Prions, proteinase K and infectivity

References

• Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136 - 44; http://dx.doi.org/10.1126/science.6801762; PMID: 6801762
   PubMed Web of Science ®Google Scholar
• Sandberg MK, Al-Doujaily H, Sharps B, Clarke AR, Collinge J. Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature 2011; 470:540 - 2; http://dx.doi.org/10.1038/nature09768; PMID: 21350487
   PubMed Web of Science ®Google Scholar
• Hill AF, Collinge J. Subclinical prion infection. Trends Microbiol 2003; 11:578 - 84; http://dx.doi.org/10.1016/j.tim.2003.10.007; PMID: 14659690
   PubMed Web of Science ®Google Scholar
• Robinson M, Cheevers WP, Burger D, Gorham JRJ. Infect Dis 1990; 161:783 - 6; http://dx.doi.org/10.1093/infdis/161.4.783
   Web of Science ®Google Scholar
• Gabizon R, McKinley MP, Prusiner SB. Properties of scrapie prion proteins in liposomes and amyloid rods. Ciba Found Symp 1988; 135:182 - 96; PMID: 2900719
   PubMedGoogle Scholar
• Wille H, Zhang GF, Baldwin MA, Cohen FE, Prusiner SB. Separation of scrapie prion infectivity from PrP amyloid polymers. J Mol Biol 1996; 259:608 - 21; http://dx.doi.org/10.1006/jmbi.1996.0343; PMID: 8683568
   PubMed Web of Science ®Google Scholar
• Prusiner SB, McKinley MP, Groth DF, Bowman KA, Mock NI, Cochran SP, et al. Scrapie agent contains a hydrophobic protein. Proc Natl Acad Sci U S A 1981; 78:6675 - 9; http://dx.doi.org/10.1073/pnas.78.11.6675; PMID: 6273882
   PubMed Web of Science ®Google Scholar
• Wang JJ, Borwornpinyo R, Odetallah N, Shih JCH. Enzymatic degradation of a prion-like protein, Sup35NM-His6. Enzyme Microb Technol 2005; 36:758 - 65; http://dx.doi.org/10.1016/j.enzmictec.2004.12.023
   Web of Science ®Google Scholar
• Safar J, Wille H, Itri V, Groth D, Serban H, Torchia M, et al. Eight prion strains have PrP(Sc) molecules with different conformations. Nat Med 1998; 4:1157 - 65; http://dx.doi.org/10.1038/2654; PMID: 9771749
   PubMed Web of Science ®Google Scholar
• Safar JG, Geschwind MD, Deering C, Didorenko S, Sattavat M, Sanchez H, et al. Diagnosis of human prion disease. Proc Natl Acad Sci U S A 2005; 102:3501 - 6; http://dx.doi.org/10.1073/pnas.0409651102; PMID: 15741275
   PubMed Web of Science ®Google Scholar
• Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, Hayes SF, et al. The most infectious prion protein particles. Nature 2005; 437:257 - 61; http://dx.doi.org/10.1038/nature03989; PMID: 16148934
   PubMed Web of Science ®Google Scholar
• Cronier S, Gros N, Tattum MH, Jackson GS, Clarke AR, Collinge J, et al. Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin. Biochem J 2008; 416:297 - 305; http://dx.doi.org/10.1042/BJ20081235; PMID: 18684106
   PubMed Web of Science ®Google Scholar
• Tzaban S, Friedlander G, Schonberger O, Horonchik L, Yedidia Y, Shaked G, et al. Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes. Biochemistry 2002; 41:12868 - 75; http://dx.doi.org/10.1021/bi025958g; PMID: 12379130
   PubMed Web of Science ®Google Scholar
• Pastrana MA, Sajnani G, Onisko B, Castilla J, Morales R, Soto C, et al. Isolation and characterization of a proteinase K-sensitive PrPSc fraction. Biochemistry 2006; 45:15710 - 7; http://dx.doi.org/10.1021/bi0615442; PMID: 17176093
   PubMed Web of Science ®Google Scholar
• Klingeborn M, Race B, Meade-White KD, Chesebro B. Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions. Proc Natl Acad Sci U S A 2011; 108:E1244 - 53; http://dx.doi.org/10.1073/pnas.1111255108; PMID: 22065744
   PubMedGoogle Scholar
• Sajnani G, Silva CJ, Ramos A, Pastrana MA, Onisko BC, Erickson ML, et al. PK-sensitive PrPSc is infectious and shares basic structural features with PK-resistant PrPSc. PLoS Pathog 2012; 3:e1002547; http://dx.doi.org/10.1371/journal.ppat.1002547
   Google Scholar
• Tixador P, Herzog L, Reine F, Jaumain E, Chapuis J, Le Dur A, et al. The physical relationship between infectivity and prion protein aggregates is strain-dependent. PLoS Pathog 2010; 6:e1000859; http://dx.doi.org/10.1371/journal.ppat.1000859; PMID: 20419156
   PubMed Web of Science ®Google Scholar
• Ladiwala AR, Lin JC, Bale SS, Marcelino-Cruz AM, Bhattacharya M, Dordick JS, et al. Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Abeta into off-pathway conformers. J Biol Chem 2010; 285:24228 - 37; http://dx.doi.org/10.1074/jbc.M110.133108; PMID: 20511235
   PubMed Web of Science ®Google Scholar
• Stathopulos PB, Scholz GA, Hwang YM, Rumfeldt JA, Lepock JR, Meiering EM. Sonication of proteins causes formation of aggregates that resemble amyloid. Protein Sci 2004; 13:3017 - 27; http://dx.doi.org/10.1110/ps.04831804; PMID: 15459333
   PubMed Web of Science ®Google Scholar
• Kuroda Y, Maeda Y, Sawa S, Shibata K, Miyamoto K, Nakagawa T. Effects of detergents on the secondary structures of prion protein peptides as studied by CD spectroscopy. J Pept Sci 2003; 9:212 - 20; http://dx.doi.org/10.1002/psc.447; PMID: 12725242
   PubMed Web of Science ®Google Scholar
• Colby DW, Giles K, Legname G, Wille H, Baskakov IV, DeArmond SJ, et al. Design and construction of diverse mammalian prion strains. Proc Natl Acad Sci U S A 2009; 106:20417 - 22; http://dx.doi.org/10.1073/pnas.0910350106; PMID: 19915150
   PubMed Web of Science ®Google Scholar