Met₁₆₆ -Glu₁₆₈ residues in human PrP β2-α2 loop account for evolutionary resistance to prion infection.

ABSTRACT:

Aims

The amino acid sequence of prion protein (PrP) is a key determinant in the transmissibility of prion diseases. While PrP sequence is highly conserved among mammalian species, minor changes in the PrP amino acid sequence may confer alterations in the transmissibility of prion diseases. Classical bovine spongiform encephalopathy (C-BSE) is the only zoonotic prion strain reported to date causing variant Creutzfeldt-Jacob disease (vCJD) in humans, although experimental transmission points to atypical L-BSE and some classical scrapie isolates as also zoonotic. The precise molecular elements in the human PrP sequence that limit the transmissibility of prion strains such as sheep/goat scrapie or cervid chronic wasting disease (CWD) are not well known.

Methods

The transmissibil

SUBMITTER: Espinosa JC 

PROVIDER: S-EPMC8247420 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature