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Article ; Online: Interaction of Mycobacteria With Host Cell Inflammasomes.

Rastogi, Shivangi / Briken, Volker

2022 Volume 13, Page(s) 791136

Abstract: The inflammasome complex is important for host defense against intracellular bacterial infections. ...

Abstract	The inflammasome complex is important for host defense against intracellular bacterial infections.
MeSH term(s)	Humans ; Inflammasomes/metabolism ; Interleukin-1beta/metabolism ; Macrophages/metabolism ; Mycobacterium Infections/metabolism ; Mycobacterium tuberculosis ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism
Chemical Substances	Inflammasomes ; Interleukin-1beta ; NLR Family, Pyrin Domain-Containing 3 Protein
Language	English
Publishing date	2022-02-14
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2022.791136
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Article ; Online: Putting the p(hosphor) in pyroptosis.

Rastogi, Shivangi / Evavold, Charles L / Briken, Volker

Cell host & microbe

2022 Volume 30, Issue 12, Page(s) 1650–1652

Abstract: A recent study in Science found Mycobacterium tuberculosis inhibits pyroptosis of the host cell by secreting a phosphatase (PtpB). PtpB targets the plasma membrane to dephosphorylate PI4P and PI(4,5) ... ...

Abstract	A recent study in Science found Mycobacterium tuberculosis inhibits pyroptosis of the host cell by secreting a phosphatase (PtpB). PtpB targets the plasma membrane to dephosphorylate PI4P and PI(4,5)P
MeSH term(s)	Mice ; Animals ; Pyroptosis ; Phosphate-Binding Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Cell Membrane/metabolism ; Mycobacterium tuberculosis/metabolism
Chemical Substances	Phosphate-Binding Proteins ; Intracellular Signaling Peptides and Proteins
Language	English
Publishing date	2022-12-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2022.11.010
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Article ; Online: Mycobacterium tuberculosis inhibits the NLRP3 inflammasome activation via its phosphokinase PknF.

Rastogi, Shivangi / Ellinwood, Sarah / Augenstreich, Jacques / Mayer-Barber, Katrin D / Briken, Volker

PLoS pathogens

2021 Volume 17, Issue 7, Page(s) e1009712

Abstract: Mycobacterium tuberculosis (Mtb) has evolved to evade host innate immunity by interfering with macrophage functions. Interleukin-1β (IL-1β) is secreted by macrophages after the activation of the inflammasome complex and is crucial for host defense ... ...

Abstract	Mycobacterium tuberculosis (Mtb) has evolved to evade host innate immunity by interfering with macrophage functions. Interleukin-1β (IL-1β) is secreted by macrophages after the activation of the inflammasome complex and is crucial for host defense against Mtb infections. We have previously shown that Mtb is able to inhibit activation of the AIM2 inflammasome and subsequent pyroptosis. Here we show that Mtb is also able to inhibit host cell NLRP3 inflammasome activation and pyroptosis. We identified the serine/threonine kinase PknF as one protein of Mtb involved in the NLRP3 inflammasome inhibition, since the pknF deletion mutant of Mtb induces increased production of IL-1β in bone marrow-derived macrophages (BMDMs). The increased production of IL-1β was dependent on NLRP3, the adaptor protein ASC and the protease caspase-1, as revealed by studies performed in gene-deficient BMDMs. Additionally, infection of BMDMs with the pknF deletion mutant resulted in increased pyroptosis, while the IL-6 production remained unchanged compared to Mtb-infected cells, suggesting that the mutant did not affect the priming step of inflammasome activation. In contrast, the activation step was affected since potassium efflux, chloride efflux and the generation of reactive oxygen species played a significant role in inflammasome activation and subsequent pyroptosis mediated by the Mtb pknF mutant strain. In conclusion, we reveal here that the serine/threonine kinase PknF of Mtb plays an important role in innate immune evasion through inhibition of the NLRP3 inflammasome.
MeSH term(s)	Animals ; Host-Pathogen Interactions/immunology ; Immune Evasion/immunology ; Inflammasomes/immunology ; Mice ; Mycobacterium tuberculosis/immunology ; Mycobacterium tuberculosis/metabolism ; NLR Family, Pyrin Domain-Containing 3 Protein/immunology ; Protein Serine-Threonine Kinases/immunology ; Protein Serine-Threonine Kinases/metabolism ; Tuberculosis/immunology ; Tuberculosis/metabolism
Chemical Substances	Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; PknF protein, Mycobacterium tuberculosis (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2021-07-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1009712
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Article ; Online: Use of an adipocyte model to study the transcriptional adaptation of Mycobacterium tuberculosis to store and degrade host fat.

