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Article ; Online: Emerging themes in SecA2-mediated protein export.

Feltcher, Meghan E / Braunstein, Miriam

2012 Volume 10, Issue 11, Page(s) 779–789

Abstract: The conserved general secretion (Sec) pathway carries out most protein export in bacteria and is powered by the essential ATPase SecA. Interestingly, mycobacteria and some Gram-positive bacteria possess two SecA proteins: SecA1 and SecA2. In these ... ...

Abstract	The conserved general secretion (Sec) pathway carries out most protein export in bacteria and is powered by the essential ATPase SecA. Interestingly, mycobacteria and some Gram-positive bacteria possess two SecA proteins: SecA1 and SecA2. In these species, SecA1 is responsible for exporting most proteins, whereas SecA2 exports only a subset of substrates and is implicated in virulence. However, despite the impressive body of knowledge about the canonical SecA1, less is known concerning SecA2 function. Here, we review our current understanding of the different types of SecA2 systems and outline future directions for their study.
MeSH term(s)	Adenosine Triphosphatases/chemistry ; Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Bacteria/genetics ; Bacteria/metabolism ; Bacteria/pathogenicity ; Bacterial Physiological Phenomena ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Membrane Transport Proteins/chemistry ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Protein Transport ; SEC Translocation Channels ; SecA Proteins ; Virulence Factors/metabolism
Chemical Substances	Bacterial Proteins ; Membrane Transport Proteins ; SEC Translocation Channels ; Virulence Factors ; Adenosine Triphosphatases (EC 3.6.1.-) ; SecA Proteins (EC 7.4.2.4)
Language	English
Publishing date	2012-09-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2139054-X
ISSN	1740-1534 ; 1740-1526
ISSN (online)	1740-1534
ISSN	1740-1526
DOI	10.1038/nrmicro2874
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Article ; Online: Protein export systems of Mycobacterium tuberculosis: novel targets for drug development?

Feltcher, Meghan E / Sullivan, Jonathan Tabb / Braunstein, Miriam

Future microbiology

2010 Volume 5, Issue 10, Page(s) 1581–1597

Abstract: Protein export is essential in all bacteria and many bacterial pathogens depend on specialized protein export systems for virulence. In Mycobacterium tuberculosis, the etiological agent of the disease tuberculosis, the conserved general secretion (Sec) ... ...

Abstract	Protein export is essential in all bacteria and many bacterial pathogens depend on specialized protein export systems for virulence. In Mycobacterium tuberculosis, the etiological agent of the disease tuberculosis, the conserved general secretion (Sec) and twin-arginine translocation (Tat) pathways perform the bulk of protein export and are both essential. M. tuberculosis also has specialized export pathways that transport specific subsets of proteins. One such pathway is the accessory SecA2 system, which is important for M. tuberculosis virulence. There are also specialized ESX export systems that function in virulence (ESX-1) or essential physiologic processes (ESX-3). The increasing prevalence of drug-resistant M. tuberculosis strains makes the development of novel drugs for tuberculosis an urgent priority. In this article, we discuss our current understanding of the protein export systems of M. tuberculosis and consider the potential of these pathways to be novel targets for tuberculosis drugs.
MeSH term(s)	Antitubercular Agents/pharmacology ; Bacterial Proteins/antagonists & inhibitors ; Bacterial Proteins/metabolism ; Humans ; Membrane Transport Proteins/metabolism ; Mycobacterium tuberculosis/drug effects ; Mycobacterium tuberculosis/metabolism ; Mycobacterium tuberculosis/pathogenicity
Chemical Substances	Antitubercular Agents ; Bacterial Proteins ; Membrane Transport Proteins
Language	English
Publishing date	2010-11-12
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ISSN	1746-0921
ISSN (online)	1746-0921
DOI	10.2217/fmb.10.112
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Article ; Online: Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.

Feltcher, Meghan E / Gibbons, Henry S / Ligon, Lauren S / Braunstein, Miriam

Journal of bacteriology

2012 Volume 195, Issue 4, Page(s) 672–681

Abstract: At the core of the bacterial general secretion (Sec) pathway is the SecA ATPase, which powers translocation of unfolded preproteins containing Sec signal sequences through the SecYEG membrane channel. Mycobacteria have two nonredundant SecA homologs: ... ...

