The G127V variant of the prion protein interferes with dimer formation in vitro but not in cellulo.
Sci Rep
; 11(1): 3116, 2021 02 04.
Article
en En
| MEDLINE
| ID: mdl-33542378
ABSTRACT
Scrapie prion, PrPSc, 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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Valina
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Proteínas Recombinantes de Fusión
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Proteínas PrPSc
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Proteínas Priónicas
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Glicina
Límite:
Humans
Idioma:
En
Revista:
Sci Rep
Año:
2021
Tipo del documento:
Article
País de afiliación:
Hungria