Abstract

BackgroundPrion diseases are zoonotic diseases with a broad infection spectrum among mammalian hosts and are caused by the misfolded prion protein (PrPSc) derived from the normal prion protein (PrPC), which encodes the prion protein gene (PRNP). Currently, although several prion disease-resistant animals have been reported, a high dose of prion agent inoculation triggers prion disease infection in these disease-resistant animals. However, in chickens, natural prion disease-infected cases have not been reported, and experimental challenges with prion agents have failed to cause infection. Unlike other prion disease-resistant animals, chickens have shown perfect resistance to prion disease thus far. Thus, investigation of the chicken PRNP gene could improve for understanding the mechanism of perfect prion-disease resistance. Here, we investigated the genetic characteristics of the open reading frame (ORF) of the chicken PRNP gene in a large sampling of various chicken breeds.ResultsWe found only tandem repeat deletion polymorphisms of the chicken PRNP ORF in the 4 chicken breeds including 106 Dekalb White, 100 Ross, 98 Ogolgye and 100 Korean native chickens. In addition, the distribution of chicken insertion/deletion polymorphisms was significantly different among the 4 chicken breeds. Finally, we found significant differences in the number of PRNP SNPs between prion disease-susceptible species and prion disease-resistant species. Notably, chickens lack SNPs in the ORF of the prion protein.ConclusionIn this study, we found that the absence of SNPs in the chicken PRNP ORF is a notable feature of animals with perfect resistant to prion disease.

Highlights

  • Prion diseases are zoonotic diseases with a broad infection spectrum among mammalian hosts and are caused by the misfolded prion protein (PrPSc) derived from the normal prion protein (PrPC), which encodes the prion protein gene (PRNP)

  • Real challenge study has not been performed to confirm the transmission of prion disease to horse, horse prion protein transgenic mouse showed the resistance to infection of several agents of prion diseases, including RML, scrapie, chronic wasting disease (CWD), transmissible mink encephalopathy (TME) and bovine spongiform encephalopathy (BSE) [27]

  • The c.268_269insC polymorphism, which was found in the Dekalb White breed, was not found in the 3 studied chicken breeds (Tables 1 and 2 and Additional file 1)

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Summary

Introduction

Prion diseases are zoonotic diseases with a broad infection spectrum among mammalian hosts and are caused by the misfolded prion protein (PrPSc) derived from the normal prion protein (PrPC), which encodes the prion protein gene (PRNP). Kim et al BMC Genomics (2019) 20:922 Among these SNPs, several prion disease-associated SNPs have been reported in prion disease-susceptible species, including humans, sheep and goats. Dog, which is known as prion disease resistant animal, showed very little polymorphisms in the PRNP ORF [26]. Horse prion protein had high structural stability and its horse specific amino acids showed the protective effect against prion disease [28, 29]. These results suggest that horse is a prion disease-resistant animal. Horse has only one SNP in the ORF of the PRNP gene [5]

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