Transgenic and Knockout Mice in Research on Prion Diseases

Brain Pathology - Tập 8 Số 4 - Trang 715-733 - 1998
Alex J. Raeber1, Sebastian Brandner1, Michael A. Klein1, Yves Benninger1, Christine Musahl1, Rico Frigg1, Christiane Roeckl1, Michael B. Fischer1, Charles Weissmann2, Adriano Aguzzi1
1Institute of Neuropathology, Department of Pathology, Schmelzbergstr. 12, University Hospital, 8091 Zürich, Switzerland
2Institute of Molecular Biology, Abteilung 1, University of Zürich, Winterthurerstr. 190, 8057 Zürich, Switzerland.

Tóm tắt

Since the discovery of the prion protein (PrP) gene more than a decade ago, transgenetic investigations on the PrP gene have shaped the field of prion biology in an unprecedented way. Many questions regarding the role of PrP in susceptibility of an organism exposed to prions have been elucidated. For example mice with a targeted disruption of the PrP gene have allowed the demonstration that an organism that lacks PrPc is resistant to infection by prions. Reconstitution of these mice with mutant PrP genes allowed investigations on the structure‐activity relationship of the PrP gene with regard to scrapie susceptibility. Unexpectedly, transgenic mice expressing PrP with specific amino‐proximal truncations spontaneously develop a neurologic syndrome presenting with ataxia and cerebellar lesions. A distinct spontaneous neurologic phenotype was observed in mice with internal deletions in PrP. Using ectopic expression of PrP in PrP knockout mice has turned out to be a valuable approach towards the identification of host cells that are capable of replicating prions. Transgenic mice have also contributed to our understanding of the molecular basis of the species barrier for prions. Finally, the availability of PrP knockout mice and transgenic mice overexpressing PrP allows selective reconstitution experiments aimed at expressing PrP in neurografts or in specific populations of hemato‐ and lymphopoietic cells. Such studies have shed new light onto the mechanisms of prion spread and disease pathogenesis.

Từ khóa


Tài liệu tham khảo

10.1038/381734a0

10.1016/S0140-6736(97)22011-8

10.1016/0966-842X(96)30012-7

10.1038/383666a0

10.1038/39758

10.1038/33812

10.1038/382779a0

10.1016/0092-8674(86)90662-8

10.1099/0022-1317-77-8-1925

10.1212/WNL.42.1.149

10.1128/JVI.68.12.7859-7868.1994

10.1038/37981

10.1126/science.6815801

10.1111/j.1750-3639.1998.tb00130.x

10.1038/379339a0

10.1073/pnas.93.23.13148

10.1038/37783

10.1038/380345a0

10.1098/rstb.1994.0036

10.1099/0022-1317-68-1-79

10.1038/39057

10.1007/BF03403528

10.1016/0092-8674(93)90360-3

10.1038/356577a0

Campbell IL, 1994, Activation of cerebral cytokine gene expression and its correlation with onset of reactive astrocyte and acute‐phase response gene expression in scrapie, J Virol, 68, 2383, 10.1128/jvi.68.4.2383-2387.1994

10.1073/pnas.91.12.5690

10.1016/0092-8674(86)90875-5

10.1016/0092-8674(90)90225-4

Caughey B, 1997, Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie‐associated prion protein in guanidine denaturation studies, J Virol, 71, 4107, 10.1128/jvi.71.5.4107-4110.1997

10.1016/S0140-6736(96)90638-8

10.1038/315331a0

10.1006/neur.1995.0025

10.1016/S0140-6736(96)01310-4

10.1038/383685a0

10.1038/370295a0

10.1016/S0896-6273(00)80424-9

10.1007/BF00266934

10.1016/0021-9975(68)90005-4

Dickinson AG, 1988, Genetic aspects of unconventional virus infections: the basis of the virino hypothesis, Ciba Found Symp, 135, 63

10.1073/pnas.88.2.375

10.1073/pnas.94.25.13452

10.1056/NEJM197403212901220

10.1093/infdis/117.1.15

10.1002/j.1460-2075.1996.tb00467.x

10.1038/362543a0

Fournier JG, 1995, Ultrastructural localization of cellular prion protein (PrPC) in synaptic boutons of normal hamster hippocampus, C R Acad Sci III, 318, 339

