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Article ; Online: Transposon sequencing reveals metabolic pathways essential for Mycobacterium tuberculosis infection.

Block, Alisha M / Wiegert, Parker C / Namugenyi, Sarah B / Tischler, Anna D

2024 Volume 20, Issue 3, Page(s) e1011663

Abstract: New drugs are needed to shorten and simplify treatment of tuberculosis caused by Mycobacterium tuberculosis. Metabolic pathways that M. tuberculosis requires for growth or survival during infection represent potential targets for anti-tubercular drug ... ...

Abstract	New drugs are needed to shorten and simplify treatment of tuberculosis caused by Mycobacterium tuberculosis. Metabolic pathways that M. tuberculosis requires for growth or survival during infection represent potential targets for anti-tubercular drug development. Genes and metabolic pathways essential for M. tuberculosis growth in standard laboratory culture conditions have been defined by genome-wide genetic screens. However, whether M. tuberculosis requires these essential genes during infection has not been comprehensively explored because mutant strains cannot be generated using standard methods. Here we show that M. tuberculosis requires the phenylalanine (Phe) and de novo purine and thiamine biosynthetic pathways for mammalian infection. We used a defined collection of M. tuberculosis transposon (Tn) mutants in essential genes, which we generated using a custom nutrient-rich medium, and transposon sequencing (Tn-seq) to identify multiple central metabolic pathways required for fitness in a mouse infection model. We confirmed by individual retesting and complementation that mutations in pheA (Phe biosynthesis) or purF (purine and thiamine biosynthesis) cause death of M. tuberculosis in the absence of nutrient supplementation in vitro and strong attenuation in infected mice. Our findings show that Tn-seq with defined Tn mutant pools can be used to identify M. tuberculosis genes required during mouse lung infection. Our results also demonstrate that M. tuberculosis requires Phe and purine/thiamine biosynthesis for survival in the host, implicating these metabolic pathways as prime targets for the development of new antibiotics to combat tuberculosis.
MeSH term(s)	Animals ; Mice ; Tuberculosis/genetics ; Mutation ; Mycobacterium tuberculosis/genetics ; Metabolic Networks and Pathways/genetics ; Thiamine ; Purines ; Mammals
Chemical Substances	Thiamine (X66NSO3N35) ; Purines
Language	English
Publishing date	2024-03-18
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1011663
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Microbial Degradation of Azo Dyes: Approaches and Prospects for a Hazard-Free Conversion by Microorganisms.

Ngo, Anna Christina R / Tischler, Dirk

International journal of environmental research and public health

2022 Volume 19, Issue 8

Abstract: Azo dyes have become a staple in various industries, as colors play an important role in consumer choices. However, these dyes pose various health and environmental risks. Although different wastewater treatments are available, the search for more eco- ... ...

Abstract	Azo dyes have become a staple in various industries, as colors play an important role in consumer choices. However, these dyes pose various health and environmental risks. Although different wastewater treatments are available, the search for more eco-friendly options persists. Bioremediation utilizing microorganisms has been of great interest to researchers and industries, as the transition toward greener solutions has become more in demand through the years. This review tackles the health and environmental repercussions of azo dyes and its metabolites, available biological approaches to eliminate such dyes from the environment with a focus on the use of different microorganisms, enzymes that are involved in the degradation of azo dyes, and recent trends that could be applied for the treatment of azo dyes.
MeSH term(s)	Azo Compounds/metabolism ; Biodegradation, Environmental ; Coloring Agents
Chemical Substances	Azo Compounds ; Coloring Agents
Language	English
Publishing date	2022-04-14
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2175195-X
ISSN	1660-4601 ; 1661-7827
ISSN (online)	1660-4601
ISSN	1661-7827
DOI	10.3390/ijerph19084740
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Article ; Online: Mycobacterium tuberculosis Requires the Outer Membrane Lipid Phthiocerol Dimycocerosate for Starvation-Induced Antibiotic Tolerance.

Block, Alisha M / Namugenyi, Sarah B / Palani, Nagendra P / Brokaw, Alyssa M / Zhang, Leanne / Beckman, Kenneth B / Tischler, Anna D

mSystems

2023 Volume 8, Issue 1, Page(s) e0069922

Abstract: Tolerance of Mycobacterium tuberculosis to antibiotics contributes to the long duration of tuberculosis (TB) treatment and the emergence of drug-resistant strains. M. tuberculosis drug tolerance is induced by nutrient restriction, but the genetic ... ...

