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Home / Equine Research Bank / J Mol Biol / Horse prion protein NMR structure and comparisons with relat...
Journal of molecular biology2010; 400(2); 121-128; doi: 10.1016/j.jmb.2010.04.066

Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.

Abstract: The NMR structure of the horse (Equus caballus) cellular prion protein at 25 degrees C exhibits the typical PrP(C) [cellular form of prion protein (PrP)] global architecture, but in contrast to most other mammalian PrP(C)s, it contains a well-structured loop connecting the beta2 strand with the alpha2 helix. Comparison with designed variants of the mouse prion protein resulted in the identification of a single amino acid exchange within the loop, D167S, which correlates with the high structural order of this loop in the solution structure at 25 degrees C and is unique to the PrP sequences of equine species. The beta2-alpha2 loop and the alpha3 helix form a protein surface epitope that has been proposed to be the recognition area for a hypothetical chaperone, "protein X," which would promote conversion of PrP(C) into the disease-related scrapie form and thus mediate intermolecular interactions related to the transmission barrier for transmissible spongiform encephalopathies (TSEs) between different species. The present results are evaluated in light of recent indications from in vivo experiments that the local beta2-alpha2 loop structure affects the susceptibility of transgenic mice to TSEs and the fact that there are no reports on TSE in horses.
Copyright (c) 2010 Elsevier Ltd. All rights reserved.
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Publication Date: 2010-05-08 PubMed ID: 20460128DOI: 10.1016/j.jmb.2010.04.066Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research focuses on understanding the structure of the prion protein in horses and how it relates to the disease-causing prion forms. It specifically highlights a variant protein structure which is unique to equine species and may play a role in the species’ observed resistance to prion-related diseases.

Study on Horse Prion Protein

The study utilized nuclear magnetic resonance (NRM) to study the structure of the horse cellular prion protein at 25 degrees Celsius. This method allowed researchers to determine:

  • The horse prion protein displayed the typical cellular form of a prion protein (PrP(C)).
  • Distinct from most mammalian PrP(C)s, the horse prion protein has a well-structured loop connecting the beta2 strand with the alpha2 helix.

Comparison with Mouse Prion Protein Variants

In comparing the horse prion protein structure with designed variants of a mouse prion protein, researchers found:

  • A single amino acid exchange within the loop, labelled as D167S. This variant correlates with the high structural order of this loop in the protein structure.
  • The D167S variant is unique to prion proteins sequences of equine species. This might be a significant contributing factor to their unique immunity against prion-related diseases.

Implications for Prion Diseases

The study further discusses the role of this unique beta2-alpha2 loop in prion diseases:

  • The beta2-alpha2 loop and the alpha3 helix in the horse prion protein form a surface epitope. This surface epitope is speculated to be the recognition area for a hypothetical chaperone protein known as “protein X”.
  • Protein X is proposed to promote the conversion of PrP(C) into the disease-related scrapie form. This, in turn, mediates intermolecular interactions associated with the transmission barrier for transmissible spongiform encephalopathies (TSEs) between different species.
  • The results are consistent with recent findings suggesting that the beta2-alpha2 loop structure can influence the susceptibility of an organism to TSEs. This strengthens the understanding of prion diseases and could help in developing therapies and interventions.

Significance Regarding Prion Diseases in Horses

Contrary to the general existence of prion diseases in mammals, no TSE has been reported in horses. The structural uniqueness of the horse prion protein, as reported in this research, may provide an explanation for this remarkable resistance.

Cite This Article

APA
Pérez DR, Damberger FF, Wüthrich K. (2010). Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein. J Mol Biol, 400(2), 121-128. https://doi.org/10.1016/j.jmb.2010.04.066

Publication

Journal of molecular biology
ISSN: 1089-8638
NlmUniqueID: 2985088R
Country: Netherlands
Language: English
Volume: 400
Issue: 2
Pages: 121-128

Researcher Affiliations

Pérez, Daniel R
  • Institute of Molecular Biology and Biophysics, ETH Zurich, Schafmattstrasse 20, CH-8093 Zurich, Switzerland.
Damberger, Fred F
    Wüthrich, Kurt

      MeSH Terms

      • Amino Acid Sequence
      • Animals
      • Horses
      • Humans
      • Mice
      • Mice, Transgenic
      • Models, Molecular
      • Molecular Sequence Data
      • Nuclear Magnetic Resonance, Biomolecular
      • Prion Diseases / genetics
      • Prion Diseases / metabolism
      • Prions / chemistry
      • Prions / genetics
      • Prions / metabolism
      • Protein Isoforms / chemistry
      • Protein Isoforms / genetics
      • Protein Isoforms / metabolism
      • Protein Structure, Secondary
      • Sequence Alignment

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