Prion sequence polymorphisms and chronic wasting disease resistance in Illinois white-tailed deer (Odocoileus virginianus)

References

• Belay ED, Maddox RA, Williams ES, Miller MW, Gambetti P, Schonberger LB. Chronic wasting disease and potential transmission to humans. Emerging Infectious Diseases 2004; 10:977 - 984
   PubMed Web of Science ®Google Scholar
• Baeten LA, Powers BE, Jewell JE, Spraker TR, Miller MW. A natural case of chronic wasting disease in a free-ranging moose (alces alces shirasi). J Wildl Dis 2007; 43:309 - 314
   PubMed Web of Science ®Google Scholar
• Miller MW, Williams ES. Prion disease: Horizontal prion transmission in mule deer. Nature 2003; 425:35 - 36
   PubMed Web of Science ®Google Scholar
• Williams ES, Young S. Spongiform encephalopathy of rocky mountain elk. J Wildl Dis 1982; 18:465 - 471
   PubMed Web of Science ®Google Scholar
• Mathiason CK, Powers JG, Dahmes SJ, Osborn DA, Miller KV, Warren RJ, Mason GL, Hays SA, Hayes-Klug J, Seelig DM, Wild MA, Wolfe LL, Spraker TR, Miller MW, Sigurdson CJ, Telling GC, Hoover EA. Infectious prions in the saliva and blood of deer with chronic wasting disease. Science 2006; 314:133 - 136
   PubMed Web of Science ®Google Scholar
• Sigurdson CJ, Aguzzi A. Chronic wasting disease. BBA-Molecular Basis of Disease 2007; 1772:610 - 618
   PubMed Web of Science ®Google Scholar
• Joly DO, Ribic CA, Langenberg JA, Beheler K, Batha CA, Dhuey BJ, Rolley RE, Bartelt G, Van Deelen TR, Samuel MD. Chronic wasting disease in free-ranging wisconsin whitetailed deer. Emer Infect Dis 2003; 9:599 - 601
   PubMed Web of Science ®Google Scholar
• Illinois Department of Natural Resources. WD information 2007; 2007:1
   Google Scholar
• Novakofski J, Brewer MS, Mateus-Pinilla N, Killefer J, McCusker RH. Prion biology relevant to bovine spongiform encephalopathy. J Anim Sci 2005; 83:1455 - 1476
   PubMed Web of Science ®Google Scholar
• O'Rourke KI, Spraker TR, Hamburg LK, Besser TE, Brayton KA, Knowles DP. Polymorphisms in the prion precursor functional gene but not the pseudogene are associated with susceptibility to chronic wasting disease in white-tailed deer. J Gen Virol 2004; 85:1339 - 1346
   PubMed Web of Science ®Google Scholar
• Johnson C, Johnson J, Clayton M, McKenzie D, Aiken J. Prion protein gene heterogeneity in free-ranging white-tailed deer within the chronic wasting disease affected region of wisconsin. J Wildl Dis 2003; 39:576 - 581
   PubMed Web of Science ®Google Scholar
• Johnson C, Johnson J, Vanderloo JP, Keane D, Aiken JM, McKenzie D. Prion protein polymorphisms in white-tailed deer influence susceptibility to chronic wasting disease. J Gen Virol 2006; 87:2109 - 2114
   PubMed Web of Science ®Google Scholar
• Jewell JE, Conner MM, Wolfe LL, Miller MW, Williams ES. Low frequency of PrP genotype 225SF among free-ranging mule deer (odocoileus hemionus) with chronic wasting disease. J Gen Virol 2005; 86:2127 - 2134
   PubMed Web of Science ®Google Scholar
• Raymond G, Bossers A, Raymond L, O'Rourke K, McHolland L, Bryant P III, Miller M, Williams E, Smits M, Caughey B. Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting disease. EMBO J 2000; 19:4425 - 4430
   PubMed Web of Science ®Google Scholar
• Brayton KA, O'Rourke KI, Lyda AK, Miller MW, Knowles DP. A processed pseudogene contributes to apparent mule deer prion gene heterogeneity. Gene 2004; 326:167 - 173
   PubMed Web of Science ®Google Scholar
