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The 10 kDa culture filtrate protein (CFP-10) is a critical virulence factor and secreted antigen produced by Mycobacterium tuberculosis. It belongs to the WXG100 protein family and typically functions as a 1:1 heterodimeric complex with ESAT-6, where CFP-10 serves as a molecular chaperone essential for the stability and secretion of the complex via the ESX-1 (Type VII) secretion system [1, 2, 6]. Once secreted, the complex mediates host-pathogen interactions, specifically facilitating the escape of the bacterium from the macrophage phagosome into the cytosol and modulating host immune responses by inhibiting reactive oxygen species (ROS) and NF-kappaB signaling [7, 11, 13]. CFP-10 also exhibits independent biological activity by binding to a G-protein-coupled receptor on human neutrophils, triggering calcium release and chemotaxis [5]. Because it is encoded in the RD1 genomic region, which is absent in the M. bovis BCG vaccine strain, CFP-10 is a primary diagnostic target in interferon-gamma release assays (IGRAs) used to distinguish TB infection from prior vaccination [9, 14]. Current therapeutic research is exploring CFP-10 as a target for novel anti-virulence drugs that inhibit its secretion and for therapeutic antibodies that activate macrophage-mediated bacterial killing [12, 16].
Stimulates host T-cells to release interferon-gamma for diagnostic detection; as a virulence factor, it complexes with ESAT-6 to disrupt host membranes and evade immune responses; experimental inhibitors block its interaction with the ESX-1 secretion machinery to attenuate bacterial virulence [1, 5, 8, 12].
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