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Dong wu xue yan jiu = Zoological research2014; 35(5); 436-445; doi: 10.13918/j.issn.2095-8137.2014.5.436

Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies.

Abstract: Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group of fatal neurodegenerative diseases detected in a wide range of mammalian species. The "protein-only" hypothesis of TSE suggests that prions are transmissible particles devoid of nucleic acid and the primary pathogenic event is thought to be the conversion of cellular prion protein (PrP(C)) into the disease-associated isoform (PrP(Sc)). According to susceptibility to TSEs, animals can be classified into susceptible species and low susceptibility species. In this review we focus on several species with low susceptibility to TSEs: dogs, rabbits, horses and buffaloes. We summarize recent studies into the characteristics of low susceptibility regarding protein structure, and biochemical and genetic properties.
Publication Date: 2014-10-10 PubMed ID: 25297084PubMed Central: PMC4790361DOI: 10.13918/j.issn.2095-8137.2014.5.436Google 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 article focuses on the analysis of transmissible spongiform encephalopathies (TSEs), fatal neurodegenerative diseases in various mammalian species, with detailed exploration on species with low susceptibility like dogs, rabbits, horses, and buffaloes. It reviews recent studies regarding their protein structure, genetic characteristics, and biochemical properties that contribute to lower vulnerability against TSEs.

Understanding Transmissible Spongiform Encephalopathies (TSEs)

  • TSEs, more commonly known as prion diseases, are fatal neurodegenerative diseases prevalent in several mammalian species.
  • The study gives reference to the “protein-only” hypothesis which suggests that prions, the causative agents of TSEs, are transmissible particles devoid of nucleic acid.
  • The primary pathogenic event in these diseases is thought to be the transformation of cellular prion protein (PrP(C)) into a disease-associated isoform (PrP(Sc)).

Susceptibility and Classification of Species

  • Species can be broadly classified into two categories based on their susceptibility to TSEs: susceptible species and species with low susceptibility.
  • The paper primarily focuses on animals with low susceptibility to TSEs such as dogs, rabbits, horses, and buffaloes.
  • The idea behind focusing on these species is to understand the reasons for their low vulnerability to TSEs which may provide insight into potential prevention or treatment methodologies.

Investigating Characteristics of Low Susceptibility

  • The research article presents a comprehensive review of recent studies that have examined the characteristics relative to the low susceptibility.
  • These aspects include protein structure, biochemical properties, and genetic characteristics.
  • The details of how these factors contribute to resistance against TSEs in these animals and whether these aspects are exclusive or common across species forms the crux of the research.

Implications and Future Directions

  • The understanding gained from studying low susceptibility species might unlock potential avenues for treating or preventing TSEs in high susceptibility species.
  • Further research will be required to validate these findings across other species and to explore how these mechanisms can be harnessed for the benefit of species highly susceptible to TSEs.

Cite This Article

APA
Qing LL, Zhao H, Liu LL. (2014). Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies. Dongwuxue Yanjiu, 35(5), 436-445. https://doi.org/10.13918/j.issn.2095-8137.2014.5.436

Publication

ISSN: 0254-5853
NlmUniqueID: 100961499
Country: China
Language: English
Volume: 35
Issue: 5
Pages: 436-445

Researcher Affiliations

Qing, Li-Li
  • Laboratory of Conservation and Utilization of Bio-resources, Yunnan University, Kunming 650091, China.
Zhao, Hui
  • Laboratory of Conservation and Utilization of Bio-resources, Yunnan University, Kunming 650091, China. zhaohui@ynu.edu.cn.
Liu, Lin-Lin
  • Laboratory of Conservation and Utilization of Bio-resources, Yunnan University, Kunming 650091, China.

MeSH Terms

  • Amino Acid Sequence
  • Animals
  • Molecular Sequence Data
  • Prion Diseases / genetics
  • Prion Diseases / veterinary
  • Prions / chemistry
  • Prions / genetics
  • Prions / metabolism
  • Species Specificity

Conflict of Interest Statement

The authors have declared that no competing interests exist.

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Citations

This article has been cited 10 times.
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