• Heaton MP, Leymaster KA, Freking BA, Hawk DA, Smith TP, Keele JW, Snelling WM, Fox JM, Chitko-McKown CG, Laegreid WW. Prion gene sequence variation within diverse groups of U.S. sheep, beef cattle and deer. Mamm Genome 2003; 14:765 - 777
   PubMed Web of Science ®Google Scholar
• Miller MW, Conner MM. Epidemiology of chronic wasting disease in free-ranging mule deer: Spatial, temporal and demographic influences on observed prevalence patterns. J Wildl Dis 2005; 41:275 - 290
   PubMed Web of Science ®Google Scholar
• Brinkman TJ, Deperno CS, Jenks JA, Haroldson BS, Osborn RG. Movement of female white-tailed deer: Effects of climate and intensive row-crop agriculture. J Wildl Manage 2005; 69:1099 - 1111
   Web of Science ®Google Scholar
• Nixon CM, Mankin PC, Etter DR, Hansen LP, Brewer PA, Chelsvig JE, Esker TL, Sullivan JB. White-tailed deer dispersal behavior in an agricultural environment. The American Midland Naturalist 2007; 157:212 - 220
   Web of Science ®Google Scholar
• Roseberry JL, Woolf A. Habitat-population density relationships for white-tailed deer in illinois. Wildl Soc Bull 1998; 26:252 - 258
   Web of Science ®Google Scholar
• Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 1988; 16:10881 - 10890
   PubMed Web of Science ®Google Scholar
• Peakall R, Smouse PE. Genalex 6: Genetic analysis in excel. population genetic software for teaching and research. Molecular Ecology Notes 2006; 6:288 - 295
   Web of Science ®Google Scholar
• North BV, Curtis D, Sham PC. Application of logistic regression to case-control association studies involving two causative loci. Hum Hered 2005; 59:79 - 87
   PubMed Web of Science ®Google Scholar
• Allison PD. Logistic Regression Using the SAS® System: Theory and Application 1999; SAS Institute Inc
   Google Scholar
• Stephens M, Smith NJ, Donnelly P. A new statistical method for haplotype reconstruction from population data. The American Journal of Human Genetics 2001; 68:978 - 989
   PubMed Web of Science ®Google Scholar
• Stephens M, Donnelly P. A comparison of bayesian methods for haplotype reconstruction from population genotype data. Am J Hum Genet 2003; 73:1162 - 1169
   PubMed Web of Science ®Google Scholar
• Baylis M, Goldmann W. The genetics of scrapie in sheep and goats. Curr Mol Med 2004; 4:385 - 396
   PubMed Web of Science ®Google Scholar
• Roden JA, Nieuwhof GJ, Bishop SC, Jones DA, Haresign W, Gubbins S. Breeding programmes for TSE resistance in british sheep I. assessing the impact on prion protein (PrP) genotype frequencies. Prev Vet Med 2006; 73:1 - 16
   PubMed Web of Science ®Google Scholar
• Gubbins S, Roden JA. Breeding programmes for TSE resistance in british sheep II. assessing the impact on the prevalence and incidence of scrapie. Prev Vet Med 2006; 73:17 - 31
   PubMed Web of Science ®Google Scholar
• Meade-White K, Race B, Trifilo M, Bossers A, Favara C, Lacasse R, Miller M, Williams E, Oldstone M, Race R, Chesebro B. Resistance to chronic wasting disease in transgenic mice expressing a naturally occurring allelic variant of deer prion protein. J Virol 2007; 81:4533 - 4539
   PubMed Web of Science ®Google Scholar
• Coulon A, Cosson JF, Angibault JM, Cargnelutti B, Galan M, Morellet N, Petit E, Aulagnier S, Hewison AJ. Landscape connectivity influences gene flow in a roe deer population inhabiting a fragmented landscape: An individual-based approach. Mol Ecol 2004; 13:2841 - 2850
   PubMed Web of Science ®Google Scholar
• John TJ, Samuel R. Herd immunity and herd effect: New insights and definitions. Eur J Epidemiol 2000; 16:601 - 606
