Al Ebrahim, R.N.; Alekseeva, M.G.; Bazhenov, S.V.; Fomin, V.V.; Mavletova, D.A.; Nesterov, A.A.; Poluektova, E.U.; Danilenko, V.N.; Manukhov, I.V. ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus Fermentum U-21. Biology 2024, 13, 592, doi:10.3390/biology13080592.
Al Ebrahim, R.N.; Alekseeva, M.G.; Bazhenov, S.V.; Fomin, V.V.; Mavletova, D.A.; Nesterov, A.A.; Poluektova, E.U.; Danilenko, V.N.; Manukhov, I.V. ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus Fermentum U-21. Biology 2024, 13, 592, doi:10.3390/biology13080592.
Al Ebrahim, R.N.; Alekseeva, M.G.; Bazhenov, S.V.; Fomin, V.V.; Mavletova, D.A.; Nesterov, A.A.; Poluektova, E.U.; Danilenko, V.N.; Manukhov, I.V. ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus Fermentum U-21. Biology 2024, 13, 592, doi:10.3390/biology13080592.
Al Ebrahim, R.N.; Alekseeva, M.G.; Bazhenov, S.V.; Fomin, V.V.; Mavletova, D.A.; Nesterov, A.A.; Poluektova, E.U.; Danilenko, V.N.; Manukhov, I.V. ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus Fermentum U-21. Biology 2024, 13, 592, doi:10.3390/biology13080592.
Abstract
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.
Keywords
ClpL; Chaperon; Luciferases
Subject
Biology and Life Sciences, Biology and Biotechnology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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