anthrax/phosphatase

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Reduced expression of CD45 protein-tyrosine phosphatase provides protection against anthrax pathogenesis.

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The modulation of cellular processes by small molecule inhibitors, gene inactivation, or targeted knockdown strategies combined with phenotypic screens are powerful approaches to delineate complex cellular pathways and to identify key players involved in disease pathogenesis. Using chemical genetic

HDAC8 Prevents Anthrax Lethal Toxin-induced Cell Cycle Arrest through Silencing PTEN in Human Monocytic THP-1 Cells.

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Anthrax lethal toxin (LeTx) is a cytotoxic virulence factor that causes cell cycle arrest and cell death in various cell types. However, susceptibility to the cytotoxic effects varies depending on cell types. In proliferating monocytes, LeTx has only transient cytotoxic effects due to activation of

Pharmacophore selection and redesign of non-nucleotide inhibitors of anthrax edema factor.

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Antibiotic treatment may fail to protect individuals, if not started early enough, after infection with Bacillus anthracis, due to the continuing activity of toxins that the bacterium produces. Stable and easily stored inhibitors of the edema factor toxin (EF), an adenylyl cyclase, could save lives

[Inhalation anthrax in a textile worker: non-fatal course].

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The development of dyspnea, hematemesis, melaena and symptoms of shock following an apparently minor infection of the upper respiratory tract in a 37-year-old textile worker marked the onset of an acute threatening illness. Pleuracentesis revealed 3.8 l of hemorrhagic exudate. Chest x-rays showed a

Finding the smoking gun: protein tyrosine phosphatases as tools and targets of unicellular microorganisms and viruses.

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Protein tyrosine phosphatases (PTPs) are increasingly recognized as important effectors of host-pathogen interactions. Since Guan and Dixon reported in 1990 that phosphatase YopH serves as an essential virulence determinant of Yersinia, the field shifted significantly forward, and dozens of PTPs

Anthrax lethal toxin induces acute diastolic dysfunction in rats through disruption of the phospholamban signaling network.

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BACKGROUND Anthrax lethal toxin (LT), secreted by Bacillus anthracis, causes severe cardiac dysfunction by unknown mechanisms. LT specifically cleaves the docking domains of MAPKK (MEKs); thus, we hypothesized that LT directly impairs cardiac function through dysregulation of MAPK signaling

Calyculin A sensitive protein phosphatase is required for Bacillus anthracis lethal toxin induced cytotoxicity.

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Previous studies have shown that the Bacillus anthracis lethal toxin can induce both necrosis and apoptosis in mouse macrophage-like J774A.1 cells depending on both the toxin concentration and the phosphatase activity. In this study several protein kinase or phosphatase inhibitors were employed to

Cytotoxic effects of anthrax lethal toxin on macrophage-like cell line J774A.1.

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The cytotoxic effects of anthrax lethal toxin purified from an avirulent strain were examined on mouse macrophage-like J774A.1 cells. Cell death induced by high concentration of purified lethal toxin had the characteristics of necrosis. At lower concentrations, the toxin caused no morphological

[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

A semi-synthetic ion channel platform for detection of phosphatase and protease activity.

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Sensitive methods to probe the activity of enzymes are important for clinical assays and for elucidating the role of these proteins in complex biochemical networks. This paper describes a semi-synthetic ion channel platform for detecting the activity of two different classes of enzymes with high

Regulatory interactions of a virulence-associated serine/threonine phosphatase-kinase pair in Bacillus anthracis.

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In the current study, we examined the regulatory interactions of a serine/threonine phosphatase (BA-Stp1), serine/threonine kinase (BA-Stk1) pair in Bacillus anthracis. B. anthracis STPK101, a null mutant lacking BA-Stp1 and BA-Stk1, was impaired in its ability to survive within macrophages, and

Novel inhibitors of anthrax edema factor.

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Several pathogenic bacteria produce adenylyl cyclase toxins, such as the edema factor (EF) of Bacillus anthracis. These disturb cellular metabolism by catalyzing production of excessive amounts of the regulatory molecule cAMP. Here, a structure-based method, where a 3D-pharmacophore that fit the

Identification and characterization of Bacillus anthracis by multiplex PCR on DNA chip.

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Bacillus anthracis can be identified by detecting virulence factor genes located on two plasmids, pXO1 and pXO2. Combining multiplex PCR with arrayed anchored primer PCR and biotin-avidin alkaline phosphatase indicator system, we developed a qualitative DNA chip method for characterization of B.

Comparative genomic study of spo0E family genes and elucidation of the role of Spo0E in Bacillus anthracis.

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The propensity of bacterium to sporulate or retain the vegetative form depends on the amount of phosphorylated Spo0A (Spo0A(-P)), regulated by Spo0E multigene family of phosphatases (Spo0E, YisI and YnzD). Phylogenetic analysis revealed that Spo0E multigene family of phosphatases (SMFP) descends in

GroEL Mediates Folding of Bacillus anthracis Serine/Threonine Protein Kinase, PrkC.

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Bacillus anthracis causes anthrax in human and animals. Both, signaling system such as two component system and endogenous chaperone system such as GroEL-GroES help bacteria to cope with the environmental challenges. Such molecular chaperones are the stress induced proteins that help bacteria to

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