PMID- 22712528
OWN - NLM
STAT- MEDLINE
DCOM- 20130128
LR  - 20210109
IS  - 1462-5822 (Electronic)
IS  - 1462-5814 (Linking)
VI  - 14
IP  - 10
DP  - 2012 Oct
TI  - Identification of a novel role of ESAT-6-dependent miR-155 induction during 
      infection of macrophages with Mycobacterium tuberculosis.
PG  - 1620-31
LID - 10.1111/j.1462-5822.2012.01827.x [doi]
AB  - Mycobacterium tuberculosis (M.tb.) replicates in host macrophages to cause 
      tuberculosis. We have investigated the role of miRNAs in M.tb.-infected murine 
      RAW264.7 cells and bone marrow-derived macrophages (BMDMs), focusing on miR-155, 
      the most highly upregulated miRNA. We observed that miR-155 upregulation is 
      directly linked to the attenuation of expression of BTB and CNC homology 1 
      (Bach1) and SH2-containing inositol 5'-phosphatase (SHIP1). Bach1 is a 
      transcriptional repressor of haem oxygenase-1 (HO-1), whereas SHIP1 inhibits the 
      activation of the serine/threonine kinase AKT. We hypothesize that M.tb.-induced 
      miR-155 induction leads to repression of Bach1, which augments the expression of 
      HO-1, a documented activator of the M.tb. dormancy regulon. SHIP1 repression 
      facilitates AKT activation, which is required for M.tb. survival. In addition, 
      M.tb.-induced miR-155 inhibits expression of cyclooxygenase-2 (Cox-2) and 
      interleukin-6 (Il-6), two modulators of the innate immune response. Importantly, 
      we observed that the virulence-associated secreted protein ESAT-6 plays a key 
      role in miR-155 induction and its subsequent effects on Bach1 and SHIP1 
      repression. Inhibition of miR-155 hindered survival of M.tb. in RAW264.7 and in 
      murine BMDMs. Thus, our results offer new insights into the role of miRNAs in 
      modulation of the host innate immune response by M.tb. for its own benefit.
CI  - (c) 2012 Blackwell Publishing Ltd.
FAU - Kumar, Ranjeet
AU  - Kumar R
AD  - Department of Chemistry, Bose Institute, Kolkata, India.
FAU - Halder, Priyanka
AU  - Halder P
FAU - Sahu, Sanjaya K
AU  - Sahu SK
FAU - Kumar, Manish
AU  - Kumar M
FAU - Kumari, Mandavi
AU  - Kumari M
FAU - Jana, Kuladip
AU  - Jana K
FAU - Ghosh, Zhumur
AU  - Ghosh Z
FAU - Sharma, Pawan
AU  - Sharma P
FAU - Kundu, Manikuntala
AU  - Kundu M
FAU - Basu, Joyoti
AU  - Basu J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120711
PL  - India
TA  - Cell Microbiol
JT  - Cellular microbiology
JID - 100883691
RN  - 0 (Antigens, Bacterial)
RN  - 0 (Bach1 protein, mouse)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Basic-Leucine Zipper Transcription Factors)
RN  - 0 (ESAT-6 protein, Mycobacterium tuberculosis)
RN  - 0 (MicroRNAs)
RN  - 0 (Mirn155 microRNA, mouse)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
RN  - EC 3.1.3.56 (Inositol Polyphosphate 5-Phosphatases)
RN  - EC 3.1.3.86 (Inpp5d protein, mouse)
RN  - EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases)
SB  - IM
MH  - Animals
MH  - Antigens, Bacterial/*metabolism
MH  - Bacterial Proteins/*metabolism
MH  - Basic-Leucine Zipper Transcription Factors/biosynthesis
MH  - Cells, Cultured
MH  - Gene Expression Profiling
MH  - *Host-Pathogen Interactions
MH  - Immune Evasion
MH  - Inositol Polyphosphate 5-Phosphatases
MH  - Macrophages/*immunology/*microbiology
MH  - Mice
MH  - MicroRNAs/*biosynthesis
MH  - Microbial Viability
MH  - Mycobacterium tuberculosis/*immunology
MH  - Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases
MH  - Phosphoric Monoester Hydrolases/biosynthesis
EDAT- 2012/06/21 06:00
MHDA- 2013/01/29 06:00
CRDT- 2012/06/21 06:00
PHST- 2012/01/14 00:00 [received]
PHST- 2012/06/06 00:00 [revised]
PHST- 2012/06/11 00:00 [accepted]
PHST- 2012/06/21 06:00 [entrez]
PHST- 2012/06/21 06:00 [pubmed]
PHST- 2013/01/29 06:00 [medline]
AID - 10.1111/j.1462-5822.2012.01827.x [doi]
PST - ppublish
SO  - Cell Microbiol. 2012 Oct;14(10):1620-31. doi: 10.1111/j.1462-5822.2012.01827.x. 
      Epub 2012 Jul 11.