Taking advantage of this possibility, TuMV virus-like particles (VLPs) have been genetically derivatized with a peptide from the chaperonin Hsp60, a protein described to be involved in inflammation processes and autoimmune diseases.
High degree of sequence homology between microbial and mammalian HSP60, due to evolutionary conservation, carries a risk of misdirected autoimmunity against HSPs expressed on the stressed cells of vascular endothelium.
Our results extend the role of specific hsp60 immunomodulation in the control of beta cell autoimmunity and demonstrate that immunoregulatory networks activated by specific phsp60 vaccination can spread to other Ags targeted during the progression of diabetes, like insulin and GAD.
Enzyme-linked immunosorbent assay-based examination of murine sera for immunoglobulin G1 (IgG1) and IgG2a immunoreactivity against diabetic autoantigens insulin and HSP60 revealed no statistically significant relationship between CVB3-protected mice or diabetic mice and specific autoimmunity.
Thus, newly diagnosed type 1 diabetes patients, similar to prediabetic and newly diabetic NOD mice, show heightened autoimmunity to hsp60 and hsp60 peptides.
Hsp 60 has been strongly implicated as an example of molecular mimicry in the pathogenicity of autoimmune diseases and, more recently, in T cell-mediated protection.
Our results demonstrate, that in contrast to some other autoimmune diseaseshsp60 mRNA is not overexpressed in thyroids from patients with Graveś disease.
The presence of the 60 kDa heat shock protein (hsp60) in seminal fluid and its relationship to sperm autoimmunity or a localized immune response to Chlamydia trachomatis were examined.
Heat shock proteins (hsp) are a group of proteins with a highly conserved structure and of these, hsp60 has been suggested to play a role in autoimmunity due to T lymphocyte crossreactivity between bacterial and human hsp60.