Abstract	Tolerance of Mycobacterium tuberculosis to antibiotics contributes to the long duration of tuberculosis (TB) treatment and the emergence of drug-resistant strains. M. tuberculosis drug tolerance is induced by nutrient restriction, but the genetic determinants that promote antibiotic tolerance triggered by nutrient limitation have not been comprehensively identified. Here, we show that M. tuberculosis requires production of the outer membrane lipid phthiocerol dimycocerosate (PDIM) to tolerate antibiotics under nutrient-limited conditions. We developed an arrayed transposon (Tn) mutant library in M. tuberculosis Erdman and used orthogonal pooling and transposon sequencing (Tn-seq) to map the locations of individual mutants in the library. We screened a subset of the library (~1,000 mutants) by Tn-seq and identified 32 and 102 Tn mutants with altered tolerance to antibiotics under stationary-phase and phosphate-starved conditions, respectively. Two mutants recovered from the arrayed library,
MeSH term(s)	Humans ; Membrane Lipids/chemistry ; Mycobacterium tuberculosis/drug effects ; Mycobacterium tuberculosis/genetics ; Tuberculosis ; Drug Resistance, Bacterial
Chemical Substances	Membrane Lipids ; phthiocerol dimycocerosate (63642-22-8)
Language	English
Publishing date	2023-01-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2379-5077
ISSN (online)	2379-5077
DOI	10.1128/msystems.00699-22
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Article ; Online: Mycobacterium tuberculosis Requires Regulation of ESX-5 Secretion for Virulence in Irgm1-Deficient Mice.

Elliott, Sarah R / White, Dylan W / Tischler, Anna D

Infection and immunity

2019 Volume 87, Issue 2

Abstract: ... ...

Abstract	The
MeSH term(s)	Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacterial Secretion Systems/genetics ; GTP-Binding Proteins/deficiency ; Gene Expression Regulation, Bacterial ; Mice ; Mice, Inbred C57BL ; Mycobacterium tuberculosis/immunology ; Mycobacterium tuberculosis/pathogenicity ; Tuberculosis/immunology ; Tuberculosis/microbiology ; Virulence/physiology ; Virulence Factors/metabolism
Chemical Substances	Bacterial Proteins ; Bacterial Secretion Systems ; ESX-5 protein, Mycobacterium tuberculosis ; Ifi1 protein, mouse ; Virulence Factors ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2019-01-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.00660-18
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Article ; Online: Toxin secretion and trafficking by Mycobacterium tuberculosis.

Pajuelo, David / Tak, Uday / Zhang, Lei / Danilchanka, Olga / Tischler, Anna D / Niederweis, Michael

Nature communications

2021 Volume 12, Issue 1, Page(s) 6592

Abstract: The tuberculosis necrotizing toxin (TNT) is the major cytotoxicity factor of Mycobacterium tuberculosis (Mtb) in macrophages. TNT is the C-terminal domain of the outer membrane protein CpnT and gains access to the cytosol to kill macrophages infected ... ...

Abstract	The tuberculosis necrotizing toxin (TNT) is the major cytotoxicity factor of Mycobacterium tuberculosis (Mtb) in macrophages. TNT is the C-terminal domain of the outer membrane protein CpnT and gains access to the cytosol to kill macrophages infected with Mtb. However, molecular mechanisms of TNT secretion and trafficking are largely unknown. A comprehensive analysis of the five type VII secretion systems of Mtb revealed that the ESX-4 system is required for export of CpnT and surface accessibility of TNT. Furthermore, the ESX-2 and ESX-4 systems are required for permeabilization of the phagosomal membrane in addition to the ESX-1 system. Thus, these three ESX systems need to act in concert to enable trafficking of TNT into the cytosol of Mtb-infected macrophages. These discoveries establish new molecular roles for the two previously uncharacterized type VII secretion systems ESX-2 and ESX-4 and reveal an intricate link between toxin secretion and phagosomal permeabilization by Mtb.
MeSH term(s)	Antigens, Bacterial/metabolism ; Bacterial Outer Membrane Proteins ; Bacterial Proteins ; Bacterial Toxins/metabolism ; Cell Death ; Macrophages/metabolism ; Mycobacterium tuberculosis/metabolism ; Phagosomes/metabolism ; Toxins, Biological/metabolism ; Type VII Secretion Systems
Chemical Substances	Antigens, Bacterial ; Bacterial Outer Membrane Proteins ; Bacterial Proteins ; Bacterial Toxins ; ESAT-6 protein, Mycobacterium tuberculosis ; Rv3903 protein, Mycobacterium tuberculosis ; Toxins, Biological ; Type VII Secretion Systems
Language	English
Publishing date	2021-11-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-26925-1
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Article ; Online: Phosphate responsive regulation provides insights for ESX-5 function in Mycobacterium tuberculosis.

