anthrax/protease

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Full Sequence Amino Acid Scanning of θ-Defensin RTD-1 Yields a Potent Anthrax Lethal Factor Protease Inhibitor.

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θ-Defensin RTD-1 is a noncompetitive inhibitor of anthrax lethal factor (LF) protease (IC50 = 390 ± 20 nM, Ki = 365 ± 20 nM) and a weak inhibitor of other mammalian metalloproteases such as TNFα converting enzyme (TACE) (Ki = 4.45 ± 0.48 μM). Using full sequence amino acid scanning in combination

Anthrax lethal factor protease inhibitors: synthesis, SAR, and structure-based 3D QSAR studies.

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We have recently identified a series of compounds that efficiently inhibit anthrax lethal factor (LF) metallo-protease. Here we present further structure-activity relationship and CoMFA (comparative molecular field analysis) studies on newly derived inhibitors. The obtained 3D QSAR model was

Activation of plasminogen activator inhibitor implicates protease InhA in the acute-phase response to Bacillus anthracis infection.

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Anthrax is a zoonotic disease caused by Bacillus anthracis. The infection is associated with inflammation and sepsis, but little is known about the acute-phase response during disease and the nature of the bacterial factors causing it. In this study, we examined the levels of the acute-phase

Mixed-type noncompetitive inhibition of anthrax lethal factor protease by aminoglycosides.

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We report a detailed kinetic investigation of the aminoglycosides neomycin B and neamine as inhibitors of the lethal factor protease from Bacillus anthracis. Both inhibitors display a mixed-type, noncompetitive kinetic pattern, which suggests the existence of multiple enzyme-inhibitor binding sites

Cationic polyamines inhibit anthrax lethal factor protease.

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BACKGROUND Anthrax is a human disease that results from infection by the bacteria, Bacillus anthracis and has recently been used as a bioterrorist agent. Historically, this disease was associated with Bacillus spore exposure from wool or animal carcasses. While current vaccine approaches (targeted

Purification and biophysical characterization of the core protease domain of anthrax lethal factor.

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Anthrax lethal toxin (LeTx) stands for the major virulence factor of the anthrax disease. It comprises a 90kDa highly specific metalloprotease, the anthrax lethal factor (LF). LF possesses a catalytic Zn(2+) binding site and is highly specific against MAPK kinases, thus representing the most potent

Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin.

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Proteolytic cleavage of the protective antigen (PA) protein of anthrax toxin at residues 164-167 is necessary for toxic activity. Cleavage by a cellular protease at this sequence, Arg-Lys-Lys-Arg, normally follows binding of PA to a cell surface receptor. We attempted to identify this protease by

Anthrax protective antigen is a calcium-dependent serine protease.

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Bacillus anthracis secretes a three component exotoxin-complex, which contributes to anthrax pathogenesis. Formation of this complex starts with the binding of protective antigen (PA) to its cellular receptor. In this study, we report that PA is a calcium-dependent serine protease and that the

Targeting the membrane-anchored serine protease testisin with a novel engineered anthrax toxin prodrug to kill tumor cells and reduce tumor burden.

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The membrane-anchored serine proteases are a unique group of trypsin-like serine proteases that are tethered to the cell surface via transmembrane domains or glycosyl-phosphatidylinositol-anchors. Overexpressed in tumors, with pro-tumorigenic properties, they are attractive targets for

Low molecular weight inhibitors of the protease anthrax lethal factor.

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Anthrax Lethal Factor (LF) is a zinc-dependent metalloprotease that together with the protective antigen constitute the anthrax lethal toxin, the most prominent virulence factor of the disease anthrax. This review summarizes the current knowledge on anthrax toxicity and defense in relation to LF.

Selectively guanidinylated derivatives of neamine. Syntheses and inhibition of anthrax lethal factor protease.

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A series of mono-, di-, and tri-guanidinylated derivatives of neamine were prepared via selective guanidinylation of neamine. These molecules represent a novel scaffold as inhibitors of anthrax lethal factor zinc metalloprotease. Methods for the synthesis of these compounds are described, and

Ultrasensitive detection of protease activity of anthrax and botulinum toxins by a new PCR-based assay.

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Anthrax and botulism are dangerous infectious diseases that can be fatal unless detected and treated quickly. Fatalities from these diseases are primarily due to endopeptidase toxins secreted by the pathogens. Rapid and sensitive detection of the presence of active toxins is the key element for

Feeding Anthrax: The Crystal Structure of Bacillus anthracis InhA Protease.

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Pathogenic bacteria secrete proteases to evade host defense and to acquire nutrients. In this issue of Structure, Arolas et al. (2016) describe the structural basis of activation and latency of InhA, a major secreted protease of Bacillus anthracis.

Small-molecule inhibitors of lethal factor protease activity protect against anthrax infection.

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Bacillus anthracis, the causative agent of anthrax, manifests its pathogenesis through the action of two secreted toxins. The bipartite lethal and edema toxins, a combination of lethal factor or edema factor with the protein protective antigen, are important virulence factors for this bacterium. We

Auranofin protects against anthrax lethal toxin-induced activation of the Nlrp1b inflammasome.

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Anthrax lethal toxin (LT) is the major virulence factor for Bacillus anthracis. The lethal factor (LF) component of this bipartite toxin is a protease which, when transported into the cellular cytoplasm, cleaves mitogen-activated protein kinase kinase (MEK) family proteins and induces rapid toxicity

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