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  1. Article ; Online: Rickettsia rickettsii

    Fitzsimmons, Liam / Bublitz, DeAnna / Clark, Tina / Hackstadt, Ted

    mBio

    2024  Volume 15, Issue 4, Page(s) e0345023

    Abstract: We compared the growth characteristics of a ... ...

    Abstract We compared the growth characteristics of a virulent
    MeSH term(s) Animals ; Guinea Pigs ; Humans ; Chlorocebus aethiops ; Endothelial Cells/pathology ; Rickettsia ; Rickettsia rickettsii/metabolism ; Rocky Mountain Spotted Fever/microbiology ; Type V Secretion Systems/metabolism ; Vero Cells ; Virulence ; Virulence Factors/metabolism ; Interferon-beta
    Chemical Substances Type V Secretion Systems ; Virulence Factors ; Interferon-beta (77238-31-4)
    Language English
    Publishing date 2024-03-06
    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.03450-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Chlamydia trachomatis suppresses host cell store-operated Ca

    Chamberlain, Nicholas B / Dimond, Zoe / Hackstadt, Ted

    Scientific reports

    2022  Volume 12, Issue 1, Page(s) 21406

    Abstract: The obligate intracellular bacterium, Chlamydia trachomatis, replicates within a parasitophorous vacuole termed an inclusion. During development, host proteins critical for regulating intracellular calcium ( ... ...

    Abstract The obligate intracellular bacterium, Chlamydia trachomatis, replicates within a parasitophorous vacuole termed an inclusion. During development, host proteins critical for regulating intracellular calcium (Ca
    Language English
    Publishing date 2022-12-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-022-25786-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Regulator of Actin-Based Motility (RoaM) Downregulates Actin Tail Formation by Rickettsia rickettsii and Is Negatively Selected in Mammalian Cell Culture.

    Nock, Adam M / Clark, Tina R / Hackstadt, Ted

    mBio

    2022  Volume 13, Issue 2, Page(s) e0035322

    Abstract: The etiological agent of Rocky Mountain spotted fever, Rickettsia rickettsii, is an obligately intracellular pathogen that induces the polymerization of actin filaments to propel the bacterium through the cytoplasm and spread to new host cells. Cell-to- ... ...

    Abstract The etiological agent of Rocky Mountain spotted fever, Rickettsia rickettsii, is an obligately intracellular pathogen that induces the polymerization of actin filaments to propel the bacterium through the cytoplasm and spread to new host cells. Cell-to-cell spread via actin-based motility is considered a key virulence determinant for spotted fever group rickettsiae, as interruption of
    MeSH term(s) Actins/genetics ; Actins/metabolism ; Animals ; Cell Culture Techniques ; Guinea Pigs ; Mammals/metabolism ; Rickettsia/genetics ; Rickettsia/metabolism ; Rickettsia rickettsii/genetics ; Rocky Mountain Spotted Fever/microbiology ; Virulence Factors/genetics
    Chemical Substances Actins ; Virulence Factors
    Language English
    Publishing date 2022-03-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.00353-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Completed genomes for

    Nock, Adam M / Clark, Tina R / Barbian, Kent / Martens, Craig / Hackstadt, Ted

    Microbiology resource announcements

    2023  Volume 12, Issue 10, Page(s) e0036223

    Abstract: Complete genomes ... ...

    Abstract Complete genomes of
    Language English
    Publishing date 2023-09-01
    Publishing country United States
    Document type Journal Article
    ISSN 2576-098X
    ISSN (online) 2576-098X
    DOI 10.1128/MRA.00362-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Nitric Oxide Inhibition of Rickettsia rickettsii.

    Fitzsimmons, Liam F / Clark, Tina R / Hackstadt, Ted

    Infection and immunity

    2021  Volume 89, Issue 12, Page(s) e0037121

    Abstract: Rickettsia rickettsii, the causative agent of Rocky Mountain spotted fever, is an enzootic, obligate, intracellular bacterial pathogen. Nitric oxide (NO) synthesized by the inducible NO synthase (iNOS) is a potent antimicrobial component of innate ... ...

