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The **65-kilodalton heat shock protein (HSP65)** is a molecular chaperone primarily studied in Mycobacterium species, notably *Mycobacterium tuberculosis* and *Mycobacterium avium* subsp. *paratuberculosis*. It assists in **protein folding**, prevents aggregation, and aids in degradation of proteins under stress conditions. HSP65 is highly antigenic, provoking strong immune responses and cytokine production in host organisms. Its molecular similarity to human proteins leads to **molecular mimicry**, making it a proposed trigger for several autoimmune diseases (such as type 1 diabetes, autoimmune thyroiditis, and multiple sclerosis) by stimulating cross-reactive autoantibodies. HSP65 is overexpressed during bacterial stress and phagocytosis by macrophages, contributing to pathogen defense and immunomodulation[1][2][3]. It is not the direct molecular target of existing drugs but rather a biologically and immunologically important protein with indirect roles in infection and autoimmunity.
Induction of immune response via antigenicity (immunodominant protein); Triggering of autoimmunity through molecular mimicry
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