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Prion protein gene polymorphisms in natural goat scrapie

Laboratory of Microbiology and Infectious Diseases¹, Laboratory of Pathology³ and Clinic of Productive Animal Medicine⁴, Faculty of Veterinary Medicine, Aristotle University, 54006 Thessaloniki, Greece
Laboratory of Pharmacology, Department of Pharmaceutical Sciences, Aristotle University, 54006 Thessaloniki, Greece²
University of Macedonia, Department of Business Administration, 156 Egnatia Street, 54006 Thessaloniki, Greece⁵

Author for correspondence: Theodoros Sklaviadis. Fax +30 31 997 645. e-mail sklaviad{at}auth.gr

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 (HR) and 240 (SP) and ‘silent’ nucleotide alterations at codons 42 (ag) and 138 (ct). Additionally, novel caprine amino acid polymorphisms were detected at codons 21 (VA), 23 (LP), 49 (GS), 154 (RH), 168 (PQ) and 220 (QH) and new silent mutations were found at codons 107 (ga) and 207 (ga). The following variants were found in scrapie-affected goats: VV₂₁, LL₂₃, GG_49, 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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