Mycobacterium tuberculosis chaperonin 60.1 (Cpn60.1)

Mycobacterium tuberculosis chaperonin 60.1 (Cpn60.1), also known as GroEL1, is a molecular chaperone and a key virulence factor of the tuberculosis-causing bacterium. Unlike its essential paralog Cpn60.2 (GroEL2), Cpn60.1 is non-essential for bacterial growth in vitro but is critical for the formation of mature granulomas and survival under low-oxygen conditions during infection. It functions as a potent immunomodulator, stimulating the production of pro-inflammatory cytokines by interacting with host receptors such as CD14 and TLR4. Interestingly, while the full-length protein is pro-inflammatory, a specific peptide derived from it, IRL201104, has demonstrated significant anti-inflammatory properties by increasing the expression of the anti-inflammatory molecule A20 and inhibiting NF-kappaB. This peptide is currently being developed as a first-in-class immune resetting therapy for allergic and inflammatory diseases, including asthma and eosinophilic esophagitis. Cpn60.1 also interacts with the mycolic acid synthesis enzyme KasA, influencing biofilm formation and antibiotic tolerance.

Other names

GroEL1Hsp60.1Rv3417c60 kDa chaperonin 1Antigen Cpn60.1Heat shock protein 60.1