Prion protein gene polymorphisms in natural goat scrapie

A total of 51 goats, including seven clinical cases, from the first herd in Greece reported to have scrapie was examined to discern an association between scrapie susceptibility and polymorphisms of the gene encoding the prion protein (PrP). Each animal was evaluated for clinical signs of the disease, histopathological lesions associated with scrapie, the presence of detectable protease-resistant PrP in the brain and PrP genotype. Eleven different PrP genotypes encoding at least five unique predicted mature PrP amino acid sequences were found. These genotypes included the amino acid polymorphisms at codons 143 (H→R) and 240 (S→P) and ‘silent’ nucleotide alterations at codons 42 (a→g) and 138 (c→t). Additionally, novel caprine amino acid polymorphisms were detected at codons 21 (V→A), 23 (L→P), 49 (G→S), 154 (R→H), 168 (P→Q) and 220 (Q→H) and new silent mutations were found at codons 107 (g→a) and 207 (g→a). The following variants were found in scrapie-affected goats: VV21, LL23, GG49, SS49, HH143, HR143, RR154, PP168, PP240, SP240 and SS240. All scrapie-affected animals carried the HH143RR154 genotype, with the exception of two goats (HR143), both of which had detectable protease-resistant PrP but showed no clinical signs or histopathological lesions characteristic of scrapie.

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No polymorphisms in the coding region of the prion-like protein gene in Thoroughbred racehorses

Acta Veterinaria Hungarica ◽

10.1556/004.2019.019 ◽

2019 ◽

Vol 67 (2) ◽

pp. 174-182 ◽

Cited By ~ 4

Author(s):

Min-Ju Jeong ◽

Byung-Hoon Jeong

Keyword(s):

Amino Acid ◽

Prion Protein ◽

Protein Gene ◽

Prion Diseases ◽

Amino Acid Sequences ◽

Prion Protein Gene ◽

Coding Region ◽

Thoroughbred Racehorses ◽

Thoroughbred Horses ◽

Protein Isoform

Prion diseases are fatal neurodegenerative diseases characterised by the accumulation of an abnormal prion protein isoform (PrPSc), which is converted from the normal prion protein (PrPC). Prion diseases have been reported in an extensive number of species but not in horses up to now; therefore, horses are known to be a species resistant to prion diseases. The prion-like protein gene (PRND) is closely located downstream of the prion protein gene (PRNP) and the prion-like protein (Doppel) is a homologue with PrP. Previous studies have shown that an association between prion diseases and polymorphisms of the PRND gene is reported in the main hosts of prion diseases. Hence, we examined the genetic variations of the PRND gene in Thoroughbred horses. Interestingly, polymorphisms of the PRND gene were not detected. In addition, we conducted a comparative analysis of the amino acid sequences of the PRND gene to identify the differences between horses and other species. The amino acid sequence of the horse PRND gene showed the highest identity to that of sheep (83.7%), followed by that of goats, cattle and humans. To the best of our knowledge, this is the first genetic study of the PRND gene in horses.

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