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Article ; Online: Francisella tularensis Exploits AMPK Activation to Harvest Host-Derived Nutrients Liberated from Host Lipolysis.

Dominguez, Sedelia R / Whiles, Shannon / Deobald, Kelly N / Kawula, Thomas

2022 Volume 90, Issue 8, Page(s) e0015522

Abstract: Francisella tularensis is a zoonotic, facultative intracellular bacterial pathogen that replicates in a variety of cell types during infection. Following entry into the cell and phagosome escape, the bacterium replicates rapidly in the cytoplasm. F. ... ...

Abstract	Francisella tularensis is a zoonotic, facultative intracellular bacterial pathogen that replicates in a variety of cell types during infection. Following entry into the cell and phagosome escape, the bacterium replicates rapidly in the cytoplasm. F. tularensis intracellular growth depends on the availability of metabolizable essential nutrients to support replication. However, the mechanism by which metabolizable nutrients become available to the bacterium in the intracellular environment is not fully understood. We found that F. tularensis-infected cells had significantly smaller and fewer lipid droplets than uninfected cells. Inhibition of triacylglycerol degradation significantly reduced bacterial growth, whereas inhibition of triacylglycerol formation did not reduce bacterial growth, suggesting that triacylglycerols sequestered within lipid droplets are important nutrient sources for F. tularensis. We found that F. tularensis-infected cells had increased activation of lipolysis and the upstream regulatory protein AMP protein kinase (AMPK). These data suggest that F. tularensis exploits AMPK activation and lipid metabolism to use host-derived nutrients. Finally, we found that AMPK activation is correlated with an increased bacterial burden, which suggests that it is a host-mediated response to nutrient starvation that results from increased bacterial replication. Altogether, we conclude that F. tularensis exploits AMPK activation to access nutrients sequestered in lipid droplets, specifically glycerol and fatty acids, to undergo efficient bacterial replication and cause successful infection.
MeSH term(s)	AMP-Activated Protein Kinases/metabolism ; Francisella tularensis ; Humans ; Lipolysis ; Nutrients ; Phagosomes/microbiology ; Triglycerides/metabolism ; Tularemia/microbiology
Chemical Substances	Triglycerides ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2022-08-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/iai.00155-22
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Francisella tularensis

Steele, Shaun P / Chamberlain, Zach / Park, Jason / Kawula, Thomas H

eLife

2019 Volume 8

Abstract: Previously, we found that phagocytic cells ingest bacteria directly from the cytosol of infected cells without killing the initially infected cell (Steele et al., 2016). Here, we explored the events immediately following bacterial transfer. ...

Abstract	Previously, we found that phagocytic cells ingest bacteria directly from the cytosol of infected cells without killing the initially infected cell (Steele et al., 2016). Here, we explored the events immediately following bacterial transfer.
MeSH term(s)	Animals ; Cytoplasmic Vesicles/microbiology ; Disease Models, Animal ; Endocytosis ; Francisella tularensis/growth & development ; Lung/microbiology ; Lung/pathology ; Mice ; Phagocytes/microbiology ; Phagocytes/physiology ; Tularemia/microbiology ; Tularemia/pathology
Language	English
Publishing date	2019-04-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.45252
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Article ; Online: The role of autophagy in intracellular pathogen nutrient acquisition.

Steele, Shaun / Brunton, Jason / Kawula, Thomas

Frontiers in cellular and infection microbiology

2015 Volume 5, Page(s) 51

Abstract: Following entry into host cells intracellular pathogens must simultaneously evade innate host defense mechanisms and acquire energy and anabolic substrates from the nutrient-limited intracellular environment. Most of the potential intracellular nutrient ... ...

Abstract	Following entry into host cells intracellular pathogens must simultaneously evade innate host defense mechanisms and acquire energy and anabolic substrates from the nutrient-limited intracellular environment. Most of the potential intracellular nutrient sources are stored within complex macromolecules that are not immediately accessible by intracellular pathogens. To obtain nutrients for proliferation, intracellular pathogens must compete with the host cell for newly-imported simple nutrients or degrade host nutrient storage structures into their constituent components (fatty acids, carbohydrates, and amino acids). It is becoming increasingly evident that intracellular pathogens have evolved a wide variety of strategies to accomplish this task. One recurrent microbial strategy is to exploit host degradative processes that break down host macromolecules into simple nutrients that the microbe can use. Herein we focus on how a subset of bacterial, viral, and eukaryotic pathogens leverage the host process of autophagy to acquire nutrients that support their growth within infected cells.
MeSH term(s)	Animals ; Autophagy ; Bacterial Physiological Phenomena ; Eukaryotic Cells/physiology ; Host-Pathogen Interactions ; Humans ; Virus Physiological Phenomena
Language	English
Publishing date	2015
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2015.00051
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Article ; Online: Defining the Metabolic Pathways and Host-Derived Carbon Substrates Required for Francisella tularensis Intracellular Growth.

