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Biochemical properties of highly neuroinvasive prion strains.

Abstract：

:Infectious prions propagate from peripheral entry sites into the central nervous system (CNS), where they cause progressive neurodegeneration that ultimately leads to death. Yet the pathogenesis of prion disease can vary dramatically depending on the strain, or conformational variant of the aberrantly folded and aggregated protein, PrP(Sc). Although most prion strains invade the CNS, some prion strains cannot gain entry and do not cause clinical signs of disease. The conformational basis for this remarkable variation in the pathogenesis among strains is unclear. Using mouse-adapted prion strains, here we show that highly neuroinvasive prion strains primarily form diffuse aggregates in brain and are noncongophilic, conformationally unstable in denaturing conditions, and lead to rapidly lethal disease. These neuroinvasive strains efficiently generate PrP(Sc) over short incubation periods. In contrast, the weakly neuroinvasive prion strains form large fibrillary plaques and are stable, congophilic, and inefficiently generate PrP(Sc) over long incubation periods. Overall, these results indicate that the most neuroinvasive prion strains are also the least stable, and support the concept that the efficient replication and unstable nature of the most rapidly converting prions may be a feature linked to their efficient spread into the CNS.

journal_name

PLoS Pathog

journal_title

PLoS pathogens

authors

Bett C,Joshi-Barr S,Lucero M,Trejo M,Liberski P,Kelly JW,Masliah E,Sigurdson CJ

doi

10.1371/journal.ppat.1002522

subject

Has Abstract

pub_date

2012-02-01 00:00:00

pages

e1002522

issue

2

eissn

1553-7366

issn

1553-7374

pii

PPATHOGENS-D-11-02044

journal_volume

8

pub_type

杂志文章

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