    Abstract Rickettsia rickettsii, the causative agent of Rocky Mountain spotted fever, is an enzootic, obligate, intracellular bacterial pathogen. Nitric oxide (NO) synthesized by the inducible NO synthase (iNOS) is a potent antimicrobial component of innate immunity and has been implicated in the control of virulent
    MeSH term(s) Energy Metabolism ; Host-Pathogen Interactions/immunology ; Immunity, Innate ; Macrophages/immunology ; Macrophages/metabolism ; Macrophages/microbiology ; Nitric Oxide/metabolism ; Nitric Oxide Synthase Type II/metabolism ; Rickettsia rickettsii/physiology ; Rocky Mountain Spotted Fever/immunology ; Rocky Mountain Spotted Fever/metabolism ; Rocky Mountain Spotted Fever/microbiology
    Chemical Substances Nitric Oxide (31C4KY9ESH) ; Nitric Oxide Synthase Type II (EC 1.14.13.39)
    Language English
    Publishing date 2021-09-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 218698-6
    ISSN 1098-5522 ; 0019-9567
    ISSN (online) 1098-5522
    ISSN 0019-9567
    DOI 10.1128/IAI.00371-21
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 684: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: Selective fragmentation of the trans-Golgi apparatus by Rickettsia rickettsii.

    Aistleitner, Karin / Clark, Tina / Dooley, Cheryl / Hackstadt, Ted

    PLoS pathogens

    2020  Volume 16, Issue 5, Page(s) e1008582

    Abstract: Fragmentation of the Golgi apparatus is observed during a number of physiological processes including mitosis and apoptosis, but also occurs in pathological states such as neurodegenerative diseases and some infectious diseases. Here we show that highly ... ...

    Abstract Fragmentation of the Golgi apparatus is observed during a number of physiological processes including mitosis and apoptosis, but also occurs in pathological states such as neurodegenerative diseases and some infectious diseases. Here we show that highly virulent strains of Rickettsia rickettsii, the causative agent of Rocky Mountain spotted fever, induce selective fragmentation of the trans-Golgi network (TGN) soon after infection of host cells by secretion of the effector protein Rickettsial Ankyrin Repeat Protein 2 (RARP2). Remarkably, this fragmentation is pronounced for the trans-Golgi network but the cis-Golgi remains largely intact and appropriately localized. Thus R. rickettsii targets specifically the TGN and not the entire Golgi apparatus. Dispersal of the TGN is mediated by the secreted effector protein RARP2, a recently identified type IV secreted effector that is a member of the clan CD cysteine proteases. Site-directed mutagenesis of a predicted cysteine protease active site in RARP2 prevents TGN disruption. General protein transport to the cell surface is severely impacted in cells infected with virulent strains of R. rickettsii. These findings suggest a novel manipulation of cellular organization by an obligate intracellular bacterium to determine interactions with the host cell.
    MeSH term(s) Animals ; Chlorocebus aethiops ; Rickettsia rickettsii/metabolism ; Rocky Mountain Spotted Fever/metabolism ; Rocky Mountain Spotted Fever/pathology ; Vero Cells ; trans-Golgi Network/metabolism ; trans-Golgi Network/microbiology ; trans-Golgi Network/ultrastructure
    Language English
    Publishing date 2020-05-18
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7366
    ISSN (online) 1553-7374
    ISSN 1553-7366
    DOI 10.1371/journal.ppat.1008582
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Chlamydia trachomatis Alters Mitochondrial Protein Composition and Secretes Effector Proteins That Target Mitochondria.

    Dimond, Zoe / Bauler, Laura D / Zhang, Yixiang / Carmody, Aaron / Hackstadt, Ted

    mSphere

    2022  , Page(s) e0042322

    Abstract: Mitochondria are critical cellular organelles that perform a wide variety of functions, including energy production and immune regulation. To perform these functions, mitochondria contain approximately 1,500 proteins, the majority of which are encoded in ...