Radlinski, Lauren C / Brunton, Jason / Steele, Shaun / Taft-Benz, Sharon / Kawula, Thomas H

mBio

2018 Volume 9, Issue 6

Abstract: Francisella ... ...

Abstract	Francisella tularensis
MeSH term(s)	Animals ; Carbon/metabolism ; Cytoplasm/microbiology ; DNA Replication ; Female ; Francisella tularensis/growth & development ; Francisella tularensis/metabolism ; Fructose-Bisphosphatase/metabolism ; Gluconeogenesis ; Glycolysis ; Macrophages/microbiology ; Macrophages/physiology ; Metabolic Flux Analysis ; Metabolic Networks and Pathways ; Mice ; Mice, Inbred C57BL ; Phosphofructokinases/metabolism ; Tularemia/metabolism ; Virulence
Chemical Substances	Carbon (7440-44-0) ; Phosphofructokinases (EC 2.7.1 -) ; Fructose-Bisphosphatase (EC 3.1.3.11)
Language	English
Publishing date	2018-11-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mBio.01471-18
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Article ; Online: A method for functional trans-complementation of intracellular Francisella tularensis.

Steele, Shaun / Taft-Benz, Sharon / Kawula, Thomas

PloS one

2014 Volume 9, Issue 2, Page(s) e88194

Abstract: Francisella tularensis is a highly infectious bacterial pathogen that invades and replicates within numerous host cell types. After uptake, F. tularensis bacteria escape the phagosome, replicate within the cytosol, and suppress cytokine responses. ... ...

Abstract	Francisella tularensis is a highly infectious bacterial pathogen that invades and replicates within numerous host cell types. After uptake, F. tularensis bacteria escape the phagosome, replicate within the cytosol, and suppress cytokine responses. However, the mechanisms employed by F. tularensis to thrive within host cells are mostly unknown. Potential F. tularensis mutants involved in host-pathogen interactions are typically discovered by negative selection screens for intracellular replication or virulence. Mutants that fulfill these criteria fall into two categories: mutants with intrinsic intracellular growth defects and mutants that fail to modify detrimental host cell processes. It is often difficult and time consuming to discriminate between these two possibilities. We devised a method to functionally trans-complement and thus identify mutants that fail to modify the host response. In this assay, host cells are consistently and reproducibly infected with two different F. tularensis strains by physically tethering the bacteria to antibody-coated beads. To examine the efficacy of this protocol, we tested phagosomal escape, cytokine suppression, and intracellular replication for F. tularensis ΔripA and ΔpdpC. ΔripA has an intracellular growth defect that is likely due to an intrinsic defect and fails to suppress IL-1β secretion. In the co-infection model, ΔripA was unable to replicate in the host cell when wild-type bacteria infected the same cell, but cytokine suppression was rescued. Therefore, ΔripA intracellular growth is due to an intrinsic bacterial defect while cytokine secretion results from a failed host-pathogen interaction. Likewise, ΔpdpC is deficient for phagosomal escape, intracellular survival and suppression of IL-1β secretion. Wild-type bacteria that entered through the same phagosome as ΔpdpC rescued all of these phenotypes, indicating that ΔpdpC failed to properly manipulate the host. In summary, functional trans-complementation using bead-bound bacteria co-infections is a method to rapidly identify mutants that fail to modify a host response. Francisella tularensis is a facultative intracellular bacterial pathogen and is the causative agent of the disease tularemia. F. tularensis enters host cells through phagocytosis, escapes the phagosome, and replicates in the host cell cytosol while suppressing cytokine secretion [1]-[4]. Although substantial progress has been made in understanding the intracellular life cycle of F. tularensis, the F. tularensis proteins responsible for manipulating many host cell pathways are unknown. Identifying novel host-pathogen effector proteins is difficult because there is no rapid method to reliably distinguish between bacterial proteins that modify host processes and proteins that are involved in bacterial processes that are required for the bacteria to survive or replicate in the intracellular environment. The ability to identify mutants that are deficient for host-pathogen interactions is important because it can aid in prioritizing the investigation of genes of interest and in downstream experimental design. Moreover, certain mutant phenotypes, such as decreased phagosomal escape, hinder investigation of other potential phenotypes. A method to specifically complement these phenotypes would allow for further characterizations of certain F. tularensis mutants. Thus we sought to develop a method to easily identify and functionally complement mutants that are deficient for interactions with the host.
MeSH term(s)	Animals ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Line ; Coinfection/genetics ; Coinfection/microbiology ; Cytosol/metabolism ; Cytosol/microbiology ; Cytosol/physiology ; Francisella tularensis/genetics ; Francisella tularensis/metabolism ; Francisella tularensis/physiology ; Host-Pathogen Interactions/genetics ; Host-Pathogen Interactions/physiology ; Interleukin-1beta/genetics ; Interleukin-1beta/metabolism ; Life Cycle Stages/genetics ; Life Cycle Stages/physiology ; Macrophages/metabolism ; Macrophages/microbiology ; Macrophages/physiology ; Mice ; Mice, Inbred C57BL ; Mutation/genetics ; Phagocytosis/genetics ; Phagocytosis/physiology ; Phagosomes/genetics ; Phagosomes/metabolism ; Phagosomes/microbiology ; Phenotype ; Tularemia/genetics ; Tularemia/metabolism ; Tularemia/microbiology ; Tularemia/physiopathology ; Virulence/genetics ; Virulence/physiology
Chemical Substances	Bacterial Proteins ; Interleukin-1beta
Language	English
Publishing date	2014-02-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0088194
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Article ; Online: Trogocytosis-associated cell to cell spread of intracellular bacterial pathogens.

