Bacillus anthracis toxins

Liu, Shihui; Moayeri, Mahtab; Pomerantsev, Andrei P.; Leppla, Stephen H.

doi:10.1016/b978-0-12-800188-2.00013-6

Cited by 9 publications

(10 citation statements)

References 375 publications

(371 reference statements)

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“…EsxB is secreted through the ESAT-6 system 1 (ESX-1) T7SS of M. tuberculosis and has many homologues across Mycobacteria and other T7SS-containing bacteria ( 76 ). LF, one of three anthrax toxin components secreted by B. anthracis , is known as lethal factor; it is thought to be secreted through the classical Sec machinery ( 77 ) although to our knowledge this hasn’t been specifically demonstrated, but it has otherwise been found to reside within MVs with the two other anthrax toxin components ( 78 ). SrpC is one of three serine rich proteins that, due to its extensive post-translational glycosylation, is secreted through the accessory SecA2 system by Streptococcus salivarius ( 79 ).…”

Section: Resultsmentioning

confidence: 99%

PncsHub: a platform for annotating and analyzing non-classically secreted proteins in Gram-positive bacteria

Dai

et al. 2021

Nucleic Acids Research

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From industry to food to health, bacteria play an important role in all facets of life. Some of the most important bacteria have been purposely engineered to produce commercial quantities of antibiotics and therapeutics, and non-classical secretion systems are at the forefront of these technologies. Unlike the classical Sec or Tat pathways, non-classically secreted proteins share few common characteristics and use much more diverse secretion pathways for protein transport. Systematically categorizing and investigating the non-classically secreted proteins will enable a deeper understanding of their associated secretion mechanisms and provide a landscape of the Gram-positive secretion pathway distribution. We therefore developed PncsHub (https://pncshub.erc.monash.edu/), the first universal platform for comprehensively annotating and analyzing Gram-positive bacterial non-classically secreted proteins. PncsHub catalogs 4,914 non-classically secreted proteins, which are delicately categorized into 8 subtypes (including the ‘unknown’ subtype) and annotated with data compiled from up to 26 resources and visualisation tools. It incorporates state-of-the-art predictors to identify new and homologous non-classically secreted proteins and includes three analytical modules to visualise the relationships between known and putative non-classically secreted proteins. As such, PncsHub aims to provide integrated services for investigating, predicting and identifying non-classically secreted proteins to promote hypothesis-driven laboratory-based experiments.

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Section: Resultsmentioning

confidence: 99%

PncsHub: a platform for annotating and analyzing non-classically secreted proteins in Gram-positive bacteria

Dai

et al. 2021

Nucleic Acids Research

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“…Pathogenicity of B. anthracis is mediated by three virulence factors: the capsule and two exotoxins . The virulence factor that most contributes to the deadly symptoms seen in infection is a three-protein toxin comprised of protective antigen (PA), lethal factor (LF), and edema factor (EF) . Interestingly, none of these toxins are virulent on their ownPA must combine either with LF to form lethal toxin (LT, LeT, or LeTx) or with EF to form edema toxin (ET). ,, LT is largely considered to be the primary virulence factor .…”

Section: Small-molecule Antivirulence Agentsmentioning

confidence: 99%

Chemical Strategies To Target Bacterial Virulence

2017

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Antibiotic resistance is a significant emerging health threat. Exacerbating this problem is the overprescription of antibiotics as well as a lack of development of new antibacterial agents. A paradigm shift toward the development of nonantibiotic agents that target the virulence factors of bacterial pathogens is one way to begin to address the issue of resistance. Of particular interest are compounds targeting bacterial AB toxins that have the potential to protect against toxin-induced pathology without harming healthy commensal microbial flora. Development of successful antitoxin agents would likely decrease the use of antibiotics, thereby reducing selective pressure that leads to antibiotic resistance mutations. In addition, antitoxin agents are not only promising for therapeutic applications, but also can be used as tools for the continued study of bacterial pathogenesis. In this review, we discuss the growing number of examples of chemical entities designed to target exotoxin virulence factors from important human bacterial pathogens.

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“…1a) and a family of related clostridial binary toxins, C2, iota, and CDT (Nestorovich et al 2011; Roeder et al 2014). Following intentional dissemination of Bacillus anthracis spores via the “anthrax letters” in Sept. 2001, quite remarkable developments were made in understanding molecular details of anthrax toxin uptake (Moayeri et al 2015; Liu et al 2015). Briefly, the tripartite anthrax toxin is released as three separate proteins, lethal factor (LF), edema factor (EF), and protective antigen (PA) that self-assemble at the host cell surface to form complexes contributing to the symptoms of anthrax.…”

Section: Multivalent Inhibitors Of Channel-forming Bacterial Exotoxinsmentioning

confidence: 99%

Multivalent Inhibitors of Channel-Forming Bacterial Toxins

Yamini

Nestorovich

2016

Current Topics in Microbiology and Immunology

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Rational design of multivalent molecules represents a remarkable modern tool to transform weak non-covalent interactions into strong binding by creating multiple finely-tuned points of contact between multivalent ligands and their supposed multivalent targets. Here, we describe several prominent examples where the multivalent blockers were investigated for their ability to directly obstruct oligomeric channel-forming bacterial exotoxins, such as the pore-forming bacterial toxins and B component of the binary bacterial toxins. We address problems related to the blocker/target symmetry match and nature of the functional groups, as well as chemistry and length of the linkers connecting the functional groups to their multivalent scaffolds. Using the anthrax toxin and AB5 toxin case studies, we briefly review how the oligomeric toxin components can be successfully disabled by the multivalent non-channel-blocking inhibitors, which are based on a variety of multivalent scaffolds.

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Bacillus anthracis toxins

Cited by 9 publications

References 375 publications

PncsHub: a platform for annotating and analyzing non-classically secreted proteins in Gram-positive bacteria

PncsHub: a platform for annotating and analyzing non-classically secreted proteins in Gram-positive bacteria

Chemical Strategies To Target Bacterial Virulence

Multivalent Inhibitors of Channel-Forming Bacterial Toxins

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