tularemia/phosphatase

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Neutrophile alkaline phosphatase changes in tularemia, sandfly fever, Q fever and noninfectious fevers.

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Combined deletion of four Francisella novicida acid phosphatases attenuates virulence and macrophage vacuolar escape.

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Francisella tularensis is a facultative intracellular pathogen and the etiologic agent of tularemia. It is capable of escape from macrophage phagosomes and replicates in the host cell cytosol. Bacterial acid phosphatases are thought to play a major role in the virulence and intracellular survival of

Inhibition of AcpA phosphatase activity with ascorbate attenuates Francisella tularensis intramacrophage survival.

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Acid phosphatase activity in the highly infectious intracellular pathogen Francisella tularensis is directly related with the ability of these bacteria to survive inside host cells. Pharmacological inactivation of acid phosphatases could potentially help in the treatment of tularemia or even be

Increased Resistance to Intradermal Francisella tularensis LVS Infection by Inactivation of the Sts Phosphatases.

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The Suppressor of TCR signaling proteins (Sts-1 and Sts-2) are two homologous phosphatases that negatively regulate signaling pathways in a number of hematopoietic lineages, including T lymphocytes. Mice lacking Sts expression are characterized by enhanced T cell responses. Additionally, a recent

Acid phosphatases do not contribute to the pathogenesis of type A Francisella tularensis.

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The intracellular pathogen Francisella tularensis is the causative agent of tularemia, a zoonosis that can affect humans with potentially lethal consequences. Essential to Francisella virulence is its ability to survive and proliferate within phagocytes through phagosomal escape and cytosolic

[Phosphatase and penicillinase activities as stable traits for the differentiation of the racial classification of Francisella tularensis].

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In the causative agent of tularemia new markers correlating with different subspecies of this microbe have been detected. Thus, F. tularensis strains belonging to the American and Central Asian subspecies are characterized by phosphatase activity, which makes it possible to use the phosphatase test

The acid phosphatase AcpA is secreted in vitro and in macrophages by Francisella spp.

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Francisella tularensis is a remarkably infectious facultative intracellular pathogen that causes the zoonotic disease tularemia. Essential to the pathogenesis of F. tularensis is its ability to escape the destructive phagosomal environment and inhibit the host cell respiratory burst. F. tularensis

Identification of Genes Required for Secretion of the Francisella Oxidative Burst-Inhibiting Acid Phosphatase AcpA.

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Francisella tularensis is a Tier 1 bioterror threat and the intracellular pathogen responsible for tularemia in humans and animals. Upon entry into the host, Francisella uses multiple mechanisms to evade killing. Our previous studies have shown that after entering its primary cellular host, the

[Cytochemical changes in the peripheral blood leukocytes of guinea pigs inoculated against plague, tularemia and anthrax].

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The immunization of guinea pigs with trivaccine and monovaccines against plaque, tularemia and anthrax induces a decrease in the activity of acidic phosphatase in lymphocytes, as well as a decrease in the number of lymphocytes containing this enzyme. A decrease in the activity of alkaline

Attenuated virulence of a Francisella mutant lacking the lipid A 4'-phosphatase.

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Francisella tularensis causes tularemia, a highly contagious disease of animals and humans, but the virulence features of F. tularensis are poorly defined. F. tularensis and the related mouse pathogen Francisella novicida synthesize unusual lipid A molecules lacking the 4'-monophosphate group

Characterization of recombinant Francisella tularensis acid phosphatase A.

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Francisella tularensis is the etiologic agent of the potentially fatal human disease tularemia and is capable of survival and multiplication within professional phagocytes of the host. While the mechanisms that allow intracellular survival of the bacterium are only now beginning to be elucidated at

Changes in whole blood and serum components of grivet monkeys with experimental respiratory Francisella tularensis infection.

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Grivet monkeys infected with virulent Francisella tularensis Strain Schu S4 showed significant early changes in serum levels of trace metals, triglycerides and activities of alkaline phosphatase, lactate dehydrogenase and alpha-hydroxybutyrate dehydrogenase. Free amino acid levels decreased slightly

Differential expression of microRNAs in Francisella tularensis-infected human macrophages: miR-155-dependent downregulation of MyD88 inhibits the inflammatory response.

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Francisella tularensis is a Gram-negative, facultative intracellular pathogen that replicates in the cytosol of macrophages and is the causative agent of the potentially fatal disease tularemia. A characteristic feature of F. tularensis is its limited proinflammatory capacity, but the mechanisms

Multiple mechanisms of NADPH oxidase inhibition by type A and type B Francisella tularensis.

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Ft is a facultative intracellular pathogen that infects many cell types, including neutrophils. In previous work, we demonstrated that the type B Ft strain LVS disrupts NADPH oxidase activity throughout human neutrophils, but how this is achieved is incompletely defined. Here, we used several type A

[Francisella tularensis--feature of pathogen, pathogenesis, diagnostics].

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Francisella tularensis belongs to the Francisellaceae family. There are four known subspecies of Francisella tularensis: tularensis, holarctica, mediasiatica and novicida. Fully virulent strains possess a capsule, which protects F. tularensis from bactericidal action of serum. The main virulen

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