Les agrégats amyloïdes de la protéine prion HET-s sont infectieux

Marie-Lise Maddelein

doi:10.1051/medsci/200218121187

Accès gratuit

Numéro		Med Sci (Paris) Volume 18, Numéro 12, Décembre 2002


Page(s)		1187 - 1189
Section		Le Magazine : Nouvelles
DOI		https://doi.org/10.1051/medsci/200218121187
Publié en ligne		15 décembre 2002

Wickner RB, Taylor KL, Edskes HK, Maddelein ML, Moriyama H, Roberts BT. Prions in Saccharomyces and Podospora spp.: protein base inheritance. Microbiol Mol Biol Rev 1999; 63: 844–61. [Google Scholar]
Bueler HM, Aguzzi A, Sailer A, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993; 73: 1339–47. [Google Scholar]
Caughey B. Transmissiblespongiform encephalopathies, amyloidoses and yeast prions : common threads? Nat Med 2000; 6: 751–4. [Google Scholar]
Wickner RB. Evidence for a prion analog inS. cerevisae : the [URE3] non-Mendelien genetic element as an altered URE2 protein. Science 1994; 264: 566–9. [Google Scholar]
Coustou V, Deleu C, Saupe S, Bégueret J. The protein product of the het-s heterocaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci USA 1997; 94: 9773–8. [Google Scholar]
Liautard JP, Alvarez-Martinez MT, Féraudet C, Torrent J. La protéine prion : structure, dynamique et conversion in vitro. Med Sci 2002; 18: 62–9. [Google Scholar]
Maddelein ML, Dos Reis S, Duvezin-Caubet S, Coulary-Salin B, Saupe S. Amyloid aggregates of the HET-s prion protein are infectious. Proc Natl Acad Sci USA 2002; 99: 7402–7. [Google Scholar]
Coustou-Linares V, Maddelein ML, Bégueret J, Saupe S. In vivo aggregation of the HET-s prion protein of the fungus Podospora anserina. Mol Microbiol 2001; 42: 1325–35. [Google Scholar]
Dos-Reis S, Coulary-Salin B, Forges V, Lascu I,Bégueret J, Saupe S. The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid-like fibrils. J Biol Chem 2002; 277: 5703–6. [Google Scholar]
Uptain SM, Sawinicki GJ, Caughey B, LindquistS. Strains of [PSI(+)] are distinguished by their efficiencies of prionmediated conformational conversion. EMBO J 2001; 20: 6236–45. [Google Scholar]
Speransky VV, Taylor KL, Edskes HK, Wickner RB, Steven AC. Prion filament networks in [URE3] cells of Saccharomyces cerevisiae. J Cell Sci 2001; 153: 1327–36. [Google Scholar]

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[1] Wickner RB, Taylor KL, Edskes HK, Maddelein ML, Moriyama H, Roberts BT. Prions in Saccharomyces and Podospora spp.: protein base inheritance. Microbiol Mol Biol Rev 1999; 63: 844–61. [Google Scholar]

[2] Bueler HM, Aguzzi A, Sailer A, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993; 73: 1339–47. [Google Scholar]

[3] Caughey B. Transmissiblespongiform encephalopathies, amyloidoses and yeast prions : common threads? Nat Med 2000; 6: 751–4. [Google Scholar]

[4] Wickner RB. Evidence for a prion analog inS. cerevisae : the [URE3] non-Mendelien genetic element as an altered URE2 protein. Science 1994; 264: 566–9. [Google Scholar]

[5] Coustou V, Deleu C, Saupe S, Bégueret J. The protein product of the het-s heterocaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci USA 1997; 94: 9773–8. [Google Scholar]

[6] Liautard JP, Alvarez-Martinez MT, Féraudet C, Torrent J. La protéine prion : structure, dynamique et conversion in vitro. Med Sci 2002; 18: 62–9. [Google Scholar]

[7] Maddelein ML, Dos Reis S, Duvezin-Caubet S, Coulary-Salin B, Saupe S. Amyloid aggregates of the HET-s prion protein are infectious. Proc Natl Acad Sci USA 2002; 99: 7402–7. [Google Scholar]

[8] Coustou-Linares V, Maddelein ML, Bégueret J, Saupe S. In vivo aggregation of the HET-s prion protein of the fungus Podospora anserina. Mol Microbiol 2001; 42: 1325–35. [Google Scholar]

[9] Dos-Reis S, Coulary-Salin B, Forges V, Lascu I,Bégueret J, Saupe S. The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid-like fibrils. J Biol Chem 2002; 277: 5703–6. [Google Scholar]

[10] Uptain SM, Sawinicki GJ, Caughey B, LindquistS. Strains of [PSI(+)] are distinguished by their efficiencies of prionmediated conformational conversion. EMBO J 2001; 20: 6236–45. [Google Scholar]

[11] Speransky VV, Taylor KL, Edskes HK, Wickner RB, Steven AC. Prion filament networks in [URE3] cells of Saccharomyces cerevisiae. J Cell Sci 2001; 153: 1327–36. [Google Scholar]