Rastogi, Shivangi / Agarwal, Pooja / Krishnan, Manju Y

International journal of mycobacteriology

2015 Volume 5, Issue 1, Page(s) 92–98

Abstract: During its persistence in the infected host, Mycobacterium tuberculosis (Mtb) accumulates host-derived fatty acids in intracytoplasmic lipid inclusions as triacylglycerols which serve primarily as carbon and energy reserves. The Mtb genome codes for more ...

Abstract	During its persistence in the infected host, Mycobacterium tuberculosis (Mtb) accumulates host-derived fatty acids in intracytoplasmic lipid inclusions as triacylglycerols which serve primarily as carbon and energy reserves. The Mtb genome codes for more than 15 triacylglycerol synthases, 24 lipase/esterases, and seven cutinase-like proteins. Hence, we looked at the expression of the corresponding genes in intracellular bacilli persisting amidst the host triacylglycerols. We used the Mtb infected murine adipocyte model to ensure persistence and transcripts were quantified using real-time reverse transcriptase polymerase chain reaction. Dormancy and glyoxylate metabolism was confirmed by the upregulated expression of dosR and icl, respectively, by intra-adipocyte bacilli compared with in vitro growing bacilli. The study revealed that tgs1, tgs2, Rv3371, and mycolyltransferase Ag85A are the predominant triacylglycerol synthases, while lipF, lipH, lipJ, lipK, lipN, lipV, lipX, lipY, culp5, culp7, and culp6 are the predominant lipases/esterases used by Mtb for the storage and degradation of host-derived fat. Moreover, it was observed that many of these enzymes are used by Mtb during active replication rather than during nonreplicating persistence, indicating their probable function in cell wall synthesis.
MeSH term(s)	Adaptation, Physiological/genetics ; Adipocytes/metabolism ; Adipocytes/microbiology ; Animals ; Bacterial Proteins/genetics ; Disease Models, Animal ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Glyoxylates/metabolism ; Host-Pathogen Interactions ; Lipase/metabolism ; Lipid Metabolism/genetics ; Macrophages/microbiology ; Mice ; Mycobacterium tuberculosis/enzymology ; Mycobacterium tuberculosis/genetics ; Mycobacterium tuberculosis/growth & development ; Mycobacterium tuberculosis/metabolism ; Protein Kinases/genetics ; Real-Time Polymerase Chain Reaction
Chemical Substances	Bacterial Proteins ; DosR protein, Mycobacterium tuberculosis ; Glyoxylates ; Protein Kinases (EC 2.7.-) ; Lipase (EC 3.1.1.3) ; glyoxylic acid (JQ39C92HH6)
Language	English
Publishing date	2015-10-29
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2212-554X
ISSN (online)	2212-554X
DOI	10.1016/j.ijmyco.2015.10.003
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Article: Pillar[6]MaxQ: A Potent Supramolecular Host for

Brockett, Adam T / Xue, Weijian / King, David / Deng, Chun-Lin / Zhai, Canjia / Shuster, Michael / Rastogi, Shivangi / Briken, Volker / Roesch, Matthew R / Isaacs, Lyle

Chem

2022 Volume 9, Issue 4, Page(s) 881–900

Abstract: Pillar[6]MaxQ (P6AS) functions as ... ...

Abstract	Pillar[6]MaxQ (P6AS) functions as an
Language	English
Publishing date	2022-12-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2869032-1
ISSN	2451-9294 ; 2451-9294 ; 2451-9308
ISSN (online)	2451-9294
ISSN	2451-9294 ; 2451-9308
DOI	10.1016/j.chempr.2022.11.019
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Article ; Online: Cdc15 Phosphorylates the C-terminal Domain of RNA Polymerase II for Transcription during Mitosis.

Singh, Amit Kumar / Rastogi, Shivangi / Shukla, Harish / Asalam, Mohd / Rath, Srikanta Kumar / Akhtar, Md Sohail

The Journal of biological chemistry

2017 Volume 292, Issue 13, Page(s) 5507–5518

Abstract: In eukaryotes, the basal transcription in interphase is orchestrated through the regulation by kinases (Kin28, Bur1, and Ctk1) and phosphatases (Ssu72, Rtr1, and Fcp1), which act through the post-translational modification of the C-terminal domain (CTD) ... ...