Abstract	At the core of the bacterial general secretion (Sec) pathway is the SecA ATPase, which powers translocation of unfolded preproteins containing Sec signal sequences through the SecYEG membrane channel. Mycobacteria have two nonredundant SecA homologs: SecA1 and SecA2. While the essential SecA1 handles "housekeeping" export, the nonessential SecA2 exports a subset of proteins and is required for Mycobacterium tuberculosis virulence. Currently, it is not understood how SecA2 contributes to Sec export in mycobacteria. In this study, we focused on identifying the features of two SecA2 substrates that target them to SecA2 for export, the Ms1704 and Ms1712 lipoproteins of the model organism Mycobacterium smegmatis. We found that the mature domains of Ms1704 and Ms1712, not the N-terminal signal sequences, confer SecA2-dependent export. We also demonstrated that the lipid modification and the extreme N terminus of the mature protein do not impart the requirement for SecA2 in export. We further showed that the Ms1704 mature domain can be efficiently exported by the twin-arginine translocation (Tat) pathway. Because the Tat system exports only folded proteins, this result implies that SecA2 substrates can fold in the cytoplasm and suggests a putative role of SecA2 in enabling export of such proteins. Thus, the mycobacterial SecA2 system may represent another way that bacteria solve the problem of exporting proteins that can fold in the cytoplasm.
MeSH term(s)	Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Amino Acid Sequence ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Gene Expression Regulation, Bacterial/physiology ; Gene Products, tat/genetics ; Gene Products, tat/metabolism ; Lipoproteins/genetics ; Lipoproteins/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Mutagenesis ; Mutation ; Mycobacterium smegmatis/genetics ; Mycobacterium smegmatis/metabolism ; Plasmids ; Protein Structure, Tertiary ; Protein Transport/physiology ; Virulence
Chemical Substances	Bacterial Proteins ; Gene Products, tat ; Lipoproteins ; Membrane Transport Proteins ; Adenosine Triphosphatases (EC 3.6.1.-) ; SecA2 protein, Mycobacterium (EC 3.6.1.-)
Language	English
Publishing date	2012-11-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.02032-12
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Article: Protein Export by the Mycobacterial SecA2 System Is Determined by the Preprotein Mature Domain

Feltcher, Meghan E / Gibbons, Henry S / Ligon, Lauren S / Braunstein, Miriam

Journal of bacteriology. 2013 Feb. 15, v. 195, no. 4

2013

Abstract	At the core of the bacterial general secretion (Sec) pathway is the SecA ATPase, which powers translocation of unfolded preproteins containing Sec signal sequences through the SecYEG membrane channel. Mycobacteria have two nonredundant SecA homologs: SecA1 and SecA2. While the essential SecA1 handles “housekeeping” export, the nonessential SecA2 exports a subset of proteins and is required for Mycobacterium tuberculosis virulence. Currently, it is not understood how SecA2 contributes to Sec export in mycobacteria. In this study, we focused on identifying the features of two SecA2 substrates that target them to SecA2 for export, the Ms1704 and Ms1712 lipoproteins of the model organism Mycobacterium smegmatis. We found that the mature domains of Ms1704 and Ms1712, not the N-terminal signal sequences, confer SecA2-dependent export. We also demonstrated that the lipid modification and the extreme N terminus of the mature protein do not impart the requirement for SecA2 in export. We further showed that the Ms1704 mature domain can be efficiently exported by the twin-arginine translocation (Tat) pathway. Because the Tat system exports only folded proteins, this result implies that SecA2 substrates can fold in the cytoplasm and suggests a putative role of SecA2 in enabling export of such proteins. Thus, the mycobacterial SecA2 system may represent another way that bacteria solve the problem of exporting proteins that can fold in the cytoplasm.
Keywords	Mycobacterium smegmatis ; Mycobacterium tuberculosis ; adenosinetriphosphatase ; bacteria ; bacteriology ; cytoplasm ; lipoproteins ; protein transport ; secretion ; signal peptide ; virulence
Language	English
Dates of publication	2013-0215
Size	p. 672-681.
Publishing place	American Society for Microbiology
Document type	Article
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.02032-12
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Article ; Online: Comparison of the membrane proteome of virulent Mycobacterium tuberculosis and the attenuated Mycobacterium bovis BCG vaccine strain by label-free quantitative proteomics.

Gunawardena, Harsha P / Feltcher, Meghan E / Wrobel, John A / Gu, Sheng / Braunstein, Miriam / Chen, Xian

Journal of proteome research

2013 Volume 12, Issue 12, Page(s) 5463–5474

Abstract: The Mycobacterium tuberculosis membrane is rich in antigens that are potential targets for diagnostics and the development of new vaccines. To better understand the mechanisms underlying MTB virulence and identify new targets for therapeutic intervention, ...

