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      Validated MALDI-TOF-MS method for anthrax lethal factor provides early diagnosis and evaluation of therapeutics

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          Abstract

          Anthrax lethal factor (LF) is a zinc-dependent endoprotease and a critical virulence factor for Bacillus anthracis, the causative agent of anthrax. The mass spectrometry (MS) method for total-LF quantification includes three steps; 1) LF specific antibody capture/concentration, 2) LF-specific hydrolysis of a peptide substrate, and 3) detection and quantification of LF-cleaved peptides by isotope-dilution MALDI-TOF/MS. Recombinant LF spiked plasma was used for calibration and quality control (QC) materials. Specificity was 100% from analysis of serum and plasma from 383 non-infected humans, 31 rabbits, and 24 rhesus macaques. Sensitivity was 100% from 32 human clinical anthrax cases including infections by inhalation, ingestion, cutaneous and injection exposures and experimental infections for 29 rabbits and 24 rhesus macaques with inhalation anthrax. Robustness evaluation included sample storage, serum and plasma, antimicrobial and antitoxin effects and long-term performance. Data from 100 independent runs gave detection limits 0.01 ng/mL (111 amol/mL) for the 4-h method and 0.0027 ng/mL (30 amol/mL) for an alternate 20-h method. QC precision ranged from 7.7 to 14.8% coefficient of variation and accuracy from 0.2 to 9.8% error. The validated LF MS method provides sensitive quantification of anthrax total-LF using a robust high throughput platform for early diagnosis and evaluation of therapeutics during an anthrax emergency.

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          Most cited references35

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          Dose-Response Analysis Using R

          Dose-response analysis can be carried out using multi-purpose commercial statistical software, but except for a few special cases the analysis easily becomes cumbersome as relevant, non-standard output requires manual programming. The extension package drc for the statistical environment R provides a flexible and versatile infrastructure for dose-response analyses in general. The present version of the package, reflecting extensions and modifications over the last decade, provides a user-friendly interface to specify the model assumptions about the dose-response relationship and comes with a number of extractors for summarizing fitted models and carrying out inference on derived parameters. The aim of the present paper is to provide an overview of state-of-the-art dose-response analysis, both in terms of general concepts that have evolved and matured over the years and by means of concrete examples.
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            Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor.

            Anthrax lethal toxin, produced by the bacterium Bacillus anthracis, is the major cause of death in animals infected with anthrax. One component of this toxin, lethal factor (LF), is suspected to be a metalloprotease, but no physiological substrates have been identified. Here it is shown that LF is a protease that cleaves the amino terminus of mitogen-activated protein kinase kinases 1 and 2 (MAPKK1 and MAPKK2) and that this cleavage inactivates MAPKK1 and inhibits the MAPK signal transduction pathway. The identification of a cleavage site for LF may facilitate the development of LF inhibitors.
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              Anthrax toxin: receptor binding, internalization, pore formation, and translocation.

              Anthrax toxin consists of three nontoxic proteins that self-assemble at the surface of receptor-bearing mammalian cells or in solution, yielding a series of toxic complexes. Two of the proteins, called Lethal Factor (LF) and Edema Factor (EF), are enzymes that act on cytosolic substrates. The third, termed Protective Antigen (PA), is a multifunctional protein that binds to receptors, orchestrates the assembly and internalization of the complexes, and delivers them to the endosome. There, the PA moiety forms a pore in the endosomal membrane and promotes translocation of LF and EF to the cytosol. Recent advances in understanding the entry process include insights into how PA recognizes its two known receptors and its ligands, LF and EF; how the PA:receptor interaction influences the pH-dependence of pore formation; and how the pore functions in promoting translocation of LF and EF across the endosomal membrane.
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                Author and article information

                Journal
                0370535
                518
                Anal Biochem
                Anal Biochem
                Analytical biochemistry
                0003-2697
                1096-0309
                18 January 2021
                07 December 2017
                15 February 2018
                24 February 2021
                : 543
                : 97-107
                Affiliations
                [a ]Centers for Disease Control and Prevention, 4770 Buford Highway Mailstop F-50, Atlanta, GA 30341, USA
                [b ]Battelle Atlanta Analytical Services, 2987 Clairmont Road NE, Suite 450, Atlanta, GA 30329, USA
                [c ]Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30329, USA
                [d ]Battelle Biomedical Research Center, 1425 Plain City Georgesville Rd, West Jefferson, OH 43162, USA
                Author notes
                [* ]Corresponding author. aboyer@ 123456cdc.gov (A.E. Boyer).
                Article
                HHSPA1663402
                10.1016/j.ab.2017.12.007
                7904043
                29224733
                93c3b676-4d7f-42f8-90cd-53e9b3ca3ad3

                This is an open access article under the CC BY-NC-ND license ( http://creativecommons.org/licenses/BY-NC-ND/4.0/).

                Categories
                Article

                Biochemistry
                bacillus anthracis,anthrax,bacterial protein toxin,lethal factor,enzyme activity,isotope-dilution mass spectrometry

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