   PubMed Web of Science ®Google Scholar
• Safar J, Wang W, Padgett MP, Ceroni M, Piccardo P, Zopf D, Gajdusek DC, Gibbs CJ. Molecular mass, biochemical composition and physicochemical behavior of the infectious form of the scrapie precursor protein monomer. Proceedings of the National Academy of Sciences 1990; 87:6373 - 6377
   PubMed Web of Science ®Google Scholar
• Wells MA, Jackson GS, Jones S, Hosszu LL, Craven CJ, Clarke AR, Collinge J, Waltho JP. A reassessment of copper(II) binding in the full-length prion protein. Biochem J 2006; 399:435 - 444
   PubMed Web of Science ®Google Scholar
• Millhauser GL. Copper and the prion protein: Methods, structures, function and disease. Annu Rev Phys Chem 2007; 58:299 - 320
   PubMed Web of Science ®Google Scholar
• Sigurdsson EM, Brown DR, Alim MA, Scholtzova H, Carp R, Meeker HC, Prelli F, Frangione B, Wisniewski T. Copper chelation delays the onset of prion disease. J Biol Chem 2003; 278:46199 - 46202
   PubMed Web of Science ®Google Scholar
• Hijazi N, Shaked Y, Rosenmann H, Ben-Hur T, Gabizon R. Copper binding to PrPC may inhibit prion disease propagation. Brain Res 2003; 993:192 - 200
   PubMed Web of Science ®Google Scholar
• Beck JA, Mead S, Campbell TA, Dickinson A, Wientjens D, Croes EA, Van Duijn CM, Collinge J. Two-octapeptide repeat deletion of prion protein associated with rapidly progressive dementia. Neurology 2001; 57:354 - 356
   PubMed Web of Science ®Google Scholar
• Capellari S, Parchi P, Wolff BD, Campbell J, Atkinson R, Posey DM, Petersen RB, Gambetti P. Creutzfeldt-jakob disease associated with a deletion of two repeats in the prion protein gene. Neurology 2002; 59:1628 - 1630
   PubMed Web of Science ®Google Scholar
• Owen F, Poulter M, Lofthouse R, Collinge J, Crow TJ, Risby D, Baker HF, Ridley RM, Hsiao K, Prusiner SB. Insertion in prion protein gene in familial creutzfeldt-jakob disease. Lancet 1989; 1:51 - 52
   PubMed Web of Science ®Google Scholar
• Castilla J, Gutierrez-Adan A, Brun A, Pintado B, Parra B, Ramirez MA, Salguero FJ, Diaz San Segundo F, Rabano A, Cano MJ, Torres JM. Different behavior toward bovine spongiform encephalopathy infection of bovine prion protein transgenic mice with one extra repeat octapeptide insert mutation. J Neurosci 2004; 24:2156 - 2164
   PubMed Web of Science ®Google Scholar
• Bocharova OV, Breydo L, Salnikov VV, Baskakov IV. Copper(II) inhibits in vitro conversion of prion protein into amyloid fibrils. Biochemistry 2005; 44:6776 - 6787
   PubMed Web of Science ®Google Scholar
• Kuczius T, Buschmann A, WenLan Z, Karch H, Becker K, Peters G, Groschup MH. Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding. Biol Chem 2004; 385:739 - 747
   PubMed Web of Science ®Google Scholar
• Nishina K, Jenks S, Supattapone S. Ionic strength and transition metals control PrPSc protease resistance and conversion-inducing activity. J Biol Chem 2004; 279:40788 - 40794
   PubMed Web of Science ®Google Scholar
• Jackson GS, Murray I, Hosszu LLP, Gibbs N, Waltho JP, Clarke AR, Collinge J. Location and properties of metal-binding sites on the human prion protein. Proceedings of the National Academy of Sciences 2001; 98:8531 - 8535
   PubMed Web of Science ®Google Scholar
• Burns CS, Aronoff-Spencer E, Legname G, Prusiner SB, Antholine WE, Gerfen GJ, Peisach J, Millhauser GL. Copper coordination in the full-length, recombinant prion protein. Biochemistry 2003; 42:6794 - 6803
   PubMed Web of Science ®Google Scholar
