Molecular analysis of carbohydrate N-acetylgalactosamine 4-O sulfotransferase 8 (CHST8) as a candidate gene for bovine spongiform encephalopathy susceptibility.
Endogenous prion proteins (PrP) play the central role in the pathogenesis of transmissible spongiform encephalopathies. The carbohydrate N-acetylgalactosamine 4-O sulfotransferase 8 (CHST8) promotes the conversion of the cellular PrP(C) into the pathogenic PrP(d). Six sequence variants within the CHST8 gene were identified by comparative sequencing and genotyped for a sample of 623 animals comprising bovine spongiform encephalopathy (BSE)-affected and healthy control cows representing German Fleckvieh (German Simmental), German Holstein (Holstein-Friesian) and Brown Swiss. Significant differences in the allele, genotype and haplotype frequencies between BSE-affected and healthy cows indicate an association of sequence variant g.37254017G>T with the development of the disease in Brown Swiss cattle.
Morina
R
R
Institute of Veterinary Medicine, Georg-August University, Goettingen, Germany.
Knorr
C
C
Haase
B
B
Leeb
T
T
Seuberlich
T
T
Zurbriggen
A
A
Brem
G
G
Schütz
E
E
Brenig
B
B
D000818:Animals; D002417:Cattle / Q000235:genetics*; D016643:Encephalopathy, Bovine Spongiform / Q000235:genetics* / Q000378:metabolism; D020022:Genetic Predisposition to Disease; D018621:PrPC Proteins / Q000378:metabolism; D015238:Sulfotransferases / Q000235:genetics* / Q000378:metabolism; D000097811:Carbohydrate Sulfotransferases
D018621:PrPC Proteins; D015238:Sulfotransferases; D000097811:Carbohydrate Sulfotransferases