Identification of the pathological prion protein allotypes in scrapie-infected heterozygous bank voles (Clethrionomys glareolus) by high-performance liquid chromatography-mass spectrometry.
Cerebral formation of the pathological isoform of the prion protein (PrP) is a crucial molecular event in prion diseases. The bank vole (Clethrionomys glareolus) is a rodent species highly susceptible to natural scrapie. The PrP gene of bank vole is polymorphic (Met/Ile) at codon 109. Here we show that homozygous 109Met/Met voles have incubation times shorter than heterozygous 109Met/Ile voles after experimental challenge with three different scrapie isolates. An HPLC-MS/MS method was optimized and applied to investigate whether in heterozygous animals both PrP allotypes are able to undergo pathological conversion. The results demonstrate that both allotypes of the prion protein participate to pathological deposition.
Cartoni
C
C
Istituto Superiore di Sanità, Department of Food Safety and Veterinary Public Health, Viale Regina Elena 299, 00161 Rome, Italy. cartoni@iss.it
Schininà
M E
ME
Maras
B
B
Nonno
R
R
Vaccari
G
G
Di Baria
M A
MA
Conte
M
M
Liu
Q G
QG
Lu
M
M
Cardone
F
F
Windl
O
O
Pocchiari
M
M
Agrimi
U
U
D000595:Amino Acid Sequence; D000818:Animals; D003411:Arvicolinae; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D006224:Cricetinae; D013058:Mass Spectrometry / Q000379:methods; D008647:Mesocricetus; D008969:Molecular Sequence Data; D011110:Polymorphism, Genetic; D011328:Prions / Q000032:analysis* / Q000235:genetics*; D012608:Scrapie / Q000473:pathology*; D016415:Sequence Alignment
D011328:Prions