NR AVYJ
AU Richt,J.A.; Kasinathan,P.; Hamir,A.N.; Castilla,J.; Sathiyaseelan,T.; Vargas,F.; Sathiyaseelan,J.; Wu,H.; Matsushita,H.; Koster,J.; Kato,S.; Ishida,I.; Soto,C.; Robl,J.M.; Kuroiwa,Y.
TI Production of cattle lacking prion protein
QU Nature Biotechnology 2007 Jan; 25(1): 132-8
PT journal article; research support, n.i.h., extramural
AB Prion diseases are caused by propagation of misfolded forms of the normal cellular prion protein PrPc, such as PrP(BSE) in bovine spongiform encephalopathy (BSE) in cattle and PrP(CJD) in Creutzfeldt-Jakob disease (CJD) in humans. Disruption of PrPc expression in mice, a species that does not naturally contract prion diseases, results in no apparent developmental abnormalities. However, the impact of ablating PrPc function in natural host species of prion diseases is unknown. Here we report the generation and characterization of PrPc-deficient cattle produced by a sequential gene-targeting system. At over 20 months of age, the cattle are clinically, physiologically, histopathologically, immunologically and reproductively normal. Brain tissue homogenates are resistant to prion propagation in vitro as assessed by protein misfolding cyclic amplification. PrPc-deficient cattle may be a useful model for prion research and could provide industrial bovine products free of prion proteins.
MH Animals; Animals, Genetically Modified/*genetics; Cattle; *Gene Silencing; Genetic Engineering/*methods; PrPc Proteins/*genetics
AD National Animal Disease Center, Agriculture Research Services, United States Department of Agriculture, 2300 Dayton Avenue, Ames, Iowa 50010, USA. jricht@nadc.ars.usda.gov
SP englisch
PO USA