HspX-mediated protection against tuberculosis depends on its chaperoning of a mycobacterial molecule.

摘要: New approaches consisting of 'multistage' vaccines against (TB) are emerging that combine early antigenic proteins with latency-associated antigens. In this study, HspX was tested for its potential to elicit both short- and long-term protective immune responses. is a logical component in vaccine strategies targeting responses primary infection, as well reactivation latent because previously shown, it produced during latency, our studies show, elicits protection within 30 days infection. Recent have shown the current TB vaccine, bacilli Calmette-Guerin (BCG), does not induce strong interferon-γ T-cell antigens like HspX, which may be part why BCG fails protect disease. We therefore protein alone prophylactic boost vaccination, found purified from M. tuberculosis cell lysates protected mice aerosol challenge improved efficacy when used booster vaccine. Native highly immunogenic protective, dose-dependent manner, infection models. Based on these promising findings, recombinant E. coli, would enable facile purification; however, (rHspX) consistently failed challenge. Incubation rHspX mycobacterial lysate re-purification following incubation restored capacity confer protection. These data suggest possibility native form chaperone an antigen mycobacteria-specific.