    Abstract Mitochondria are critical cellular organelles that perform a wide variety of functions, including energy production and immune regulation. To perform these functions, mitochondria contain approximately 1,500 proteins, the majority of which are encoded in the nuclear genome, translated in the cytoplasm, and translocated to the mitochondria using distinct mitochondrial targeting sequences (MTS). Bacterial proteins can also contain MTS and localize to the mitochondria. For the obligate intracellular human pathogen Chlamydia trachomatis, interaction with various host cell organelles promotes intracellular replication. However, the extent and mechanisms through which Chlamydia cells interact directly with mitochondria remain unclear. We investigated the presence of MTS in the C. trachomatis genome and discovered 30 genes encoding proteins with around 70% or greater probability of mitochondrial localization. Five are translocated to the mitochondria upon ectopic expression in HeLa cells. Mass spectrometry of isolated mitochondria from infected cells revealed that two of these proteins localize to the mitochondria during infection. Comparison of mitochondria from infected and uninfected cells suggests that chlamydial infection affects the mitochondrial protein composition. Around 125 host proteins were significantly decreased or absent in mitochondria from infected cells. Among these were proapoptotic factors and those related to mitochondrial fission/fusion dynamics. Conversely, 82 host proteins were increased in or specific to mitochondria of infected cells, many of which act as antiapoptotic factors and upregulators of cellular metabolism. These data support the notion that C. trachomatis specifically targets host mitochondria to manipulate cell fate decisions and metabolic function to support pathogen survival and replication.
    Language English
    Publishing date 2022-10-26
    Publishing country United States
    Document type Journal Article
    ISSN 2379-5042
    ISSN (online) 2379-5042
    DOI 10.1128/msphere.00423-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Chlamydia trachomatis inclusion membrane protein MrcA interacts with the inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) to regulate extrusion formation.

    Nguyen, Phu Hai / Lutter, Erika I / Hackstadt, Ted

    PLoS pathogens

    2018  Volume 14, Issue 3, Page(s) e1006911

    Abstract: Chlamydia trachomatis is an obligate intracellular bacterium that replicates within a vacuole termed an inclusion. At the end of their intracellular developmental cycle, chlamydiae are released either by lysis of the host cell or extrusion of the intact ... ...

    Abstract Chlamydia trachomatis is an obligate intracellular bacterium that replicates within a vacuole termed an inclusion. At the end of their intracellular developmental cycle, chlamydiae are released either by lysis of the host cell or extrusion of the intact inclusion. The inclusion membrane is extensively modified by the insertion of type III secreted inclusion membrane proteins, Incs, which contribute to inclusion membrane structure and facilitate host-pathogen interactions. An interaction was identified between the inclusion membrane protein, MrcA, and the Ca2+ channel inositol-1,4,5-trisphosphate receptor, type 3 (ITPR3). ITPR3 was recruited and localized to active Src-family-kinase rich microdomains on the inclusion membrane as was the Ca2+ sensor, STIM1. Disruption of MrcA by directed mutagenesis resulted in loss of ITPR3 recruitment and simultaneous reduction of chlamydial release by extrusion. Complementation of MrcA restored ITPR3 recruitment and extrusion. Inhibition of extrusion was also observed following siRNA depletion of host ITPR3 or STIM1. Chlamydial extrusion was also inhibited by the calcium chelator BAPTA-AM. Each of these treatments resulted in a concomitant reduction in phosphorylation of the myosin regulatory light chain (MLC2) and a loss of myosin motor activity at the end of the developmental cycle which is consistent with the reduced extrusion formation. These studies suggest that Ca2+ signaling pathways play an important role in regulation of release mechanisms by C. trachomatis.
    MeSH term(s) Chlamydia Infections/genetics ; Chlamydia Infections/metabolism ; Chlamydia Infections/microbiology ; Chlamydia trachomatis/genetics ; Chlamydia trachomatis/metabolism ; HeLa Cells ; Host-Pathogen Interactions ; Humans ; Inclusion Bodies/metabolism ; Inclusion Bodies/microbiology ; Inositol 1,4,5-Trisphosphate Receptors/genetics ; Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Phosphorylation
    Chemical Substances Inositol 1,4,5-Trisphosphate Receptors ; Membrane Proteins
    Language English
    Publishing date 2018-03-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1006911
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Identification of an autotransporter peptidase of Rickettsia rickettsii responsible for maturation of surface exposed autotransporters.