Steele, Shaun / Radlinski, Lauren / Taft-Benz, Sharon / Brunton, Jason / Kawula, Thomas H

eLife

2016 Volume 5

Abstract: Macrophages are myeloid-derived phagocytic cells and one of the first immune cell types to respond to microbial infections. However, a number of bacterial pathogens are resistant to the antimicrobial activities of macrophages and can grow within these ... ...

Abstract	Macrophages are myeloid-derived phagocytic cells and one of the first immune cell types to respond to microbial infections. However, a number of bacterial pathogens are resistant to the antimicrobial activities of macrophages and can grow within these cells. Macrophages have other immune surveillance roles including the acquisition of cytosolic components from multiple types of cells. We hypothesized that intracellular pathogens that can replicate within macrophages could also exploit cytosolic transfer to facilitate bacterial spread. We found that viable Francisella tularensis, as well as Salmonella enterica bacteria transferred from infected cells to uninfected macrophages along with other cytosolic material through a transient, contact dependent mechanism. Bacterial transfer occurred when the host cells exchanged plasma membrane proteins and cytosol via a trogocytosis related process leaving both donor and recipient cells intact and viable. Trogocytosis was strongly associated with infection in mice, suggesting that direct bacterial transfer occurs by this process in vivo.
MeSH term(s)	Animals ; Cell Communication ; Cell Line ; Cytoplasm/microbiology ; Epithelial Cells/microbiology ; Epithelial Cells/physiology ; Francisella tularensis/isolation & purification ; Immunological Synapses/microbiology ; Macrophages/immunology ; Macrophages/microbiology ; Mice ; Salmonella enterica/isolation & purification
Language	English
Publishing date	2016-01-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.10625
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Article ; Online: Genetic requirements for Staphylococcus aureus nitric oxide resistance and virulence.

Grosser, Melinda R / Paluscio, Elyse / Thurlow, Lance R / Dillon, Marcus M / Cooper, Vaughn S / Kawula, Thomas H / Richardson, Anthony R

PLoS pathogens

2018 Volume 14, Issue 3, Page(s) e1006907

Abstract: Staphylococcus aureus exhibits many defenses against host innate immunity, including the ability to replicate in the presence of nitric oxide (NO·). S. aureus NO· resistance is a complex trait and hinges on the ability of this pathogen to metabolically ... ...

