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through Myeloid Differentiation Factor 88-Dependent and -Independent Mechanisms1
* Division of Immunology and Infectious Disease, Harvard School of Public Health, Boston, MA 02115;
Trudeau Institute, Saranac Lake, NY 12983;
Department of Microbiology, Immunology, and Pathology, Colorado State University, Fort Collins, CO 80523; and
Departments of Medicine and Microbiology, New York University School of Medicine, New York, NY 10016
Mycobacterium tuberculosis overcomes macrophage bactericidal activities and persists intracellularly. One mechanism by which M. tuberculosis avoids macrophage killing might be through inhibition of IFN-
-mediated signaling. In this study we provide evidence that at least two distinct components of M. tuberculosis, the 19-kDa lipoprotein and cell wall peptidoglycan (contained in the mycolylarabinogalactan peptidoglycan (mAGP) complex), inhibit macrophage responses to IFN- at a transcriptional level. Moreover, these components engage distinct proximal signaling pathways to inhibit responses to IFN-: the 19-kDa lipoprotein inhibits IFN- signaling in a Toll-like receptor (TLR)2-dependent and myeloid differentiation factor 88-dependent fashion whereas mAGP inhibits independently of TLR2, TLR4, and myeloid differentiation factor 88. In addition to inhibiting the induction of specific IFN- responsive genes, the 19-kDa lipoprotein and mAGP inhibit the ability of IFN- to activate murine macrophages to kill virulent M. tuberculosis without inhibiting production of NO. These results imply that inhibition of macrophage responses to IFN- may contribute to the inability of an apparently effective immune response to eradicate M. tuberculosis.
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