Abstract	The Mycobacterium tuberculosis membrane is rich in antigens that are potential targets for diagnostics and the development of new vaccines. To better understand the mechanisms underlying MTB virulence and identify new targets for therapeutic intervention, we investigated the differential composition of membrane proteomes between virulent M. tuberculosis H37Rv (MTB) and the Mycobacterium bovis BCG vaccine strain. To compare the membrane proteomes, we used LC-MS/MS analysis in combination with label-free quantitative proteomics, utilizing the area under the curve of the extracted ion chromatograms of peptides obtained from m/z and retention time alignment of MS1 features. With this approach, we obtained relative abundance ratios for 2203 identified membrane-associated proteins in high confidence. Of these proteins, 294 showed statistically significant differences of at least two fold in relative abundance between MTB and BCG membrane fractions. Our comparative analysis detected several proteins associated with known genomic regions of difference between MTB and BCG as being absent, which validated the accuracy of our approach. In further support of our label-free quantitative data, we verified select protein differences by immunoblotting. To our knowledge, we have generated the first comprehensive and high-coverage profile of comparative membrane proteome changes between virulent MTB and its attenuated relative BCG, which helps elucidate the proteomic basis of the intrinsic virulence of the MTB pathogen.
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/isolation & purification ; Cell Membrane/chemistry ; Chromatography, Liquid ; Gene Expression Regulation, Bacterial ; Genetic Loci ; Immunoblotting ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/isolation & purification ; Molecular Sequence Annotation ; Mycobacterium bovis/chemistry ; Mycobacterium bovis/genetics ; Mycobacterium tuberculosis/chemistry ; Mycobacterium tuberculosis/genetics ; Mycobacterium tuberculosis/pathogenicity ; Peptides ; Proteolysis ; Proteome/chemistry ; Proteomics/methods ; Tandem Mass Spectrometry ; Trypsin/chemistry ; Virulence
Chemical Substances	Bacterial Proteins ; Membrane Proteins ; Peptides ; Proteome ; Trypsin (EC 3.4.21.4)
Language	English
Publishing date	2013-10-28
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/pr400334k
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Article ; Online: Label-free Quantitative Proteomics Reveals a Role for the Mycobacterium tuberculosis SecA2 Pathway in Exporting Solute Binding Proteins and Mce Transporters to the Cell Wall.

Feltcher, Meghan E / Gunawardena, Harsha P / Zulauf, Katelyn E / Malik, Seidu / Griffin, Jennifer E / Sassetti, Christopher M / Chen, Xian / Braunstein, Miriam

Molecular & cellular proteomics : MCP

2015 Volume 14, Issue 6, Page(s) 1501–1516

Abstract: Mycobacterium tuberculosis is an example of a bacterial pathogen with a specialized SecA2-dependent protein export system that contributes to its virulence. Our understanding of the mechanistic basis of SecA2-dependent export and the role(s) of the SecA2 ...

Abstract	Mycobacterium tuberculosis is an example of a bacterial pathogen with a specialized SecA2-dependent protein export system that contributes to its virulence. Our understanding of the mechanistic basis of SecA2-dependent export and the role(s) of the SecA2 pathway in M. tuberculosis pathogenesis has been hindered by our limited knowledge of the proteins exported by the pathway. Here, we set out to identify M. tuberculosis proteins that use the SecA2 pathway for their export from the bacterial cytoplasm to the cell wall. Using label-free quantitative proteomics involving spectral counting, we compared the cell wall and cytoplasmic proteomes of wild type M. tuberculosis to that of a ΔsecA2 mutant. This work revealed a role for the M. tuberculosis SecA2 pathway in the cell wall localization of solute binding proteins that work with ABC transporters to import solutes. Another discovery was a profound effect of SecA2 on the cell wall localization of the Mce1 and Mce4 lipid transporters, which contribute to M. tuberculosis virulence. In addition to the effects on solute binding proteins and Mce transporter export, our label-free quantitative analysis revealed an unexpected relationship between SecA2 and the hypoxia-induced DosR regulon, which is associated with M. tuberculosis latency. Nearly half of the transcriptionally controlled DosR regulon of cytoplasmic proteins were detected at higher levels in the ΔsecA2 mutant versus wild type M. tuberculosis. By increasing the list of M. tuberculosis proteins known to be affected by the SecA2 pathway, this study expands our appreciation of the types of proteins exported by this pathway and guides our understanding of the mechanism of SecA2-dependent protein export in mycobacteria. At the same time, the newly identified SecA2-dependent proteins are helpful for understanding the significance of this pathway to M. tuberculosis virulence and physiology.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Bacterial Proteins/metabolism ; Biological Transport ; Carrier Proteins/metabolism ; Cell Wall/metabolism ; Membrane Transport Proteins/metabolism ; Proteomics
Chemical Substances	Bacterial Proteins ; Carrier Proteins ; Mce4A protein, Mycobacterium tuberculosis ; Membrane Transport Proteins ; mammalian cell entry protein Mce1A, Mycobacterium tuberculosis ; Adenosine Triphosphatases (EC 3.6.1.-) ; SecA2 protein, Mycobacterium (EC 3.6.1.-)
Language	English
Publishing date	2015-03-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2075924-1
ISSN	1535-9484 ; 1535-9476
ISSN (online)	1535-9484
ISSN	1535-9476
DOI	10.1074/mcp.M114.044685
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Article ; Online: Tat-dependent translocation of an F420-binding protein of Mycobacterium tuberculosis.

