Bacteriophage-encoded chaperonins stimulate prion protein fibrillation in an ATP-dependent manner.

Autor: Leisi EV; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Leninskie Gory 1, Bld 73, 119991 Moscow, Russia., Moiseenko AV; Faculty of Biology, Lomonosov Moscow State University, Leninskie Gory 1, Bld 12, 119991 Moscow, Russia., Kudryavtseva SS; Belozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, Bld 40, 119991 Moscow, Russia., Pozdyshev DV; Belozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, Bld 40, 119991 Moscow, Russia., Muronetz VI; Belozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, Bld 40, 119991 Moscow, Russia; Butlerov Chemical Institute, Kazan Federal University, Kremlevskaya 18, 420008 Kazan, Russia., Kurochkina LP; Belozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory 1, Bld 40, 119991 Moscow, Russia. Electronic address: lpk@belozersky.msu.ru.
Jazyk: angličtina
Zdroj: Biochimica et biophysica acta. Proteins and proteomics [Biochim Biophys Acta Proteins Proteom] 2024 Jan 01; Vol. 1872 (1), pp. 140965. Date of Electronic Publication: 2023 Sep 20.
DOI: 10.1016/j.bbapap.2023.140965
Abstrakt: The pathogenesis of the various prion diseases is based on the conformational conversion of the prion protein from its physiological cellular form to the insoluble scrapie isoform. Several chaperones, including the Hsp60 family of group I chaperonins, are known to contribute to this transformation, but data on their effects are scarce and conflicting. In this work, two GroEL-like phage chaperonins, the single-ring OBP and the double-ring EL, were found to stimulate monomeric prion protein fibrillation in an ATP-dependent manner. The resulting fibrils were characterised by thioflavin T fluorescence, electron microscopy, proteinase K digestion assay and other methods. In the presence of ATP, chaperonins were found to promote the conversion of prion protein monomers into short amyloid fibrils with their further aggregation into less toxic large clusters. Fibrils generated with the assistance of phage chaperonins differ in morphology and properties from those formed spontaneously from monomeric prion in the presence of denaturants at acidic pH.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2023. Published by Elsevier B.V.)
Databáze: MEDLINE
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