Prion Protein Biology

Prusiner, Stanley B.; Scott, Michael; DeArmond, Stephen J.; Cohen, Fred E.

doi:10.1016/s0092-8674(00)81163-0

Cited by 871 publications

(616 citation statements)

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“…Prions are infectious agents responsible for a group of diseases typi®ed by sheep scrapie, bovine spongiform encephalopathy and human Creutzfeld±Jacob disease (for review, see Horwich and Weissman, 1997;Prusiner et al, 1998). The contemporary concept suggests that they represent a conformationally altered form (PrP Sc ) of normal host-encoded protein (PrP C ), which has acquired an ability to convert PrP C into this altered prion form.…”

Section: Introductionmentioning

confidence: 99%

“…In mammals, different prion strains are de®ned by speci®c incubation times, distribution of vacuolar lesions and patterns of PrP Sc accumulation (for review, see Prusiner et al, 1998). In yeast they can be revealed by differences in the suppressor ef®ciency and mitotic stability of independently isolated [PSI + ] determinants (Derkatch et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

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[PSI⁺] prion generation in yeast: characterization of the ‘strain’ difference

Kochneva-Pervukhova

Chechenova

Valouev

et al. 2001

Yeast

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

[PSI⁺] prion generation in yeast: characterization of the ‘strain’ difference

Kochneva-Pervukhova

Chechenova

Valouev

et al. 2001

Yeast

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“…At this molar ratio, insufficient amounts of CB2 were present to bind all the tOspB. Therefore, we suggest either 1) the mAb shows turnover; or 2) the mAb propagates its effect through producing a change in tOspB that is then further propagated by the tOspB-tOspB interaction, a form of activity that in some ways resembles that of prions (51)(52)(53). Regardless of the mechanism, these results showed that CB2 effected a change in B31-tOspB that could be measured by decreased susceptibility of tOspB to cleavage by trypsin or Arg-C.…”

Section: Discussionmentioning

confidence: 93%

A Bactericidal Monoclonal Antibody Elicits a Change in Its Antigen, OspB of Borrelia burgdorferi, That Can Be Detected by Limited Proteolysis

Katona

Ayalew

Coleman

et al. 2000

The Journal of Immunology

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mAb CB2, directed against outer surface protein B (OspB), causes bacteriolysis of Borrelia burgdorferi in the absence of complement. How this happens is unknown. We examined the effect of mAb binding on OspB tertiary structure by using limited proteolysis to probe changes in protein conformation. Truncated OspB (tOspB) that lacked N-terminal lipid was cleaved by four enzymes: trypsin, endoproteinase Arg-C, endoproteinase Asp-N, and endoproteinase Glu-C. CB2 affected the cleavage by trypsin and Arg-C, but not by AspN or Glu-C. None of the enzymes cleaved CB2 under these conditions. Both trypsin and Arg-C cleaved tOspB near the N-terminus; CB2 slowed the rate of cleavage, but did not affect the identity of the sites cleaved. Irrelevant mAb had no effect, indicating that the effect was specific. CB2 was active against tOspB of strain B31, but not against tOspB of strain BEP4, to which it does not bind, suggesting that binding was required to elicit the effect on cleavage. With trypsin, CB2 showed a maximal effect at 8 mol of tOspB to 1 mol of mAb. At this ratio, not enough CB2 was present to bind all the tOspB; therefore, either CB2 shows turnover or CB2 acts by binding tOspB and effecting a change in this tOspB such that it, in turn, propagates the effect in other molecules of tOspB. Regardless of the mechanism, these data show that CB2 elicits a change in tOspB that can be measured by its reduced susceptibility to protease cleavage.

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“…Once formed, prions can propagate in an auto-catalytic manner, recruiting the normal cellular protein to fold into its abnormal conformation. 1,2 Mammalian prion diseases, also termed transmissible spongiform encephalopathies (TSEs), are fatal neurodegenerative disorders that affect humans and other mammals. Despite they have been described since the late 18th century, the recognition that these diseases were caused by infectious proteins became clear only in the early 1980-s, largely due to the work of Stanley Prusiner.…”

Section: Introductionmentioning

confidence: 99%

Mammalian prion amyloid formation in bacteria

Macedo

Cordeiro

Ventura

2016

Prion

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ABSTRACT. Mammalian prion proteins (PrPs) that cause transmissible spongiform encephalopathies are misfolded conformations of the host cellular PrP. The misfolded form, the scrapie PrP (PrP Sc ), can aggregate into amyloid fibrils that progressively accumulate in the brain, evolving to a pathological phenotype. A particular characteristic of PrP Sc is to be found as different strains, related to the diversity of conformational states it can adopt. Prion strains are responsible for the multiple phenotypes observed in prion diseases, presenting different incubation times and diverse deposition profiles in the brain. PrP biochemical properties are also strain-dependent, such as different digestion pattern after proteolysis and different stability. Although they have long been studied, strain formation is still a major unsolved issue in prion biology. The recreation of strainspecific conformational features is of fundamental importance to study this unique pathogenic phenomenon. In our recent paper, we described that murine PrP, when expressed in bacteria, forms amyloid inclusion bodies that possess different strain-like characteristics, depending on the PrP construct. Here, we present an extra-view of these data and propose that bacteria might become a successful model to generate preparative amounts of prion strain-specific assemblies for highresolution structural analysis as well as for addressing the determinants of infectivity and transmissibility.

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Prion Protein Biology

Cited by 871 publications

References 95 publications

[PSI⁺] prion generation in yeast: characterization of the ‘strain’ difference

[PSI⁺] prion generation in yeast: characterization of the ‘strain’ difference

A Bactericidal Monoclonal Antibody Elicits a Change in Its Antigen, OspB of Borrelia burgdorferi, That Can Be Detected by Limited Proteolysis

Mammalian prion amyloid formation in bacteria

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Prion Protein Biology

Cited by 871 publications

References 95 publications

[PSI+] prion generation in yeast: characterization of the ‘strain’ difference

[PSI+] prion generation in yeast: characterization of the ‘strain’ difference

A Bactericidal Monoclonal Antibody Elicits a Change in Its Antigen, OspB of Borrelia burgdorferi, That Can Be Detected by Limited Proteolysis

Mammalian prion amyloid formation in bacteria

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[PSI⁺] prion generation in yeast: characterization of the ‘strain’ difference

[PSI⁺] prion generation in yeast: characterization of the ‘strain’ difference