Bashiri, Ghader / Perkowski, Ellen F / Turner, Adrian P / Feltcher, Meghan E / Braunstein, Miriam / Baker, Edward N

PloS one

2012 Volume 7, Issue 10, Page(s) e45003

Abstract: F(420) is a unique cofactor present in a restricted range of microorganisms, including mycobacteria. It has been proposed that F(420) has an important role in the oxidoreductive reactions of Mycobacterium tuberculosis, possibly associated with anaerobic ... ...

Abstract	F(420) is a unique cofactor present in a restricted range of microorganisms, including mycobacteria. It has been proposed that F(420) has an important role in the oxidoreductive reactions of Mycobacterium tuberculosis, possibly associated with anaerobic survival and persistence. The protein encoded by Rv0132c has a predicted N-terminal signal sequence and is annotated as an F(420)-dependent glucose-6-phosphate dehydrogenase. Here we show that Rv0132c protein does not have the annotated activity. It does, however, co-purify with F(420) during expression experiments in M. smegmatis. We also show that the Rv0132c-F(420) complex is a substrate for the Tat pathway, which mediates translocation of the complex across the cytoplasmic membrane, where Rv0132c is anchored to the cell envelope. This is the first report of any F(420)-binding protein being a substrate for the Tat pathway and of the presence of F(420) outside of the cytosol in any F(420)-producing microorganism. The Rv0132c protein and its Tat export sequence are essentially invariant in the Mycobacterium tuberculosis complex. Taken together, these results show that current understanding of F(420) biology in mycobacteria should be expanded to include activities occurring in the extra-cytoplasmic cell envelope.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Carrier Proteins ; Chromatography, Gel ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Mycobacterium tuberculosis/metabolism ; Open Reading Frames ; Protein Transport/physiology
Chemical Substances	Bacterial Proteins ; Carrier Proteins ; Membrane Transport Proteins
Language	English
Publishing date	2012-10-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0045003
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Article ; Online: Root microbiota drive direct integration of phosphate stress and immunity.

Castrillo, Gabriel / Teixeira, Paulo José Pereira Lima / Paredes, Sur Herrera / Law, Theresa F / de Lorenzo, Laura / Feltcher, Meghan E / Finkel, Omri M / Breakfield, Natalie W / Mieczkowski, Piotr / Jones, Corbin D / Paz-Ares, Javier / Dangl, Jeffery L

Nature

2017 Volume 543, Issue 7646, Page(s) 513–518

Abstract: Plants live in biogeochemically diverse soils with diverse microbiota. Plant organs associate intimately with a subset of these microbes, and the structure of the microbial community can be altered by soil nutrient content. Plant-associated microbes can ... ...

Abstract	Plants live in biogeochemically diverse soils with diverse microbiota. Plant organs associate intimately with a subset of these microbes, and the structure of the microbial community can be altered by soil nutrient content. Plant-associated microbes can compete with the plant and with each other for nutrients, but may also carry traits that increase the productivity of the plant. It is unknown how the plant immune system coordinates microbial recognition with nutritional cues during microbiome assembly. Here we establish that a genetic network controlling the phosphate stress response influences the structure of the root microbiome community, even under non-stress phosphate conditions. We define a molecular mechanism regulating coordination between nutrition and defence in the presence of a synthetic bacterial community. We further demonstrate that the master transcriptional regulators of phosphate stress response in Arabidopsis thaliana also directly repress defence, consistent with plant prioritization of nutritional stress over defence. Our work will further efforts to define and deploy useful microbes to enhance plant performance.
MeSH term(s)	Arabidopsis/genetics ; Arabidopsis/immunology ; Arabidopsis/metabolism ; Arabidopsis/microbiology ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Microbiota/immunology ; Microbiota/physiology ; Mutation ; Phosphates/metabolism ; Plant Immunity/genetics ; Plant Roots/metabolism ; Plant Roots/microbiology ; Transcription Factors/deficiency ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Arabidopsis Proteins ; PHR1 protein, Arabidopsis ; Phosphates ; Transcription Factors
Language	English
Publishing date	2017-03-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/nature21417
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Article ; Online: Design of synthetic bacterial communities for predictable plant phenotypes.

