Publications by authors named "D A Mavletova"
Article Synopsis
- The U-21 strain secretes chaperones, like the ClpL protein, which shows potential as a disaggregase for treating Parkinson's disease.
- Analysis of the C0965_000195 gene reveals that ClpL can assist in refolding misfolded proteins, particularly luciferases, helping cells manage protein damage.
- Experiments indicate that both the secreted culture medium from U-21 and purified ClpL can protect proteins from denaturation, suggesting ClpL's key role in the strain’s potential therapeutic benefits.
In recent years, there has been an increasing tendency to create drugs based on certain commensal bacteria of the human microbiota and their ingredients, primarily focusing on live biotherapeutics (LBPs) and postbiotics. The creation of such drugs, termed pharmacobiotics, necessitates an understanding of their mechanisms of action and the identification of pharmacologically active ingredients that determine their target properties. Typically, these are complexes of biologically active substances synthesized by specific strains, promoted as LBPs or postbiotics (including vesicles): proteins, enzymes, low molecular weight metabolites, small RNAs, etc.
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- This study investigates the ability of specific protein fragments (2D FN3 and CD FN3) from a bacterial strain, GT15, to bind to the inflammatory cytokine TNF-α, using a sandwich ELISA method for detection.
- Results reveal that neither 2D FN3 nor CD FN3 can bind to TNF-α alone, however, the full ∆FN3.1 protein is capable of forming a binding pocket for TNF-α.
- Additionally, the study analyzes genetic variations in the amino acid sequences of ∆FN3.1 and compares FN3 domains from human gut bacteria, highlighting those with cytokine receptor motifs and their structural similarities with human proteins.
is a predominant and important genus in the bacterial population of the human gut microbiota. Despite the increasing number of studies on the beneficial functionality of bifidobacteria for human health, knowledge about their antioxidant potential is still insufficient. Several in vivo and in vitro studies of strains and their cellular components have shown good antioxidant capacity that provided a certain protection of their own and the host's cells.
View Article and Find Full Text PDFInvestigation of aminoglycoside acetyltransferases in actinobacteria of the genus Streptomyces is an integral part of the study of soil bacteria as the main reservoir and possible source of drug resistance genes. Previously, we have identified and biochemically characterized three aminoglycoside phosphotransferases, which cause resistance to kanamycin, neomycin, paromomycin, streptomycin, and hygromycin B in the strain Streptomyces rimosus ATCC 10970 (producing oxytetracycline), which is resistant to most natural aminoglycoside antibiotics. In the presented work, it was shown that the resistance of this strain to other AGs is associated with the presence of the enzyme aminoglycoside acetyltransferase, belonging to the AAC(2') subfamily.
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