candida albicans Ure2p possesses the intrinsic ability to form infectious amyloids.
  • Structural differences in the N-terminal domains dictate the prion-forming capacity and infectivity of Ure2p across different yeast species.
  • The in-register parallel β-sheet structure is crucial for the infectivity of Ure2p prions.

More Related Videos

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis10:03

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

Published on: July 16, 2008

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

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

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...
Candidiasis01:20

Candidiasis

Candidiasis is a fungal infection caused by opportunistic species of Candida. It can affect various anatomical sites, including the skin, oral cavity, nails, and genitourinary tract. Among its forms, vaginal candidiasis is the most common type of mucosal infection. It typically results from the overgrowth of Candida albicans in the vaginal mucosa. Under normal conditions, C. albicans exists as a commensal organism within the vaginal microbiota, regulated by the dominance of lactobacilli, which...
Subviral Agents01:29

Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
Antifungal Agents01:15

Antifungal Agents

Amphotericin B is a broad-spectrum antifungal agent that exploits structural differences between fungal and mammalian cell membranes. Its amphipathic structure—featuring a hydrophobic polyene-lactone ring and a hydrophilic region containing mycosamine and carboxylic acid groups—enables selective binding to ergosterol, a sterol predominantly found in fungal plasma membranes. This selective interaction underlies the drug’s antifungal activity, although weak binding to cholesterol contributes to...