Effect of Cell Genome Editing on the Outcome of Neurotransplantation in Experimental Parkinsonism

Stavrovskaya, A. V.; Новосадова, Е. В.; Olshansky, A. S.; Yamshchikova, N. G.; Gushchina, A. S.; Arsenyeva, E. L.; Гривенников, И. А.; Illarioshkin, S. N.

doi:10.17691/stm2017.9.4.01

Cited by 2 publications

(1 citation statement)

References 9 publications

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“…However, the specific components of bacterial cells that act as active factors and the mechanism of their action remain unknown. Previously, L. fermentum U-21 was shown to act as pharmabiotic, which can reduce pro-inflammatory changes in rat models of Parkinson's disease [48]. Our results suggest that the anti-parkinsonian properties of the L. fermentum U-21 strain are determined, in part, by the ClpL protein and its ability to refold protein aggregates.…”

Section: Discussionmentioning

confidence: 53%

ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus fermentum U-21

Al Ebrahim,

Alekseeva,

Bazhenov

et al. 2024

Preprint

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Strain L. fermentum U-21 secretes chaperones into the medium and it is considered as the candidate for the development of drugs, so-called disaggregases, for Parkinson’s disease therapy. This study is devoted to characterization of secreted protein encoded by C0965_000195 locus. Analysis of sequence and predicted structure of the protein encoded by C0965_000195 allows us to attribute it to the ClpL, homologs of which are known to be chaperones. The chaperone activity of ClpL L. fermentum U-21 was evaluated in vivo by refolding of differing in thermostability luciferases from Aliivibrio fischeri and Photorhabdus luminescens in Escherichia coli cells. It was observed that clpL from L. fermentum U-21 can compensate for the deficiency in the clpB gene and enhance the ability to refold thermodenatured proteins in clpB- cells. In vitro experiments have demonstrated the ability of a spent culture medium containing proteins secreted by L. fermentum U-21 cells, including ClpL, to prevent thermodenaturation of luciferases partially.We suggest that the ClpL protein from L. fermentum U-21 strain, which exhibits disaggregase properties against aggregating proteins, may be one of the clue components that play a role in the pharmabiotic properties of this strain.

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Section: Discussionmentioning

confidence: 53%