The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Toll-Like Receptor 2-Dependent Inhibition of Macrophage Class II MHC Expression and Antigen Processing by 19-kDa Lipoprotein of Mycobacterium tuberculosis
Abstract
Mycobacterium tuberculosis (MTB) induces vigorous immune responses, yet persists inside macrophages, evading host immunity. MTB bacilli or lysate was found to inhibit macrophage expression of class II MHC (MHC-II) molecules and MHC-II Ag processing. This report characterizes and identifies a specific component of MTB that mediates these inhibitory effects. The inhibitor was extracted from MTB lysate with Triton X-114, isolated by gel electroelution, and identified with Abs to be MTB 19-kDa lipoprotein. Electroelution- or immunoaffinity-purified MTB 19-kDa lipoprotein inhibited MHC-II expression and processing of both soluble Ags and Ag 85B from intact MTB bacilli. Inhibition of MHC-II Ag processing by either MTB bacilli or purified MTB 19-kDa lipoprotein was dependent on Toll-like receptor (TLR) 2 and independent of TLR 4. Synthetic analogs of lipopeptides from Treponema pallidum also inhibited Ag processing. Despite the ability of MTB 19-kDa lipoprotein to activate microbicidal and innate immune functions early in infection, TLR 2-dependent inhibition of MHC-II expression and Ag processing by MTB 19-kDa lipoprotein during later phases of macrophage infection may prevent presentation of MTB Ags and decrease recognition by T cells. This mechanism may allow intracellular MTB to evade immune surveillance and maintain chronic infection.
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Cites
Innate Immunity: The Virtues of a Nonclonal System of Recognition
Medzhitov, R., & Janeway, C. A. (1997) · Cell · doi:10.1016/s0092-8674(00)80412-2 · Cited by 2,434
Peptidoglycan- and Lipoteichoic Acid-induced Cell Activation Is Mediated by Toll-like Receptor 2
Schwandner, R., Dziarski, R., Wesche, H., Rothe, M., & Kirschning, C. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17406 · Cited by 1,704
Phagocytic processing of bacterial antigens for class I MHC presentation to T cells
Pfeifer, J. D., Wick, M. J., Roberts, R. L., Findlay, K., Normark, S. J., & Harding, C. V. (1993) · Nature · doi:10.1038/361359a0 · Cited by 615 · cited 1×
“Because alternate MHC-I Ag processing in this system (45, 46) depends on MHC-I molecules, phagocytosis, phagolysosomal function, and lysosomal proteases, this finding implies that MTB 19-kDa lipoprotein does not generally inhibit Ag uptake, proteolytic processing, or the expression of MHC-I molecules.”
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Cited by
Cell-Mediated Immune Responses in Tuberculosis
Cooper, A. M. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132703 · Cited by 1,162
Mycobacterium tuberculosis Pathogenesis and Molecular Determinants of Virulence
Smith, I. (2003) · Clinical Microbiology Reviews · doi:10.1128/cmr.16.3.463-496.2003 · Cited by 1,154
A Novel Host-Parasite Lipid Cross-talk
van der Kleij, D., Latz, E., Brouwers, J. F. H. M., Kruize, Y. C. M., Schmitz, M., Kurt-Jones, E. A., Espevik, T., de Jong, E. C., Kapsenberg, M. L., Golenbock, D. T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206941200 · Cited by 587
Self-citationWolf, A. J., Desvignes, L., Linas, B., Banaiee, N., Tamura, T., Takatsu, K., & Ernst, J. D. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20071367 · Cited by 580
Jagannath, C., Lindsey, D. R., Dhandayuthapani, S., Xu, Y., Hunter, R. L., & Eissa, N. T. (2009) · Nature Medicine · doi:10.1038/nm.1928 · Cited by 494
Metadata
- Authors
- Noss, E. H., Pai, R. K., Sellati, T. J., Radolf, J. D., Belisle, J., Golenbock, D. T., Boom, W. H., & Harding, C. V.
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2001-07
- Volume
- 167
- Issue
- 2
- Pages
- 910-918
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W2126245681
- Cited by
- 453
- References
- 3
- FWCI
- 19.52
- Type
- journal article
- Language
- en
- Open access
- closed
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