Integrity of helix 2-helix 3 domain of the PrP protein is not mandatory for prion replication.

ABSTRACT: The process of prion conversion is not yet well understood at the molecular level. The regions critical for the conformational change of PrP remain mostly debated and the extent of sequence change acceptable for prion conversion is poorly documented. To achieve progress on these issues, we applied a reverse genetic approach using the Rov cell system. This allowed us to test the susceptibility of a number of insertion mutants to conversion into prion in the absence of wild-type PrP molecules. We were able to propagate several prions with 8 to 16 extra amino acids, including a polyglycine stretch and His or FLAG tags, inserted in the middle of the protease-resistant fragment. These results demonstrate the possibility to increase the length of the loop between helices H2 and H3 up to 4-fold,

SUBMITTER: Salamat K 

PROVIDER: S-EPMC3365929 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature