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Genetic analysis of the SPRN gene in ruminants reveals polymorphisms in the alanine-rich segment of shadoo protein

¹ Roslin Institute and R(D)SVS, University of Edinburgh, Neuropathogenesis Division, Roslin, Midlothian, UK
² National TSE Laboratory, College of Veterinary Medicine, China Agriculture University, Beijing, PR China

Correspondence
Wilfred Goldmann
wilfred.goldmann{at}roslin.ed.ac.uk

Prion diseases in ruminants, especially sheep scrapie, cannot be fully explained by PRNP genetics, suggesting the influence of a second modulator gene. The SPRN gene is a good candidate for this role. The SPRN gene encodes the shadoo protein (Sho) which has homology to the PRNP gene encoding prion protein (PrP). Murine Sho has a similar neuroprotective activity to PrP and SPRN gene variants are associated with human prion disease susceptibility. SPRN gene sequences were obtained from 14 species in the orders Artiodactyla and Rodentia. We report here the sequences of more than 20 different Sho proteins that have arisen due to single amino acid substitutions and amino acid deletions or insertions. All Sho sequences contained an alanine-rich sequence homologous to a hydrophobic region with amyloidogenic characteristics in PrP. In contrast with PrP, the Sho sequence showed variability in the number of alanine residues.

The GenBank/EMBL/DDBJ accession numbers for the sequences reported in this paper are EU559165 [GenBank] , EU559166 [GenBank] , EU595763 [GenBank] –EU595770 [GenBank] , EU596567 [GenBank] –EU596573 [GenBank] , EU605791 [GenBank] –EU605794 [GenBank] , GQ149482 [GenBank] and GQ174495 [GenBank] –GQ174500.

Two supplementary tables and a supplementary method are available with the online version of this paper.