• Xie Z, O'Rourke KI, Dong Z, Jenny AL, Langenberg JA, Belay ED, Schonberger LB, Petersen RB, Zou W, Kong Q, Gambetti P, Chen SG. Chronic wasting disease of elk and deer and creutzfeldt-jakob disease: comparative analysis of the scrapie prion protein. J Biol Chem 2006; 281:4199 - 4206
   PubMed Web of Science ®Google Scholar
• Parchi P, Zou W, Wang W, Brown P, Capellari S, Ghetti B, Kopp N, Schultz-Schaeffer WJ, Kretzschmar HA, Head MW, Ironside JW, Gambetti P, Chen SG. Genetic influence on the structural variations of the abnormal prion protein. Proceedings of the National Academy of Sciences 2000; 97:10168 - 10172
   PubMed Web of Science ®Google Scholar
• O'Rourke KI, Spraker TR, Zhuang D, Greenlee JJ, Gidlewski TE, Hamir AN. Elk with a long incubation prion disease phenotype have a unique prpd profile. Neuroreport 2007; 18:1935 - 1938
   PubMed Web of Science ®Google Scholar
• Saunders GC, Cawthraw S, Mountjoy SJ, Hope J, Windl O. PrP genotypes of atypical scrapie cases in great britain. J Gen Virol 2006; 87:3141 - 3149
   PubMed Web of Science ®Google Scholar
• Balbus N, Humeny A, Kashkevich K, Henz I, Fischer C, Becker CM, Schiebel K. DNA polymorphisms of the prion doppel gene region in four different german cattle breeds and cows tested positive for bovine spongiform encephalopathy. Mamm Genome 2005; 16:884 - 892
   PubMed Web of Science ®Google Scholar
• Badaoui B, Serradilla JM, Tomas A, Urrutia B, Ares JL, Carrizosa J, Sanchez A, Jordana J, Amills M. Goat acetyl-coenzyme A carboxylase alpha: Molecular characterization, polymorphism and association with milk traits. J Dairy Sci 2007; 90:1039 - 1043
   PubMed Web of Science ®Google Scholar
• Deleault NR, Lucassen RW, Supattapone S. RNA molecules stimulate prion protein conversion. Nature 2003; 425:717 - 720
   PubMed Web of Science ®Google Scholar
• Wang D, Sadee W. Searching for polymorphisms that affect gene expression and mRNA processing: Example ABCB1 (MDR1). AAPS J 2006; 8:515 - 520
   PubMed Web of Science ®Google Scholar
• Kimchi-Sarfaty C, Oh JM, Kim IW, Sauna ZE, Calcagno AM, Ambudkar SV, Gottesman MM. A “silent” polymorphism in the MDR1 gene changes substrate specificity. Science 2007; 315:525 - 528
   PubMed Web of Science ®Google Scholar
• Sander P, Hamann H, Pfeiffer I, Wemheuer W, Brenig B, Groschup MH, Ziegler U, Distl O, Leeb T. Analysis of sequence variability of the bovine prion protein gene (PRNP) in german cattle breeds. Neurogenetics 2004; 5:19 - 25
   PubMed Web of Science ®Google Scholar
• Haase B, Doherr MG, Seuberlich T, Drogemuller C, Dolf G, Nicken P, Schiebel K, Ziegler U, Groschup MH, Zurbriggen A, Leeb T. PRNP promoter polymorphisms are associated with BSE susceptibility in swiss and german cattle. BMC Genet 2007; 8:15
   PubMed Web of Science ®Google Scholar
• Sander P, Hamann H, Drogemuller C, Kashkevich K, Schiebel K, Leeb T. Bovine prion protein gene (PRNP) promoter polymorphisms modulate PRNP expression and may be responsible for differences in bovine spongiform encephalopathy susceptibility. J Biol Chem 2005; 280:37408 - 37814
   PubMed Web of Science ®Google Scholar
• Juling K, Schwarzenbacher H, Williams JL, Fries R. A major genetic component of BSE susceptibility. BMC Biol 2006; 4:33
   PubMed Web of Science ®Google Scholar
• Johnson CJ, Phillips KE, Schramm PT, McKenzie D, Aiken JM, Pedersen JA. Prions adhere to soil minerals and remain infectious. PLoS Pathog 2006; 2:32
   PubMed Web of Science ®Google Scholar