Electron microscopic studies of the rickettsia <i>Coxiella burnetii</i>: entry, lysosomal response, and fate of rickettsial DNA in L-cells

Burton, Paul R.; Kordová, Nonna; Paretsky, D.

doi:10.1139/m71-025

Cited by 79 publications

(74 citation statements)

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“…2). Furthermore, the vacuole contains lysosomal hydrolytic enzymes such as acid phosphatase (1,28,95), cathepsin D (73,88), and 5Ј-nucleotidase (28), suggesting that the RCV is phenotypically similar to lysosomes.…”

Section: Coxiella Burnetiimentioning

confidence: 99%

Manipulation of Rab GTPase Function by Intracellular Bacterial Pathogens

Brumell

Scidmore

2007

Microbiol Mol Biol Rev

189

201

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SUMMARY Intracellular bacterial pathogens have evolved highly specialized mechanisms to enter and survive within their eukaryotic hosts. In order to do this, bacterial pathogens need to avoid host cell degradation and obtain nutrients and biosynthetic precursors, as well as evade detection by the host immune system. To create an intracellular niche that is favorable for replication, some intracellular pathogens inhibit the maturation of the phagosome or exit the endocytic pathway by modifying the identity of their phagosome through the exploitation of host cell trafficking pathways. In eukaryotic cells, organelle identity is determined, in part, by the composition of active Rab GTPases on the membranes of each organelle. This review describes our current understanding of how selected bacterial pathogens regulate host trafficking pathways by the selective inclusion or retention of Rab GTPases on membranes of the vacuoles that they occupy in host cells during infection.

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Section: Coxiella Burnetiimentioning

confidence: 99%

Manipulation of Rab GTPase Function by Intracellular Bacterial Pathogens

Brumell

Scidmore

2007

Microbiol Mol Biol Rev

189

201

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“…The organism is a moderate acidophile (Hackstadt, 1983 ; Hackstadt & Williams, 198 1 a), and parasitizes the phagolysosomal compartments of animal-host cells (Akporiaye et al, 1983;Burton et al, 1971Burton et al, , 1978. Although C. burnetii cannot be cultured in axenic media, both catabolic and anabolic reactions can be measured outside host cells in defined media, provided that the pH is in the range 44-55 (Hackstadt, 1983;Hackstadt & Williams 1981a, b, c, 1983Hendrix & Mallavia, 1984;Thompson et al, 1984;Zuerner & Thompson, 1983).…”

Section: Introductionmentioning

confidence: 99%

Isolated Coxiella burnetii synthesizes DNA during acid activation in the absence of host cells

Chen

Vodkin²,

Thompson³

et al. 1990

Journal of General Microbiology

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Two populations of CoxieIlu burnetii were isolated from fibroblast tissue cultures and examined for their ability to synthesize DNA when incubated in a defined medium. Both the populations released by mechanical lysis of heavily infected host cells, as well as those recovered from the tissue culture medium, incorporated H332P04 into DNA. Incorporation occurred at pH 4.5 but not at pH 7-0, and proceeded for 12-15 h. When incorporation of [ 3H]thymidine was studied, only the organisms obtained by mechanical lysis of host cells were active. Those which had been released by natural means into the tissue culture medium, and then recovered for study, did not incorporate precursor thymidine but were extremely active in protein biosynthesis. In mechanically released organisms, thymidine incorporation was inhibited immediately by rifamycin (40 p~) and hydroxyurea (10 mM), but it was not affected by chloramphenicol(310 p~) until 4 h after addition of the drug. Incorporation of H332P04 by both populations of organisms was also inhibited by rifamycin, chloramphenicol and hydroxyurea, but the time sequence of inhibition differed. Southern hybridization utilizing 32P-labelled DNA suggested that both populations synthesized authentic chromosomal DNA sequences, as well as QpHl plasmid DNA, during acid activation of metabolism .

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“…In animal cell lines, NMI and NMII replicate equally in vacuoles that fully mature to contain lysosomal markers (5). For example, PVs harboring replicating NMI in murine L-929 fibroblasts and J774 macrophages clearly fuse with lysosomes, as evidenced by the presence of active acid phosphatase and 5Ј-nucleotidase (2,11,25). NMII has also recently been demonstrated to replicate in a cathepsin D-positive vacuole in human HeLa epithelial cells (1).…”

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confidence: 99%