Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Human IRGM Induces Autophagy to Eliminate Intracellular Mycobacteria
Sudha B. Singh,1Alexander S. Davis,1Gregory A. Taylor,3,4Vojo Deretic1,2*
Immunity-related p47 guanosine triphosphatases (IRG) play arole in defense against intracellular pathogens. We found thatthe murine Irgm1 (LRG-47) guanosine triphosphatase induced autophagyand generated large autolysosomal organelles as a mechanismfor the elimination of intracellular Mycobacterium tuberculosis.We also identified a function for a human IRG protein in thecontrol of intracellular pathogens and report that the humanIrgm1 ortholog, IRGM, plays a role in autophagy and in the reductionof intracellular bacillary load.
1 Department of Molecular Genetics and Microbiology, University of New Mexico School of Medicine, Albuquerque, NM 87131, USA. 2 Department of Cell Biology and Physiology, University of New Mexico School of Medicine, Albuquerque, NM 87131, USA. 3 Department of Medicine, Department of Molecular Genetics and Microbiology, Department of Immunology, Center for the Study of Aging, Duke University, Durham, NC 27710, USA. 4 Geriatric Research, Education, and Clinical Center, Department of Veterans Affairs Medical Center, Durham, NC 27710, USA.
* To whom correspondence should be addressed. E-mail: vderetic{at}salud.unm.edu
Autophagy as an important process in gut homeostasis and Crohn's disease pathogenesis.
R. J Xavier, A. Huett, and J. D Rioux (2008)
Gut
57, 717-720
|Full Text »|PDF »
Chlamydia muridarum Evades Growth Restriction by the IFN-{gamma}-Inducible Host Resistance Factor Irgb10.
J. Coers, I. Bernstein-Hanley, D. Grotsky, I. Parvanova, J. C. Howard, G. A. Taylor, W. F. Dietrich, and M. N. Starnbach (2008)
J. Immunol.
180, 6237-6245
|Abstract »|Full Text »|PDF »
Modulation of the Phagosome Proteome by Interferon-{gamma}.
I. Jutras, M. Houde, N. Currier, J. Boulais, S. Duclos, S. LaBoissiere, E. Bonneil, P. Kearney, P. Thibault, E. Paramithiotis, et al. (2008)
Mol. Cell. Proteomics
7, 697-715
|Abstract »|Full Text »|PDF »
Host pathogen protein interactions predicted by comparative modeling.
F. P. Davis, D. T. Barkan, N. Eswar, J. H. McKerrow, and A. Sali (2007)
Protein Sci.
16, 2585-2596
|Abstract »|Full Text »|PDF »
Impaired Macrophage Function Underscores Susceptibility to Salmonella in Mice Lacking Irgm1 (LRG-47).
S. C. Henry, X. Daniell, M. Indaram, J. F. Whitesides, G. D. Sempowski, D. Howell, T. Oliver, and G. A. Taylor (2007)
J. Immunol.
179, 6963-6972
|Abstract »|Full Text »|PDF »
Common pathways in Crohn's disease and other inflammatory diseases revealed by genomics.
The IFN-Inducible GTPase LRG47 (Irgm1) Negatively Regulates TLR4-Triggered Proinflammatory Cytokine Production and Prevents Endotoxemia.
A. Bafica, C. G. Feng, H. C. Santiago, J. Aliberti, A. Cheever, K. E. Thomas, G. A. Taylor, S. N. Vogel, and A. Sher (2007)
J. Immunol.
179, 5514-5522
|Abstract »|Full Text »|PDF »
The p47 GTPases Iigp2 and Irgb10 Regulate Innate Immunity and Inflammation to Murine Chlamydia psittaci Infection.
I. Miyairi, V. R. R. A. Tatireddigari, O. S. Mahdi, L. A. Rose, R. J. Belland, L. Lu, R. W. Williams, and G. I. Byrne (2007)
J. Immunol.
179, 1814-1824
|Abstract »|Full Text »|PDF »
IL-1 Receptor-Mediated Signal Is an Essential Component of MyD88-Dependent Innate Response to Mycobacterium tuberculosis Infection.
C. M. Fremond, D. Togbe, E. Doz, S. Rose, V. Vasseur, I. Maillet, M. Jacobs, B. Ryffel, and V. F. J. Quesniaux (2007)
J. Immunol.
179, 1178-1189
|Abstract »|Full Text »|PDF »