Introduction
Hsp60 (~60 kDa) is a member of the heat shock protein family. The main function of Hsp60 is to capture newly synthesized or denatured protein and promote its folding. It should be noted that Hsp60 exhibits the properties of a molecular chaperonin not only at high temperatures, as its name suggests, but also under conditions of moderately acidic1 or high salinity2. Because the cells of organisms are under incessant stress, Hsp60 is a highly expressed protein. Thus, its ubiquitous distribution makes Hsp60 a promising object for research and use.
Today Hsp60 plays an important role in medicine. In particular, Hsp60, which is involved in the pro-inflammatory response, up-regulates the production of IL-83 and IL-64 in human bronchial epithelial cells and microglia, respectively. In addition, Hsp60 as an adipokine can be released from adipose tissue5. The level of chaperonins in the blood of obese patients positively correlates with markers of inflammation, which may indicate the development of cardiovascular disease. Hsp60 is also involved in the autoimmune response as an antigen6. Since Hsp60 is overexpressed in tumor cells, it can be used both to detect the early stage of cancer7 and to develop immunogenicity against it8. On the other hand, chaperonin can be used as a target not only for immunotherapy, but also for antibiotic therapy of bacterial diseases such as African sleeping sickness9,10 and Mycobacterium tuberculosisinfections11. In such cases, Hsp60 of pathogenic microorganisms is inhibited by various inhibitors9–11.
At present, in-depth analysis of Hsp60 sequences in silico is quite rare, although it is a very interesting object for research. Since Hsp60 is ubiquitous, it can be used in evolutionary analysis of organisms belonging to different taxonomic groups12–15. Using bioinformatics, epitopes in Hsp60 can be predicted16,17. In particular, an epitope-based vaccine containing Hsp60 epitopes from Helicobacter pylori was tested in a model of a Mongolian gerbil infected with H. pylori 16. Oral immunization with this vaccine reducedH. pylori colonization due to the T helper, IgG, and IgA responses and antibodies against various H. pylori antigens. In another study, B-cell epitopes were identified in silico in Hsp60 overexpressed by tumor cells17. In addition, it was proposed to use the sequence of Hsp60 gene for the species-specific identification of organisms belonging to the genus Acetobacter sp .18, Helicobacter sp .19,Staphylococcus sp .20, Bifidobacterium sp .21,22, and Bacteroidetes sp. 23 The interaction patterns of Hsp60 and the Aβ(1-42) peptide were predicted by molecular dynamics simulation and protein-peptide docking24. These results are important because Hsp60 affects oligomers of the Aβ peptide reducing their cytotoxicity in patients with Alzheimer’s disease25.
As you can see, Hsp60 has a fairly wide range of applications and requires in-depth research. Therefore, the purpose of this study is a comprehensive bioinformatic analysis of the amino acid and nucleotide sequences of Hsp60 and the compilation of convenient databases on its basis.