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MeSH Review:

Bacillus anthracis

Xia, Z.G. et al., Paton, A.W. et al., Joyce, J. et al., Jones, M.B. et al., Vilalta, A. et al., et al.

Vitale, Bernardi, Napolitani, Mock, Montecucco, Popov, Popova, Grene, Klotz, Cardwell, Bradburne, Jama, Maland, Wells, Nalca, Voss, Bailey, Alibek, Hughes, Green, Lowchyj, Lee, Grippe, Smith, Huang, Harvill, Merkel, Vilalta, Mahajan, Hartikka, Leamy, Martin, Rusalov, Bozoukova, Lalor, Hall, Kaslow, Rolland, Duesbery, Resau, Webb, Koochekpour, Koo, Leppla, Vande Woude, Bell, Mackle, Sirimuthu, Jones, Jani, Ren, Wood, Blaser, Joyce, Cook, Chabot, Hepler, Shoop, Xu, Stambaugh, Aste-Amezaga, Wang, Indrawati, Bruner, Friedlander, Keller, Caulfield, Mina, Dym, Kuepper, Tso, Arrastia, Kaplounova, Faraj, Kwapniewski, Krol, Grosser, Glick, Fochios, Remolina, Vasovic, Moses, Robin, DeVita, Tapper,

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Disease relevance of Bacillus anthracis

Protective antigen (PA) is the central component of the three-part protein toxin secreted by Bacillus anthracis, the organism responsible for anthrax [1].
Protective antigen (PA) is a component of the Bacillus anthracis lethal and edema toxins and the basis of the current anthrax vaccine [2].
Large polypeptides of the Bacillus anthracis protective antigen (PA) were inserted into an influenza A virus hemagglutinin glycoprotein (HA), and the chimeric proteins were functionally characterized and incorporated into infectious influenza viruses [3].
A spontaneous translational fusion of Bacillus cereus PlcR and PapR activates transcription of PlcR-dependent genes in Bacillus anthracis via binding with a specific palindromic sequence [4].
The structural gene for the 90-kDa lethal factor (LF) isolated from Bacillus anthracis was expressed as a fusion protein with six histidine residues in Escherichia coli [5].

High impact information on Bacillus anthracis

For instance, infection of macrophages with the TLR4-activating bacterium Bacillus anthracis triggers an apoptotic response due to inhibition of p38 MAP kinase activation by the bacterial-produced lethal toxin [6].
Blood cultures, as well as DNA amplification by polymerase chain reaction of the blood, bronchial washings, and pleural fluid specimens, were positive for Bacillus anthracis [7].
Exposure of bone marrow-derived macrophages (BMDMs) to low concentrations of Bacillus anthracis lethal toxin (LT), whose catalytic subunit is lethal factor (LF), results in induction of a robust apoptotic response dependent on activation of Toll-like receptor (TLR)4 [8].
The A subunit is a subtilase-like serine protease distantly related to the BA_2875 gene product of Bacillus anthracis [9].
Lethal factor is a protease, one component of Bacillus anthracis exotoxin, which cleaves many of the mitogen-activated protein kinase kinases (MEKs) [10].

Chemical compound and disease context of Bacillus anthracis

It is shown here that EF is an adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] produced by Bacillus anthracis in an inactive form [11].
B. cereus produces beta-lactamases, unlike Bacillus anthracis, and so is resistant to beta-lactam antibiotics; it is usually susceptible to treatment with clindamycin, vancomycin, gentamicin, chloramphenicol, and erythromycin [12].
Novel oligosaccharide side chains of the collagen-like region of BclA, the major glycoprotein of the Bacillus anthracis exosporium [13].
The capsular polypeptide of Bacillus anthracis is composed of a unique polyglutamic acid polymer in which D-glutamate monomers are joined by gamma-peptidyl bonds [14].
Immunogenicity and protective efficacy of Bacillus anthracis poly-gamma-D-glutamic acid capsule covalently coupled to a protein carrier using a novel triazine-based conjugation strategy [14].

Biological context of Bacillus anthracis

A-type ATP binding consensus sequences are critical for the catalytic activity of the calmodulin-sensitive adenylyl cyclase from Bacillus anthracis [15].
This study has been extended to examine the amino acid sequence requirements of BLIP for binding to the SHV-1 beta-lactamase, which is a poor binding substrate (Ki= 1.1 microm), and the Bacillus anthracis Bla1 enzyme (Ki= 2.5 nm) [16].
The capsule of Bacillus anthracis is an important virulence factor consisting of poly-D-glutamic acid [17].
The gene encoding the protective antigen (PA) moiety of the tripartite exotoxin of Bacillus anthracis was cloned from the recombinant plasmid pSE36 into Bacillus subtilis 1S53 by using the plasmid vector pUB110 [18].
Principles of 3' splice site selection and alternative splicing for an unusual group II intron from Bacillus anthracis [19].

Anatomical context of Bacillus anthracis

A two-component direct fluorescent-antibody (DFA) assay, using fluorescein-labeled monoclonal antibodies specific to the Bacillus anthracis cell wall (CW-DFA) and capsule (CAP-DFA) antigens, was evaluated and validated for rapid identification of B. anthracis [20].
Dipicolinic acid (DPA) is an excellent marker compound for bacterial spores, including those of Bacillus anthracis (anthrax) [21].
Passive transfer of lymphocytes and sera from mice immunised using two different formulations containing recombinant protective antigen (rPA) have been used to further elucidate the mechanism of protection against Bacillus anthracis infection [22].

Gene context of Bacillus anthracis

We studied the effects on Bacillus anthracis growth and the virulence gene (pagA, lef, and cya) expression of the QS inhibitor (5Z)-4-bromo-5-(bromomethylene)-3-butyl-2(5H)-furanone, which is naturally synthesized by the marine alga Delisea pulchra, as well as a related compound and synthetic derivatives [23].
We determined the levels of IL-1 beta, IL-6 and TNF-alpha in serum of mice challenged with virulent (Ames) or attenuated (Sterne) strains of Bacillus anthracis [24].
Inhibition of mitogen-activated protein kinase signalling by Bacillus anthracis lethal toxin causes destabilization of interleukin-8 mRNA [25].
MyD88-dependent signaling contributes to protection following Bacillus anthracis spore challenge of mice: implications for Toll-like receptor signaling [26].
The lethal factor (LF) produced by toxigenic strains of Bacillus anthracis is a Zn(2+)-endopeptidase that cleaves the mitogen-activated protein kinase kinases (MAPKKs) MEK1, MEK2 and MKK3 [27].

Analytical, diagnostic and therapeutic context of Bacillus anthracis

To address this concern, a preclinical pDNA persistence/integration study was conducted in rabbits to determine the level of pDNA in muscle 2, 28, and 64 days after intramuscular injection of DMRIE:DOPE-formulated pDNAs encoding Bacillus anthracis detoxified LF and PA proteins (VCL-AB01 vaccine) [28].
Utilization of the rpoB gene as a specific chromosomal marker for real-time PCR detection of Bacillus anthracis [29].
Denaturing high-performance liquid chromatography (DHPLC) was evaluated as a method for identifying Bacillus anthracis by analyzing two chromosomal targets, the 16S-23S intergenic spacer region (ISR) and the gyrA gene [30].
Molecular cloning and expression of the Bacillus anthracis edema factor toxin gene: a calmodulin-dependent adenylate cyclase [31].
Indirect immunoradiometric assays (IRMA) for Bacillus anthracis spores are described in which the spores were heat fixed either on multispot microscope slides or on polyvinyl or polystyrene microtitre plates [32].

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