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9 results on '"Banerjee, Srijon Kaushik"'

2. The sensor kinase MtrB of Mycobacterium tuberculosis regulates hypoxic survival and establishment of infection

Author

Banerjee, Srijon Kaushik, primary, Lata, Suruchi, additional, Sharma, Arun Kumar, additional, Bagchi, Shreya, additional, Kumar, Manish, additional, Sahu, Sanjaya Kumar, additional, Sarkar, Debasree, additional, Gupta, Pushpa, additional, Jana, Kuladip, additional, Gupta, Umesh Datta, additional, Singh, Ramandeep, additional, Saha, Sudipto, additional, Basu, Joyoti, additional, and Kundu, Manikuntala, additional

Published
2019
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5. MicroRNA 26a (miR-26a)/KLF4 and CREB-C/EBP beta regulate innate immune signaling, the polarization of macrophages and the trafficking of Mycobacterium tuberculosis to lysosomes during infection

Author

Sahu, Sanjaya Kumar, Kumar, Manish, Chakraborty, Sohini, Banerjee, Srijon Kaushik, Kumar, Ranjeet, Gupta, Pushpa, Jana, Kuladip, Gupta, Umesh D., Ghosh, Zhumur, Kundu, Manikuntala, Basu, Joyoti, Sahu, Sanjaya Kumar, Kumar, Manish, Chakraborty, Sohini, Banerjee, Srijon Kaushik, Kumar, Ranjeet, Gupta, Pushpa, Jana, Kuladip, Gupta, Umesh D., Ghosh, Zhumur, Kundu, Manikuntala, and Basu, Joyoti

Abstract

For efficient clearance of Mycobacterium tuberculosis (Mtb), macrophages tilt towards M1 polarization leading to the activation of transcription factors associated with the production of antibacterial effector molecules such as nitric oxide (NO) and proinflammatory cytokines such as interleukin 1 beta (IL-1 beta) and tumor necrosis factor alpha (TNF-alpha). At the same time, resolution of inflammation is associated with M2 polarization with increased production of arginase and cytokines such as IL-10. The transcriptional and post-transcriptional mechanisms that govern the balance between M1 and M2 polarization, and bacteria-containing processes such as autophagy and trafficking of Mtb to lysosomes, are incompletely understood. Here we report for the first time, that the transcription factor KLF4 is targeted by microRNA-26a (miR-26a). During Mtb infection, downregulation of miR-26a (observed both ex vivo and in vivo) facilitates upregulation of KLF4 which in turn favors increased arginase and decreased iNOS activity. We further demonstrate that KLF4 prevents trafficking of Mtb to lysosomes. The CREB-C/EBP beta signaling axis also favors M2 polarization. Downregulation of miR-26a and upregulation of C/ebpbeta were observed both in infected macrophages as well as in infected mice. Knockdown of C/ebpbeta repressed the expression of selected M2 markers such as Il10 and Irf4 in infected macrophages. The importance of these pathways is substantiated by observations that expression of miR-26a mimic or knockdown of Klf4 or Creb or C/ebpbeta, attenuated the survival of Mtb in macrophages. Taken together, our results attribute crucial roles for the miR-26a/KLF4 and CREB-C/EBP beta signaling pathways in regulating the survival of Mtb in macrophages. These studies expand our understanding of how Mtb hijacks host signaling pathways to survive in macrophages, and open up new exploratory avenues for host-targeted interventions.

Published
2017
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6. MicroRNA 26a (miR-26a)/KLF4 and CREB-C/EBPβ regulate innate immune signaling, the polarization of macrophages and the trafficking of Mycobacterium tuberculosis to lysosomes during infection

Author

Sahu, Sanjaya Kumar, primary, Kumar, Manish, additional, Chakraborty, Sohini, additional, Banerjee, Srijon Kaushik, additional, Kumar, Ranjeet, additional, Gupta, Pushpa, additional, Jana, Kuladip, additional, Gupta, Umesh D., additional, Ghosh, Zhumur, additional, Kundu, Manikuntala, additional, and Basu, Joyoti, additional

Published
2017
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7. Targeting multiple response regulators of Mycobacterium tuberculosis augments the host immune response to infection

Author

Banerjee, Srijon Kaushik, primary, Kumar, Manish, additional, Alokam, Reshma, additional, Sharma, Arun Kumar, additional, Chatterjee, Ayan, additional, Kumar, Ranjeet, additional, Sahu, Sanjaya Kumar, additional, Jana, Kuladip, additional, Singh, Ramandeep, additional, Yogeeswari, Perumal, additional, Sriram, Dharmarajan, additional, Basu, Joyoti, additional, and Kundu, Manikuntala, additional

Published
2016
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9. Essential protein SepF of mycobacteria interacts with FtsZ and MurG to regulate cell growth and division.

Author

Gupta S, Banerjee SK, Chatterjee A, Sharma AK, Kundu M, and Basu J

Subjects
Bacterial Outer Membrane Proteins genetics, Bacterial Proteins genetics, Cytoskeletal Proteins genetics, Gene Expression Regulation, Bacterial, Mycobacterium smegmatis, Mycobacterium tuberculosis cytology, Mycobacterium tuberculosis genetics, N-Acetylglucosaminyltransferases genetics, Protein Binding, Bacterial Outer Membrane Proteins metabolism, Bacterial Proteins metabolism, Cell Division, Cytoskeletal Proteins metabolism, Mycobacterium tuberculosis enzymology, Mycobacterium tuberculosis growth & development, N-Acetylglucosaminyltransferases metabolism
Abstract

Coordinated bacterial cell septation and cell wall biosynthesis require formation of protein complexes at the sites of division and elongation, in a temporally controlled manner. The protein players in these complexes remain incompletely understood in mycobacteria. Using in vitro and in vivo assays, we showed that Rv2147c (or SepF) of Mycobacterium tuberculosis interacts with the principal driver of cytokinesis, FtsZ. SepF also interacts with itself both in vitro and in vivo. Amino acid residues 189A, 190K and 215F are required for FtsZ-SepF interaction, and are conserved across Gram-positive bacteria. Using Mycobacterium smegmatis as a surrogate system, we confirmed that sepFMSMEG is essential. Knockdown of SepF led to cell elongation, defective growth and failure of FtsZ to localize to the site of division, suggesting that SepF assists FtsZ localization at the site of division. Furthermore, SepF interacted with MurG, a peptidoglycan-synthesizing enzyme, both in vitro and in vivo, suggesting that SepF could serve as a link between cell division and peptidoglycan synthesis. SepF emerges as a newly identified essential component of the cell division complex in mycobacteria.

Published
2015
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