10.1038/295149a0

10.1038/226462a0

10.1016/0378-1135(87)90084-8

10.1016/0165-5728(88)90140-3

10.1073/pnas.88.23.10926

10.1016/0014-4886(89)90095-2

10.1038/2151043a0

10.1006/nbdi.1996.0019

10.1111/j.1460-9568.1995.tb01049.x

10.1038/38925

10.1016/S0140-6736(05)62356-2

10.1016/S0140-6736(97)24002-X

10.1111/j.1432-1033.1988.tb13883.x

10.1006/bbrc.1995.1233

10.1038/338342a0

10.1126/science.1980379

10.1099/0022-1317-73-10-2751

10.1099/0022-1317-68-10-2711

10.1073/pnas.94.19.10086

10.1016/0092-8674(93)90635-4

10.1016/0022-510X(83)90165-X

10.1099/0022-1317-39-3-487

10.1016/0021-9975(78)90059-2

10.1099/0022-1317-51-1-183

10.1099/0022-1317-67-2-255

10.1016/0168-1702(89)90040-3

10.1016/0168-1702(89)90039-7

10.1099/0022-1317-70-8-2017

10.1111/j.1749-6632.1994.tb38911.x

10.1128/JVI.65.11.6292-6295.1991

10.1038/37789

10.1038/36337

10.1016/0140-6736(91)92826-N

Kretzschmar HA, 1986, Scrapie prion proteins are synthesized in neurons, Am J Pathol, 122, 1

Lasmezas CI, 1996, Immune system‐dependent and ‐independent replication of the scrapie agent, J Virol, 10, 1292, 10.1128/jvi.70.2.1292-1295.1996

10.1038/381743a0

10.1073/pnas.93.6.2403

Manson J, 1992, The prion protein gene: a role in mouse embryogenesis, Development, 115, 117, 10.1242/dev.115.1.117

10.1007/BF02780662

Manson JC, 1994, PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology, Neurodegeneration, 3, 331

10.1006/neur.1995.0014

10.1038/nm1297-1376

10.1016/0092-8674(83)90207-6

10.1038/ng0298-118

10.1093/molehr/3.6.529

10.1038/nbt0995-999

10.1016/0896-6273(95)90307-0

10.1038/nm0797-750

10.1128/jvi.67.11.6808-6810.1993

10.1016/0092-8674(85)90333-2

10.1002/ana.410390613

Pattison IH, 1966, The relative susceptibility of sheep, goats and mice to two types of the goat scrapie agent, Res Vet Sci, 7, 207, 10.1016/S0034-5288(18)34700-3

10.1016/S0368-1742(61)80013-1

10.1006/jmbi.1997.1328

10.1126/science.6801762

10.1146/annurev.mi.43.100189.002021

10.1126/science.1675487

10.1073/pnas.91.11.4611

10.1126/science.278.5336.245

10.1073/pnas.90.22.10608

10.1016/0092-8674(83)90168-X

10.1016/0092-8674(90)90134-Z

10.1038/33834

10.1016/0896-6273(95)90105-1

Raeber A, 1996, Prion propagation in PrP null mice with ectopic PrP expression, Experientia, 52, A44

10.1097/00001504-199805000-00011

10.1093/emboj/16.20.6057

10.1038/nm1297-1383

10.1038/382180a0

10.1016/S0014-5793(97)00920-4

10.1073/pnas.90.8.3182

10.1016/0092-8674(94)90436-7

10.1038/380528a0

Sakaguchi S, 1995, Accumulation of proteinase K‐resistant prion protein (PrP) is restricted by the expression level of normal PrP in mice inoculated with a mouse‐adapted strain of the Creutzfeldt‐Jakob disease agent, J Virol, 69, 7586, 10.1128/jvi.69.12.7586-7592.1995

10.1006/jmbi.1994.0030

10.1016/0378-1135(93)90055-C

10.1016/0092-8674(89)90608-9

10.1016/0092-8674(93)90275-U

10.1128/JVI.71.12.9032-9044.1997

10.1002/pro.5560010804

10.1073/pnas.94.26.14279

ShmerlingD FischerM BlättlerT HegyiI BrandnerS AguzziA WeissmannC(1997)Expression in mice of amino‐proximally truncated but not of full‐length PrP causes a cerebellar syndrome. In :29th Meeting of the Union of Swiss Societies for Experimental Biology Geneva Switzerland ppA46.

10.1016/S0092-8674(00)81572-X

10.1038/386564a0

10.1016/0092-8674(87)90150-4

10.1101/gad.10.14.1736

10.1126/science.274.5295.2079

10.1073/pnas.91.21.9936

10.1016/0092-8674(95)90236-8

10.1038/380639a0

10.1038/352679a0

10.1016/0014-5793(96)00610-2

10.1136/vr.121.18.419

10.1016/0092-8674(94)90177-5

10.1016/0092-8674(87)90134-6

10.1016/0896-6273(91)90074-A

10.1038/ng0295-197

10.1136/vr.130.5.90

10.1016/S0140-6736(96)91412-9

10.1097/00005072-198311000-00002

10.1006/nbdi.1997.0130