Document Detail


Mycobacterium tuberculosis activates human macrophage peroxisome proliferator-activated receptor gamma linking mannose receptor recognition to regulation of immune responses.
MedLine Citation:
PMID:  20554962     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mycobacterium tuberculosis enhances its survival in macrophages by suppressing immune responses in part through its complex cell wall structures. Peroxisome proliferator-activated receptor gamma (PPARgamma), a nuclear receptor superfamily member, is a transcriptional factor that regulates inflammation and has high expression in alternatively activated alveolar macrophages and macrophage-derived foam cells, both cell types relevant to tuberculosis pathogenesis. In this study, we show that virulent M. tuberculosis and its cell wall mannose-capped lipoarabinomannan induce PPARgamma expression through a macrophage mannose receptor-dependent pathway. When activated, PPARgamma promotes IL-8 and cyclooxygenase 2 expression, a process modulated by a PPARgamma agonist or antagonist. Upstream, MAPK-p38 mediates cytosolic phospholipase A(2) activation, which is required for PPARgamma ligand production. The induced IL-8 response mediated by mannose-capped lipoarabinomannan and the mannose receptor is independent of TLR2 and NF-kappaB activation. In contrast, the attenuated Mycobacterium bovis bacillus Calmette-Guérin induces less PPARgamma and preferentially uses the NF-kappaB-mediated pathway to induce IL-8 production. Finally, PPARgamma knockdown in human macrophages enhances TNF production and controls the intracellular growth of M. tuberculosis. These data identify a new molecular pathway that links engagement of the mannose receptor, an important pattern recognition receptor for M. tuberculosis, with PPARgamma activation, which regulates the macrophage inflammatory response, thereby playing a role in tuberculosis pathogenesis.
Authors:
Murugesan V S Rajaram; Michelle N Brooks; Jessica D Morris; Jordi B Torrelles; Abul K Azad; Larry S Schlesinger
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2010-06-16
Journal Detail:
Title:  Journal of immunology (Baltimore, Md. : 1950)     Volume:  185     ISSN:  1550-6606     ISO Abbreviation:  J. Immunol.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-07-05     Completed Date:  2010-08-10     Revised Date:  2011-07-20    
Medline Journal Info:
Nlm Unique ID:  2985117R     Medline TA:  J Immunol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  929-42     Citation Subset:  AIM; IM    
Affiliation:
Center for Microbial Interface Biology, Ohio State University, Columbus, OH 43210, USA.
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MeSH Terms
Descriptor/Qualifier:
Anilides / pharmacology
Blotting, Western
Cells, Cultured
Cyclooxygenase 2 / metabolism
Enzyme Activation / drug effects
Host-Pathogen Interactions / immunology
Humans
Interleukin-8 / metabolism
Lectins, C-Type / genetics,  metabolism*
Lipopolysaccharides / immunology,  pharmacology
Macrophages / cytology,  metabolism*,  microbiology
Mannose-Binding Lectins / genetics,  metabolism*
Models, Immunological
Mycobacterium tuberculosis / immunology*,  physiology
NF-kappa B / metabolism
PPAR gamma / antagonists & inhibitors,  genetics,  metabolism*
Phospholipases A2, Cytosolic / metabolism
RNA Interference
Receptors, Cell Surface / genetics,  metabolism*
Signal Transduction / drug effects,  immunology
Tumor Necrosis Factor-alpha / metabolism
p38 Mitogen-Activated Protein Kinases / metabolism
Grant Support
ID/Acronym/Agency:
AI052458/AI/NIAID NIH HHS; AI059639/AI/NIAID NIH HHS; R01 AI052458-05/AI/NIAID NIH HHS; R01 AI059639-05/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/2-chloro-5-nitrobenzanilide; 0/Anilides; 0/Interleukin-8; 0/Lectins, C-Type; 0/Lipopolysaccharides; 0/Mannose-Binding Lectins; 0/NF-kappa B; 0/PPAR gamma; 0/Receptors, Cell Surface; 0/Tumor Necrosis Factor-alpha; 0/lipoarabinomannan; 0/mannose receptor; EC 1.14.99.1/Cyclooxygenase 2; EC 2.7.11.24/p38 Mitogen-Activated Protein Kinases; EC 3.1.1.4/Phospholipases A2, Cytosolic
Comments/Corrections

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