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Inhibition of Chaperonin GroEL by a Monomer of Ovine Prion Protein and Its Oligomeric Forms

S. S. Kudryavtseva1, Y. Y. Stroylova1, I. A. Zanyatkin2, T. Haertle3, and V. I. Muronetz1,2*

1Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, Russia; E-mail: vimuronets@belozersky.msu.ru

2Lomonosov Moscow State University, Faculty of Bioengineering and Bioinformatics, 119234 Moscow, Russia

3Institut National de la Recherche Agronomique, 44000 Nantes, France

* To whom correspondence should be addressed.

Received June 17, 2016; Revision received July 29, 2016
The possibility of inhibition of chaperonin functional activity by amyloid proteins was studied. It was found that the ovine prion protein PrP as well as its oligomeric and fibrillar forms are capable of binding with the chaperonin GroEL. Besides, GroEL was shown to promote amyloid aggregation of the monomeric and oligomeric PrP as well as PrP fibrils. The monomeric PrP was shown to inhibit the GroEL-assisted reactivation of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The oligomers of PrP decelerate the GroEL-assisted reactivation of GAPDH, and PrP fibrils did not affect this process. The chaperonin GroEL is capable of interacting with GAPDH and different PrP forms simultaneously. A possible role of the inhibition of chaperonins by amyloid proteins in the misfolding of the enzymes involved in cell metabolism and in progression of neurodegenerative diseases of amyloid nature is discussed.
KEY WORDS: amyloid proteins, chaperonin GroEL, prion PrP, oligomeric forms of prion protein, glyceraldehyde-3-phosphate dehydrogenase, reactivation, inhibition of chaperonin

DOI: 10.1134/S0006297916100199