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

Multi-species Conserved Sequences02:51

Multi-species Conserved Sequences

Next-generation sequencing technologies have created large genomic databases of a variety of animals and plants. Ever since the human genome project was completed, scientists studied the genome of primates, mammals, and other phylogenetically distant living beings. Such large-scale  studies have provided new insights into the evolutionary relationship between organisms.
Although the genome of each species varies greatly from each other, a few sequences are highly conserved. Such conserved DNA...
Gene Evolution - Fast or Slow?02:05

Gene Evolution - Fast or Slow?

The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
In contrast, regions which code...
Mutations in Microorganisms01:18

Mutations in Microorganisms

Mutations are heritable changes in an organism’s genome involving alterations in the base sequence of DNA or RNA. These changes can influence cellular processes and phenotypic traits, potentially transforming the unaltered wild type into a mutant form. Such changes, termed forward mutations, are pivotal in shaping the genetic diversity of organisms.RNA viruses exhibit the highest mutation rates due to the absence of robust proofreading mechanisms during genome replication. In contrast,...
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
Mismatch Repair01:36

Mismatch Repair

Overview
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...

You might also read

Related Articles

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

Sort by
Same author

Neofunctionalization underlies the evolutionary origin of sclareol biosynthesis in the mint family.

Nature communications·2026
Same author

A chromosome-level genome assembly of Vanilla planifolia uncovers the genomic architecture underlying partial endoreplication.

BMC genomics·2026
Same author

Exploring PrP<sup>C</sup> unfolding as a critical step preceding its refolding in the context of PrP<sup>Sc</sup> propagation.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

[Protein aggregation: from the prion exception to a general paradigm of neurodegeneration].

Medecine sciences : M/S·2026
Same author

Cysteine residues located within the core domain of human vitamin C transporter, hSVCT2, are essential for its structural and functional properties.

International journal of biological macromolecules·2025
Same author

The prion-family protein Doppel exerts a protective role during influenza virus infection.

Journal of immunology (Baltimore, Md. : 1950)·2025

Related Experiment Video

Updated: May 16, 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

Mammalian prions: tolerance to sequence changes-how far?

Muhammad Khalid Salamat1, Carola Munoz-Montesino, Mohammed Moudjou

  • 1INRA, UR892 Virologie Immunologie Moléculaires, Jouy-en-Josas, France.

Prion
|December 13, 2012
PubMed
Summary

Prion protein (PrP) conversion tolerates significant sequence changes, challenging existing models. Our findings suggest prion replication is not dependent on specific sequences within the protease-resistant region.

Keywords:
PrP proteininsertionmutagenesisprionprotein structure

More Related Videos

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay
11:41

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay

Published on: March 10, 2015

Related Experiment Videos

Last Updated: May 16, 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

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay
11:41

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay

Published on: March 10, 2015

Area of Science:

  • Neuroscience
  • Structural Biology
  • Molecular Biology

Background:

  • Prion diseases involve the misfolding of cellular prion protein (PrP C) into abnormal, aggregated forms (PrP Sc).
  • The molecular mechanisms and critical regions of PrP involved in this conversion process remain poorly understood.
  • Previous studies indicated minimal sequence changes can disrupt prion replication.

Purpose of the Study:

  • To investigate the tolerance of prion replication to substantial sequence modifications in the prion protein.
  • To identify regions of PrP critical for conformational conversion and prion infectivity.
  • To challenge existing structural models of PrP Sc and the concept of specific prion domains.

Main Methods:

  • Employing a reverse genetic approach, introducing amino acid insertions into the H2-H3 inter-helix loop and H2 region of PrP.
  • Generating and characterizing bona fide prions with engineered sequence alterations.
  • Assessing prion replication and infectivity following sequence modifications.

Main Results:

  • Prion replication demonstrated unexpected tolerance to insertions of up to 16 amino acids in the H2-H3 loop and octapeptide insertions in H2.
  • Substantial sequence changes in the protease-resistant part of PrP did not abolish prion infectivity.
  • The study indicates that prion conversion does not necessitate a specific sequence in the H2-H3 region.

Conclusions:

  • Prion protein conversion is remarkably robust to significant sequence alterations, particularly within the protease-resistant region.
  • The findings question the necessity of specific sequences or defined N- or C-terminal prion domains within the protease-resistant region for conversion.
  • This challenges current structural models of PrP Sc and suggests a more flexible mechanism for prion propagation.