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.