The First Genetic Characterization of the <i>SPRN</i> Gene in Pekin Ducks (<i>Anas platyrhynchos domesticus</i>)
Thi-Thuy-Duong Nguyen | Mohammed Zayed | Yong-Chan Kim | Byung-Hoon Jeong
Prion diseases are fatal neurodegenerative disorders characterized by an accumulation of misfolded prion protein (PrP<sup>Sc</sup>) in brain tissues. The shadow of prion protein (Sho) encoded by the shadow of prion protein gene (<i>SPRN</i>) is involved in prion disease progress. The interaction between Sho and PrP accelerates the PrP<sup>Sc</sup> conversion rate while the <i>SPRN</i> gene polymorphisms have been associated with prion disease susceptibility in several species. Until now, the <i>SPRN</i> gene has not been investigated in ducks. We identified the duck <i>SPRN</i> gene sequence and investigated the genetic polymorphisms of 184 Pekin ducks. We compared the duck <i>SPRN</i> nucleotide sequence and the duck Sho protein amino acid sequence with those of several other species. Finally, we predicted the duck Sho protein structure and the effects of non-synonymous single nucleotide polymorphisms (SNPs) using computational programs. We were the first to report the Pekin duck <i>SPRN</i> gene sequence. The duck Sho protein sequence showed 100% identity compared with the chicken Sho protein sequence. We found 27 novel SNPs in the duck <i>SPRN</i> gene. Four amino acid substitutions were predicted to affect the hydrogen bond distribution in the duck Sho protein structure. Although MutPred2 and SNPs&GO predicted that all non-synonymous polymorphisms were neutral or benign, SIFT predicted that four variants, A22T, G49D, A68T, and M105I, were deleterious. To the best of our knowledge, this is the first report about the genetic and structural characteristics of the duck <i>SPRN</i> gene.
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