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 Experiment Videos

CD4+ T cell-mediated immunity against prion proteins.

L Stoltze1, H Rezaei, G Jung

  • 1Institute for Cell Biology, Department of Immunology, University of Tübingen, Auf der Morgenstelle 15, 72076 Tübingen, Germany. l.stoltze@prion.ucl.ac.uk

Cellular and Molecular Life Sciences : CMLS
|May 10, 2003
PubMed
Summary

The prion protein (PrP) influences susceptibility to prion diseases. Differences in PrP amino acid sequences trigger CD4+ T cell responses, crucial for distinguishing foreign from self PrP and overcoming the species barrier.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Functions of unconventional myosins.

Current opinion in cell biology·2000
Same author

Two-step fast protein liquid chromatographic purification of the Serratia marcescens hemolysin and peptide mapping with mass spectrometry.

Journal of chromatography. B, Biomedical sciences and applications·2000
Same author

The porcine humoral immune response against pseudorabies virus specifically targets attachment sites on glycoprotein gC.

Journal of virology·2000
Same author

Quantitative analysis of peptide-MHC class II interaction.

Seminars in immunology·2000
Same author

Extension of HLA-A*0201-restricted minimal epitope by N epsilon-palmitoyl-lysine increases the life span of functional presentation to cytotoxic T cells.

Journal of immunology (Baltimore, Md. : 1950)·2000
Same author

Extensive post-translational modification, including serine to D-alanine conversion, in the two-component lantibiotic, lacticin 3147.

The Journal of biological chemistry·1999

Area of Science:

  • Neuroscience
  • Immunology
  • Molecular Biology

Background:

  • The prion protein (PrP(C)) is central to transmissible spongiform encephalopathies.
  • The 'protein only' hypothesis posits prions (PrP(Sc) conformer) as the infectious agent.
  • A 'species barrier' hinders prion transmission due to PrP sequence variations.

Purpose of the Study:

  • To investigate the immunological basis of the prion disease species barrier.
  • To determine how PrP sequence differences influence immune recognition.

Main Methods:

  • Analysis of prion protein (PrP) peptide presentation on major histocompatibility complex class II molecules.
  • Assessment of CD4+ T cell activation in response to foreign PrP peptides.
  • Monitoring antibody production as an indicator of immune response.

Related Experiment Videos

Main Results:

  • PrP sequence variations lead to distinct peptide presentation on MHC class II molecules.
  • These peptides activate specific CD4+ T cells.
  • This T cell activation induces an effective immune response, including antibody production against foreign PrP.

Conclusions:

  • CD4+ T cells play a critical role in distinguishing foreign from self PrP.
  • Immune responses mediated by CD4+ T cells are key to overcoming the prion species barrier.