Abstract	Staphylococcus aureus exhibits many defenses against host innate immunity, including the ability to replicate in the presence of nitric oxide (NO·). S. aureus NO· resistance is a complex trait and hinges on the ability of this pathogen to metabolically adapt to the presence of NO·. Here, we employed deep sequencing of transposon junctions (Tn-Seq) in a library generated in USA300 LAC to define the complete set of genes required for S. aureus NO· resistance. We compared the list of NO·-resistance genes to the set of genes required for LAC to persist within murine skin infections (SSTIs). In total, we identified 168 genes that were essential for full NO· resistance, of which 49 were also required for S. aureus to persist within SSTIs. Many of these NO·-resistance genes were previously demonstrated to be required for growth in the presence of this immune radical. However, newly defined genes, including those encoding SodA, MntABC, RpoZ, proteins involved with Fe-S-cluster repair/homeostasis, UvrABC, thioredoxin-like proteins and the F1F0 ATPase, have not been previously reported to contribute to S. aureus NO· resistance. The most striking finding was that loss of any genes encoding components of the F1F0 ATPase resulted in mutants unable to grow in the presence of NO· or any other condition that inhibits cellular respiration. In addition, these mutants were highly attenuated in murine SSTIs. We show that in S. aureus, the F1F0 ATPase operates in the ATP-hydrolysis mode to extrude protons and contribute to proton-motive force. Loss of efficient proton extrusion in the ΔatpG mutant results in an acidified cytosol. While this acidity is tolerated by respiring cells, enzymes required for fermentation cannot operate efficiently at pH ≤ 7.0 and the ΔatpG mutant cannot thrive. Thus, S. aureus NO· resistance requires a mildly alkaline cytosol, a condition that cannot be achieved without an active F1F0 ATPase enzyme complex.
MeSH term(s)	Animals ; Bacterial Proteins/genetics ; Gene Expression Regulation, Bacterial ; Gene Library ; Immunity, Innate/drug effects ; Immunity, Innate/genetics ; Immunity, Innate/immunology ; Mice ; Mice, Inbred C57BL ; Nitric Oxide/pharmacology ; Staphylococcal Skin Infections/genetics ; Staphylococcal Skin Infections/immunology ; Staphylococcal Skin Infections/microbiology ; Staphylococcus aureus/drug effects ; Staphylococcus aureus/immunology ; Virulence/drug effects ; Virulence/genetics ; Virulence/immunology
Chemical Substances	Bacterial Proteins ; Nitric Oxide (31C4KY9ESH)
Language	English
Publishing date	2018-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1006907
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Article ; Online: Feeding uninvited guests: mTOR and AMPK set the table for intracellular pathogens.

Brunton, Jason / Steele, Shaun / Ziehr, Benjamin / Moorman, Nathaniel / Kawula, Thomas

PLoS pathogens

2013 Volume 9, Issue 10, Page(s) e1003552

MeSH term(s)	AMP-Activated Protein Kinases/metabolism ; Animals ; Bacteria/metabolism ; Bacterial Physiological Phenomena ; Host-Pathogen Interactions/physiology ; Humans ; Signal Transduction ; TOR Serine-Threonine Kinases/metabolism ; Virus Physiological Phenomena ; Viruses/metabolism
Chemical Substances	MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2013-10-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1003552
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Article ; Online: Francisella tularensis harvests nutrients derived via ATG5-independent autophagy to support intracellular growth.

Steele, Shaun / Brunton, Jason / Ziehr, Benjamin / Taft-Benz, Sharon / Moorman, Nathaniel / Kawula, Thomas

PLoS pathogens

2013 Volume 9, Issue 8, Page(s) e1003562

Abstract: Francisella tularensis is a highly virulent intracellular pathogen that invades and replicates within numerous host cell types including macrophages, hepatocytes and pneumocytes. By 24 hours post invasion, F. tularensis replicates up to 1000-fold in the ... ...