    Nock, Adam M / Aistleitner, Karin / Clark, Tina R / Sturdevant, Dan / Ricklefs, Stacy / Virtaneva, Kimmo / Zhang, Yixiang / Gulzar, Naila / Redekar, Neelam / Roy, Amitiva / Hackstadt, Ted

    PLoS pathogens

    2023  Volume 19, Issue 7, Page(s) e1011527

    Abstract: Members of the spotted fever group rickettsia express four large, surface-exposed autotransporters, at least one of which is a known virulence determinant. Autotransporter translocation to the bacterial outer surface, also known as type V secretion, ... ...

    Abstract Members of the spotted fever group rickettsia express four large, surface-exposed autotransporters, at least one of which is a known virulence determinant. Autotransporter translocation to the bacterial outer surface, also known as type V secretion, involves formation of a β-barrel autotransporter domain in the periplasm that inserts into the outer membrane to form a pore through which the N-terminal passenger domain is passed and exposed on the outer surface. Two major surface antigens of Rickettsia rickettsii, are known to be surface exposed and the passenger domain cleaved from the autotransporter domain. A highly passaged strain of R. rickettsii, Iowa, fails to cleave these autotransporters and is avirulent. We have identified a putative peptidase, truncated in the Iowa strain, that when reconstituted into Iowa restores appropriate processing of the autotransporters as well as restoring a modest degree of virulence.
    MeSH term(s) Rickettsia rickettsii/genetics ; Type V Secretion Systems/genetics ; Peptide Hydrolases ; Bacterial Outer Membrane Proteins ; Virulence Factors
    Chemical Substances Type V Secretion Systems ; Peptide Hydrolases (EC 3.4.-) ; Bacterial Outer Membrane Proteins ; Virulence Factors
    Language English
    Publishing date 2023-07-31
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1011527
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Expression and targeting of secreted proteins from Chlamydia trachomatis.

    Bauler, Laura D / Hackstadt, Ted

    Journal of bacteriology

    2014  Volume 196, Issue 7, Page(s) 1325–1334

    Abstract: Chlamydia trachomatis is an obligate intracellular pathogen that replicates in a vacuole termed the inclusion. Many of the interactions of chlamydiae with the host cell are dependent upon bacterial protein synthesis and presumably exposure of these ... ...

    Abstract Chlamydia trachomatis is an obligate intracellular pathogen that replicates in a vacuole termed the inclusion. Many of the interactions of chlamydiae with the host cell are dependent upon bacterial protein synthesis and presumably exposure of these proteins to the cytosol. Because of the dearth of genetic tools for chlamydiae, previous studies examining secreted proteins required the use of heterologous bacterial systems. Recent advances in genetic manipulation of chlamydia now allow for transformation of the bacteria with plasmids. We describe here a shuttle vector system, pBOMB4, that permits expression of recombinant proteins under constitutive or conditional promoter control. We show that the inclusion membrane protein IncD is secreted in a type III-dependent manner from Yersinia pseudotuberculosis and also secreted from C. trachomatis in infected cells where it localizes appropriately to the inclusion membrane. IncD truncated of the first 30 amino acids containing the secretion signal is no longer secreted and is retained by the bacteria. Cytosolic exposure of secreted proteins can be confirmed by using CyaA, GSK, or microinjection assays. A protein predicted to be retained within the bacteria, NrdB is indeed localized to the chlamydia. In addition, we have shown that the chlamydial effector protein, CPAF, which is secreted into the host cell cytosol by a Sec-dependent pathway, also accesses the cytosol when expressed from this system. These assays should prove useful to assess the secretion of other chlamydial proteins that are potentially exposed to the cytosol of the host cell.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Chlamydia Infections/microbiology ; Chlamydia trachomatis/genetics ; Chlamydia trachomatis/metabolism ; Cytoplasm/genetics ; Cytoplasm/metabolism ; Cytosol/metabolism ; Gene Expression Regulation, Bacterial ; Humans ; Molecular Sequence Data ; Protein Transport
    Chemical Substances Bacterial Proteins
    Language English
    Publishing date 2014-01-17
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.01290-13
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Ud II Zs.50: Show issues Location:
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