Elliott, Sarah R / Tischler, Anna D

Current genetics

2016 Volume 62, Issue 4, Page(s) 759–763

Abstract: Pathogenic microbes commonly respond to environmental cues in the host by activating specialized protein secretion systems. Mycobacterium tuberculosis uses the specialized Type VII ESX protein secretion systems to transport a subset of effector proteins. ...

Abstract	Pathogenic microbes commonly respond to environmental cues in the host by activating specialized protein secretion systems. Mycobacterium tuberculosis uses the specialized Type VII ESX protein secretion systems to transport a subset of effector proteins. The ESX-5 secretion system is involved in virulence, but both the mechanism of regulation and activating signal were unknown. Our work, reviewed here, has established that the phosphate sensing Pst/SenX3-RegX3 system directly activates ESX-5 secretion in response to phosphate limitation, a relevant environmental signal likely encountered by M. tuberculosis in the host. This review focuses on how elucidation of the ESX-5 regulatory network provides insight into its biological roles, which may include both phosphate acquisition and pathogenesis.
MeSH term(s)	Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacterial Secretion Systems ; Host-Pathogen Interactions ; Humans ; Mycobacterium tuberculosis/genetics ; Mycobacterium tuberculosis/immunology ; Mycobacterium tuberculosis/metabolism ; Phosphates/metabolism ; Signal Transduction ; Tuberculosis/immunology ; Tuberculosis/microbiology
Chemical Substances	Bacterial Proteins ; Bacterial Secretion Systems ; Phosphates
Language	English
Publishing date	2016-11
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	282876-5
ISSN	1432-0983 ; 0172-8083
ISSN (online)	1432-0983
ISSN	0172-8083
DOI	10.1007/s00294-016-0604-4
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Zs.A 2586: Show issues

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Article ; Online: Phosphate starvation: a novel signal that triggers ESX-5 secretion in Mycobacterium tuberculosis.

Elliott, Sarah R / Tischler, Anna D

Molecular microbiology

2016 Volume 100, Issue 3, Page(s) 510–526

Abstract: Mycobacterium tuberculosis uses the Type VII ESX secretion systems to transport proteins across its complex cell wall. ESX-5 has been implicated in M. tuberculosis virulence, but the regulatory mechanisms controlling ESX-5 secretion were unknown. Here we ...

Abstract	Mycobacterium tuberculosis uses the Type VII ESX secretion systems to transport proteins across its complex cell wall. ESX-5 has been implicated in M. tuberculosis virulence, but the regulatory mechanisms controlling ESX-5 secretion were unknown. Here we uncover a link between ESX-5 and the Pst/SenX3-RegX3 system that controls gene expression in response to phosphate availability. The DNA-binding response regulator RegX3 is normally activated by phosphate limitation. Deletion of pstA1, which encodes a Pst phosphate uptake system component, causes constitutive activation of RegX3. A ΔpstA1 mutant exhibited RegX3-dependent overexpression of esx-5 genes and hyper-secretion of the ESX-5 substrates EsxN and PPE41 when the bacteria were grown in phosphate-rich medium. In wild-type M. tuberculosis, phosphate limitation activated esx-5 transcription and secretion of both EsxN and PPE41, and this response required RegX3. Electrophoretic mobility shift assays revealed that RegX3 binds directly to a promoter within the esx-5 locus. Remarkably, phosphate limitation also induced secretion of EsxB, an effector of the virulence-associated ESX-1 secretion system, though this induction was RegX3 independent. Our work demonstrates that the Pst/SenX3-RegX3 system directly regulates ESX-5 secretion at the transcriptional level in response to phosphate availability and defines phosphate limitation as an environmental signal that activates ESX-5 secretion.
MeSH term(s)	ATP-Binding Cassette Transporters/genetics ; Bacterial Proteins/biosynthesis ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacterial Proteins/secretion ; Binding Sites/genetics ; Electrophoretic Mobility Shift Assay ; Enzyme Activation/physiology ; Gene Expression Regulation, Bacterial/genetics ; Mycobacterium tuberculosis/genetics ; Mycobacterium tuberculosis/metabolism ; Mycobacterium tuberculosis/pathogenicity ; Phosphates/metabolism ; Phosphotransferases/metabolism ; Promoter Regions, Genetic/genetics ; Protein Binding/physiology ; Type VII Secretion Systems/genetics ; Type VII Secretion Systems/metabolism ; Virulence Factors/biosynthesis ; Virulence Factors/genetics ; Virulence Factors/metabolism
Chemical Substances	Bacterial Proteins ; ESX-5 protein, Mycobacterium tuberculosis ; Phosphates ; RegX3 protein, Mycobacterium ; Type VII Secretion Systems ; Virulence Factors ; phosphate-specific transport protein A, bacteria ; Phosphotransferases (EC 2.7.-) ; SenX3 protein, Mycobacterium (EC 2.7.3.-)
Language	English
Publishing date	2016-05
Publishing country	England
Document type	Journal Article
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/mmi.13332
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Zs.A 2502: Show issues

