Back to Search
Start Over
The G127V variant of the prion protein interferes with dimer formation in vitro but not in cellulo.
- Source :
-
Scientific reports [Sci Rep] 2021 Feb 04; Vol. 11 (1), pp. 3116. Date of Electronic Publication: 2021 Feb 04. - Publication Year :
- 2021
-
Abstract
- Scrapie prion, PrP <superscript>Sc</superscript> , formation is the central event of all types of transmissible spongiform encephalopathies (TSEs), while the pathway with possible intermediates and their mechanism of formation from the normal isoform of prion (PrP), remains not fully understood. Recently, the G127V variant of the human PrP is reported to render the protein refractory to transmission of TSEs, via a yet unknown mechanism. Molecular dynamics studies suggested that this mutation interferes with the formation of PrP dimers. Here we analyze the dimerization of 127G and 127VPrP, in both in vitro and a mammalian cell culture system. Our results show that while molecular dynamics may capture the features affecting dimerization in vitro, G127V inhibiting dimer formation of PrP, these are not evidenced in a more complex cellular system.
- Subjects :
- Amino Acid Substitution
Cloning, Molecular
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression
Genetic Vectors chemistry
Genetic Vectors metabolism
Glycine chemistry
HeLa Cells
Humans
Luminescent Proteins genetics
Luminescent Proteins metabolism
Molecular Dynamics Simulation
Mutation
PrPSc Proteins genetics
PrPSc Proteins metabolism
Prion Diseases genetics
Prion Diseases metabolism
Prion Proteins genetics
Prion Proteins metabolism
Protein Multimerization
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Valine chemistry
Red Fluorescent Protein
Glycine metabolism
PrPSc Proteins chemistry
Prion Proteins chemistry
Recombinant Fusion Proteins chemistry
Valine metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 11
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 33542378
- Full Text :
- https://doi.org/10.1038/s41598-021-82647-w