Herrera Paredes, Sur / Gao, Tianxiang / Law, Theresa F / Finkel, Omri M / Mucyn, Tatiana / Teixeira, Paulo José Pereira Lima / Salas González, Isaí / Feltcher, Meghan E / Powers, Matthew J / Shank, Elizabeth A / Jones, Corbin D / Jojic, Vladimir / Dangl, Jeffery L / Castrillo, Gabriel

PLoS biology

2018 Volume 16, Issue 2, Page(s) e2003962

Abstract: Specific members of complex microbiota can influence host phenotypes, depending on both the abiotic environment and the presence of other microorganisms. Therefore, it is challenging to define bacterial combinations that have predictable host phenotypic ... ...

Abstract	Specific members of complex microbiota can influence host phenotypes, depending on both the abiotic environment and the presence of other microorganisms. Therefore, it is challenging to define bacterial combinations that have predictable host phenotypic outputs. We demonstrate that plant-bacterium binary-association assays inform the design of small synthetic communities with predictable phenotypes in the host. Specifically, we constructed synthetic communities that modified phosphate accumulation in the shoot and induced phosphate starvation-responsive genes in a predictable fashion. We found that bacterial colonization of the plant is not a predictor of the plant phenotypes we analyzed. Finally, we demonstrated that characterizing a subset of all possible bacterial synthetic communities is sufficient to predict the outcome of untested bacterial consortia. Our results demonstrate that it is possible to infer causal relationships between microbiota membership and host phenotypes and to use these inferences to rationally design novel communities.
MeSH term(s)	Bacteria/genetics ; Bacteria/isolation & purification ; Brassicaceae/genetics ; Brassicaceae/metabolism ; Brassicaceae/microbiology ; Genes, Bacterial ; Genes, Plant ; Host Microbial Interactions ; Microbial Consortia ; Phosphates/metabolism ; Plant Roots/microbiology ; Plant Shoots/metabolism ; RNA, Ribosomal, 16S/genetics ; Symbiosis
Chemical Substances	Phosphates ; RNA, Ribosomal, 16S
Language	English
Publishing date	2018-02-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.2003962
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Article ; Online: Genome-wide identification of Mycobacterium tuberculosis exported proteins with roles in intracellular growth.

McCann, Jessica R / McDonough, Justin A / Sullivan, Jonathan Tabb / Feltcher, Meghan E / Braunstein, Miriam

Journal of bacteriology

2010 Volume 193, Issue 4, Page(s) 854–861

Abstract: The exported proteins of Mycobacterium tuberculosis that are localized at the bacterial cell surface or secreted into the environment are ideally situated to interact with host factors and to function in virulence. In this study, we constructed a novel β- ...

Abstract	The exported proteins of Mycobacterium tuberculosis that are localized at the bacterial cell surface or secreted into the environment are ideally situated to interact with host factors and to function in virulence. In this study, we constructed a novel β-lactamase reporter transposon and used it directly in M. tuberculosis for genome-wide identification of exported proteins. From 177 β-lactam-resistant transposon mutants, we identified 111 different exported proteins. The majority of these proteins have no known function, and for nearly half of the proteins, our demonstration that they are exported when fused to a β-lactamase reporter is the first experimental proof of their extracytoplasmic localization. The transposon mutants in our banked library were of further value as a collection of mutants lacking individual exported proteins. By individually testing each of 111 mutants for growth in macrophages, six attenuated mutants with insertions in mce1A, mce1B, mce2F, rv0199, ctaC, and lppX were identified. Given that much of the M. tuberculosis genome encodes proteins of unknown function, our library of mapped transposon mutants is a valuable resource for efforts in functional genomics. This work also demonstrates the power of a β-lactamase reporter transposon that could be applied similarly to other bacterial pathogens.
MeSH term(s)	Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cells, Cultured ; Extracellular Space/genetics ; Extracellular Space/metabolism ; Female ; Gene Expression Regulation, Bacterial ; Genes, Reporter ; Genome, Bacterial ; Humans ; Macrophages/microbiology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mycobacterium tuberculosis/genetics ; Mycobacterium tuberculosis/growth & development ; Mycobacterium tuberculosis/metabolism ; Protein Transport ; Tuberculosis/microbiology
Chemical Substances	Bacterial Proteins
Language	English
Publishing date	2010-12-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.01271-10
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