Abstract	In eukaryotes, the basal transcription in interphase is orchestrated through the regulation by kinases (Kin28, Bur1, and Ctk1) and phosphatases (Ssu72, Rtr1, and Fcp1), which act through the post-translational modification of the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. The CTD comprises the repeated Tyr-Ser-Pro-Thr-Ser-Pro-Ser motif with potential epigenetic modification sites. Despite the observation of transcription and periodic expression of genes during mitosis with entailing CTD phosphorylation and dephosphorylation, the associated CTD specific kinase(s) and its role in transcription remains unknown. Here we have identified Cdc15 as a potential kinase phosphorylating Ser-2 and Ser-5 of CTD for transcription during mitosis in the budding yeast. The phosphorylation of CTD by Cdc15 is independent of any prior Ser phosphorylation(s). The inactivation of Cdc15 causes reduction of global CTD phosphorylation during mitosis and affects the expression of genes whose transcript levels peak during mitosis. Cdc15 also influences the complete transcription of clb2 gene and phosphorylates Ser-5 at the promoter and Ser-2 toward the 3' end of the gene. The observation that Cdc15 could phosphorylate Ser-5, as well as Ser-2, during transcription in mitosis is in contrast to the phosphorylation marks put by the kinases in interphase (G
MeSH term(s)	Amino Acid Motifs ; Binding Sites ; Cell Cycle Proteins/metabolism ; Cyclin B/genetics ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation, Fungal ; Mitosis/genetics ; Phosphorylation ; Protein Domains ; Protein Processing, Post-Translational/genetics ; RNA Polymerase II/genetics ; RNA Polymerase II/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Transcription, Genetic
Chemical Substances	CDC15 protein ; CLB2 protein, S cerevisiae ; Cell Cycle Proteins ; Cyclin B ; Saccharomyces cerevisiae Proteins ; RNA Polymerase II (EC 2.7.7.-) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2017-02-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M116.761056
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Article ; Online: Down-regulation of PE11, a cell wall associated esterase, enhances the biofilm growth of Mycobacterium tuberculosis and reduces cell wall virulence lipid levels.

Rastogi, Shivangi / Singh, Amit Kumar / Pant, Garima / Mitra, Kalyan / Sashidhara, Koneni V / Krishnan, Manju Y

Microbiology (Reading, England)

2017 Volume 163, Issue 1, Page(s) 52–61

Abstract: PE11 (Rv1169c or LipX) is a cell wall associated esterase/lipase of Mycobacterium tuberculosis (Mtb). Evidences suggest that PE11 is expressed by Mtb both in vitro and in vivo. Previous studies have shown that PE11 leads to modification in cell wall ... ...

Abstract	PE11 (Rv1169c or LipX) is a cell wall associated esterase/lipase of Mycobacterium tuberculosis (Mtb). Evidences suggest that PE11 is expressed by Mtb both in vitro and in vivo. Previous studies have shown that PE11 leads to modification in cell wall lipid content and enhanced virulence when expressed in the non-pathogenic surrogate Mycobacterium smegmatis. Since cell wall lipids often play different roles in pathogenic and non-pathogenic mycobacteria, we investigated the role of PE11 in its host, Mtb. Mtb with lowered expression of PE11 (PE11 knock-down) displayed significant changes in colony morphology and cell wall lipid profile, confirming the role of PE11 in cell wall architecture. In addition, the levels of phthiocerol dimycocerosates, a cell wall virulence factor, were decreased. Levels of trehalose esters and free mycolic acids were increased. In contrast to M. smegmatis expressing Mtb PE11, a role reversal was observed in Mtb with respect to pellicle/biofilm formation. The PE11 knock-down Mtb strain showed significantly enhanced aggregation and early biofilm growth in detergent-free medium, compared to the wild-type. Knock-down strain also showed nearly 27-fold up-regulation of a fibronectin attachment protein (Rv1759c), linking biofilm growth with over-expression of bacterial proteins that help in aggregation and/or binding to host extracellular matrix. The knock-down also resulted in poor virulence of Mtb in PMA (phorbol 12-myristate 13-acetate) treated and PMA+IFN-γ treated THP-1 macrophages. Therefore, the study not only links PE11 to cell wall virulence lipids but also reveals the involvement of this cell wall associated esterase in down-regulation of biofilm in Mtb.
MeSH term(s)	Bacterial Proteins/biosynthesis ; Bacterial Proteins/genetics ; Biofilms/growth & development ; Cell Line ; Cell Wall/metabolism ; Esterases/biosynthesis ; Esterases/genetics ; Fibronectins/metabolism ; Gene Knockout Techniques ; Humans ; Lipids/biosynthesis ; Macrophages/microbiology ; Membrane Lipids/metabolism ; Mycobacterium smegmatis/genetics ; Mycobacterium smegmatis/pathogenicity ; Mycobacterium tuberculosis/genetics ; Mycobacterium tuberculosis/growth & development ; Mycobacterium tuberculosis/pathogenicity ; Mycolic Acids/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Trehalose/metabolism ; Virulence Factors/metabolism
Chemical Substances	Bacterial Proteins ; Fibronectins ; Lipids ; Membrane Lipids ; Mycolic Acids ; Virulence Factors ; phthiocerol dimycocerosate (63642-22-8) ; Trehalose (B8WCK70T7I) ; Esterases (EC 3.1.-) ; PE11 protein, Mycobacterium tuberculosis (EC 3.1.-) ; Tetradecanoylphorbol Acetate (NI40JAQ945)
Language	English
Publishing date	2017-02-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.000417
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Article ; Online: The diacylglycerol acyltransferase Rv3371 of Mycobacterium tuberculosis is required for growth arrest and involved in stress-induced cell wall alterations.