Abstract	Francisella tularensis is a highly virulent intracellular pathogen that invades and replicates within numerous host cell types including macrophages, hepatocytes and pneumocytes. By 24 hours post invasion, F. tularensis replicates up to 1000-fold in the cytoplasm of infected cells. To achieve such rapid intracellular proliferation, F. tularensis must scavenge large quantities of essential carbon and energy sources from the host cell while evading anti-microbial immune responses. We found that macroautophagy, a eukaryotic cell process that primarily degrades host cell proteins and organelles as well as intracellular pathogens, was induced in F. tularensis infected cells. F. tularensis not only survived macroautophagy, but optimal intracellular bacterial growth was found to require macroautophagy. Intracellular growth upon macroautophagy inhibition was rescued by supplying excess nonessential amino acids or pyruvate, demonstrating that autophagy derived nutrients provide carbon and energy sources that support F. tularensis proliferation. Furthermore, F. tularensis did not require canonical, ATG5-dependent autophagy pathway induction but instead induced an ATG5-independent autophagy pathway. ATG5-independent autophagy induction caused the degradation of cellular constituents resulting in the release of nutrients that the bacteria harvested to support bacterial replication. Canonical macroautophagy limits the growth of several different bacterial species. However, our data demonstrate that ATG5-independent macroautophagy may be beneficial to some cytoplasmic bacteria by supplying nutrients to support bacterial growth.
MeSH term(s)	Amino Acids/metabolism ; Animals ; Apoptosis Regulatory Proteins/antagonists & inhibitors ; Apoptosis Regulatory Proteins/genetics ; Apoptosis Regulatory Proteins/metabolism ; Autophagy ; Autophagy-Related Protein 5 ; Beclin-1 ; Blotting, Western ; Cells, Cultured ; Embryo, Mammalian/metabolism ; Embryo, Mammalian/microbiology ; Embryo, Mammalian/pathology ; Fibroblasts/metabolism ; Fibroblasts/microbiology ; Fibroblasts/pathology ; Francisella tularensis/genetics ; Francisella tularensis/growth & development ; Francisella tularensis/pathogenicity ; Macrophages/metabolism ; Macrophages/microbiology ; Macrophages/pathology ; Mice ; Microscopy, Fluorescence ; Microtubule-Associated Proteins/physiology ; Pyruvic Acid/metabolism ; RNA, Messenger/genetics ; RNA, Small Interfering/genetics ; Real-Time Polymerase Chain Reaction ; Reverse Transcriptase Polymerase Chain Reaction ; Tularemia/genetics ; Tularemia/microbiology ; Tularemia/pathology
Chemical Substances	Amino Acids ; Apoptosis Regulatory Proteins ; Atg5 protein, mouse ; Autophagy-Related Protein 5 ; Beclin-1 ; Becn1 protein, mouse ; Microtubule-Associated Proteins ; RNA, Messenger ; RNA, Small Interfering ; Pyruvic Acid (8558G7RUTR)
Language	English
Publishing date	2013-08-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1003562
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Article ; Online: A Phosphatidylinositol 3-Kinase Effector Alters Phagosomal Maturation to Promote Intracellular Growth of Francisella.

Ledvina, Hannah E / Kelly, Katherine A / Eshraghi, Aria / Plemel, Rachael L / Peterson, S Brook / Lee, Brian / Steele, Shaun / Adler, Marlen / Kawula, Thomas H / Merz, Alexey J / Skerrett, Shawn J / Celli, Jean / Mougous, Joseph D

Cell host & microbe

2018 Volume 24, Issue 2, Page(s) 285–295.e8

Abstract: Many pathogenic intracellular bacteria manipulate the host phago-endosomal system to establish and maintain a permissive niche. The fate and identity of these intracellular compartments is controlled by phosphoinositide lipids. By mechanisms that have ... ...

Abstract	Many pathogenic intracellular bacteria manipulate the host phago-endosomal system to establish and maintain a permissive niche. The fate and identity of these intracellular compartments is controlled by phosphoinositide lipids. By mechanisms that have remained undefined, a Francisella pathogenicity island-encoded secretion system allows phagosomal escape and replication of bacteria within host cell cytoplasm. Here we report the discovery that a substrate of this system, outside pathogenicity island A (OpiA), represents a family of wortmannin-resistant bacterial phosphatidylinositol (PI) 3-kinase enzymes with members found in a wide range of intracellular pathogens, including Rickettsia and Legionella spp. We show that OpiA acts on the Francisella-containing phagosome and promotes bacterial escape into the cytoplasm. Furthermore, we demonstrate that the phenotypic consequences of OpiA inactivation are mitigated by endosomal maturation arrest. Our findings suggest that Francisella, and likely other intracellular bacteria, override the finely tuned dynamics of phagosomal PI(3)P in order to promote intracellular survival and pathogenesis.
MeSH term(s)	Animals ; Bacterial Proteins/metabolism ; Cytoplasm/microbiology ; DNA Replication ; Disease Models, Animal ; Endosomes/microbiology ; Female ; Francisella/genetics ; Francisella/growth & development ; Francisella/pathogenicity ; Genes, Bacterial/genetics ; Genomic Islands ; HEK293 Cells ; HeLa Cells ; Host-Pathogen Interactions/physiology ; Humans ; Lipid Metabolism ; Macrophages/microbiology ; Male ; Mice ; Mice, Inbred C57BL ; Phagosomes/metabolism ; Phagosomes/microbiology ; Phosphatidylinositol 3-Kinase/metabolism ; Phosphatidylinositols/metabolism ; RAW 264.7 Cells ; Type VI Secretion Systems/metabolism ; Virulence Factors/metabolism
Chemical Substances	Bacterial Proteins ; PdpC protein, Francisella tularensis ; Phosphatidylinositols ; Type VI Secretion Systems ; Virulence Factors ; Phosphatidylinositol 3-Kinase (EC 2.7.1.137)
Language	English
Publishing date	2018-07-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2018.07.003
Database	MEDical Literature Analysis and Retrieval System OnLINE

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