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Article ; Online: Toxin secretion and trafficking by Mycobacterium tuberculosis

David Pajuelo / Uday Tak / Lei Zhang / Olga Danilchanka / Anna D. Tischler / Michael Niederweis

Nature Communications, Vol 12, Iss 1, Pp 1-

2021 Volume 13

Abstract: The tuberculosis necrotizing toxin (TNT) is the major cytotoxicity factor of M. tuberculosis (Mtb). Mtb possesses five type VII secretion systems (ESX). Pajuelo et al. show that the ESX-4 system is required for TNT secretion and that ESX-2 and ESX-4 ... ...

Abstract	The tuberculosis necrotizing toxin (TNT) is the major cytotoxicity factor of M. tuberculosis (Mtb). Mtb possesses five type VII secretion systems (ESX). Pajuelo et al. show that the ESX-4 system is required for TNT secretion and that ESX-2 and ESX-4 systems work in concert with ESX-1 to permeabilize the phagosomal membrane and enable trafficking of TNT into the cytoplasm of macrophages infected with Mtb.
Keywords	Science ; Q
Language	English
Publishing date	2021-11-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article ; Online: Recombinant Pichinde viral vector expressing tuberculosis antigens elicits strong T cell responses and protection in mice.

Kirk, Natalie M / Huang, Qinfeng / Vrba, Sophia / Rahman, Mizanur / Block, Alisha M / Murphy, Hannah / White, Dylan W / Namugenyi, Sarah B / Ly, Hinh / Tischler, Anna D / Liang, Yuying

Frontiers in immunology

2023 Volume 14, Page(s) 1127515

Abstract: Introduction: Tuberculosis (TB) caused by : Methods: Using this tri-segmented PICV vector (rP18tri), we have generated viral vectored TB vaccines (TBvac-1, TBvac-2, and TBvac-10) encoding several known TB immunogens (Ag85B, EsxH, and ESAT-6/EsxA). A ... ...

Abstract	Introduction: Tuberculosis (TB) caused by Methods: Using this tri-segmented PICV vector (rP18tri), we have generated viral vectored TB vaccines (TBvac-1, TBvac-2, and TBvac-10) encoding several known TB immunogens (Ag85B, EsxH, and ESAT-6/EsxA). A P2A linker sequence was used to allow for the expression of two proteins from one open-reading-frame (ORF) on the viral RNA segments. The immunogenicity of TBvac-2 and TBvac-10 and the protective efficacy of TBvac-1 and TBvac-2 were evaluated in mice. Results: Both viral vectored vaccines elicited strong antigen-specific CD4 and CD8 T cells through intramuscular (IM) and intranasal (IN) routes as evaluated by MHC-I and MHC-II tetramer analyses, respectively. The IN inoculation route helped to elicit strong lung T cell responses. The vaccine-induced antigen-specific CD4 T cells are functional, expressing multiple cytokines as detected by intracellular cytokine staining. Finally, immunization with TBvac-1 or TBvac-2, both expressing the same trivalent antigens (Ag85B, EsxH, ESAT6/EsxA), reduced Conclusions: The novel PICV vector-based TB vaccine candidates can express more than two antigens
MeSH term(s)	Animals ; Humans ; Mice ; Antigens, Bacterial/genetics ; Antigens, Viral ; Bacterial Proteins/genetics ; Cytokines/metabolism ; Seroepidemiologic Studies ; Tuberculosis ; Tuberculosis Vaccines/genetics ; Vaccines, Synthetic/genetics ; T-Lymphocytes/immunology
Chemical Substances	Antigens, Bacterial ; Antigens, Viral ; Bacterial Proteins ; Cytokines ; Tuberculosis Vaccines ; Vaccines, Synthetic
Language	English
Publishing date	2023-02-08
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2023.1127515
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Article: Correction to: Draft genome sequence of

Kumaran, Selvapravin / Ngo, Anna Christina R / Schultes, Fabian Peter Josef / Tischler, Dirk

3 Biotech

2021 Volume 11, Issue 9, Page(s) 417

Abstract: This corrects the article DOI: 10.1007/s13205-020-2136-3.]. ...

Abstract	[This corrects the article DOI: 10.1007/s13205-020-2136-3.].
Language	English
Publishing date	2021-08-20
Publishing country	Germany
Document type	Published Erratum
ZDB-ID	2600522-0
ISSN	2190-5738 ; 2190-572X
ISSN (online)	2190-5738
ISSN	2190-572X
DOI	10.1007/s13205-021-02895-5
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