Rastogi, Shivangi / Singh, Amit Kumar / Chandra, Gyan / Kushwaha, Pragati / Pant, Garima / Singh, Kavita / Mitra, Kalyan / Sashidhara, Koneni V / Krishnan, Manju Y

Tuberculosis (Edinburgh, Scotland)

2017 Volume 104, Page(s) 8–19

Abstract: Triacylglycerol (TAG) is important to mycobacteria both as cell envelope component and energy reservoir. Mycobacterium tuberculosis (Mtb) genome encodes at least 15 putative TAG synthase (tgs)s. We report that one of these genes, Rv3371, specific to ... ...

Abstract	Triacylglycerol (TAG) is important to mycobacteria both as cell envelope component and energy reservoir. Mycobacterium tuberculosis (Mtb) genome encodes at least 15 putative TAG synthase (tgs)s. We report that one of these genes, Rv3371, specific to pathogenic mycobacteria, when expressed in M. smegmatis leads to modifications in colony morphotype, bacterial architecture, cell surface properties and elevated TAG levels. Rv3371 was found to largely localize in the cell membrane. The Rv3371 promoter is minimally active during exponential growth in vitro, however, is up-regulated under stationary phase, hypoxia, nutrient starvation, nitrosative stress, low iron, in IFN-γ activated macrophages and infected mice. The low iron-induced expression of Rv3371 is likely due to the de-repression by Rv1404, which is probably activated by ideR. An Rv3371 deletion mutant of Mtb showed impaired non-replicating persistence in vitro and altered sensitivity to anti-mycobacterial drugs. In low iron medium, the Rv3371 deletion mutant showed reduced formation of TAG containing extracellular vesicles. Therefore Rv3371 is likely involved in Mtb growth arrest and cell wall alterations during persistence.
Language	English
Publishing date	2017-05
Publishing country	Scotland
Document type	Journal Article
ZDB-ID	2046804-0
ISSN	1873-281X ; 1472-9792
ISSN (online)	1873-281X
ISSN	1472-9792
DOI	10.1016/j.tube.2017.02.001
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Article ; Online: Isocitrate lyase of Mycobacterium tuberculosis is inhibited by quercetin through binding at N-terminus.

Shukla, Harish / Kumar, Vikash / Singh, Amit Kumar / Rastogi, Shivangi / Khan, Shaheb Raj / Siddiqi, Mohammad Imran / Krishnan, Manju Yasoda / Akhtar, Md Sohail

International journal of biological macromolecules

2015 Volume 78, Page(s) 137–141

Abstract: Combating tuberculosis requires new therapeutic strategies that not only target the actively dividing bacilli but also the dormant bacilli during persistent infection. Isocitrate lyase (ICL) is a key enzyme of the glyoxylate shunt, crucial for the ... ...

Abstract	Combating tuberculosis requires new therapeutic strategies that not only target the actively dividing bacilli but also the dormant bacilli during persistent infection. Isocitrate lyase (ICL) is a key enzyme of the glyoxylate shunt, crucial for the survival of bacteria in macrophages and mice. MtbICL is considered as one of the potential and attractive drug targets against persistent infection. We report the inhibition of MtbICL by quercetin with IC50 of 3.57 μM. In addition, quercetin strongly inhibited the growth of Mtb H37Rv utilizing acetate, rather than glucose as the sole carbon source, suggesting the inhibition of glyoxylate shunt. Quercetin binds at the N-terminus of MtbICL (Kd - 6.68 μM).
MeSH term(s)	Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Isocitrate Lyase/antagonists & inhibitors ; Isocitrate Lyase/chemistry ; Models, Molecular ; Molecular Conformation ; Mycobacterium tuberculosis/enzymology ; Protein Binding ; Protein Interaction Domains and Motifs ; Quercetin/chemistry ; Quercetin/pharmacology
Chemical Substances	Enzyme Inhibitors ; Quercetin (9IKM0I5T1E) ; Isocitrate Lyase (EC 4.1.3.1)
Language	English
Publishing date	2015
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2015.04.005
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