Inhibition of anthrax lethal factor by curcumin and chemically modified curcumin derivatives

References

• Mock M, Mignot T. Anthrax toxins and the host: a story of intimacy. Cell Microbiol 2003;5:15–23
   PubMed Web of Science ®Google Scholar
• Brittingham KC, Ruthel G, Panchal RG, et al. Dendritic cells endocytose Bacillus anthracis spores: implications for anthrax pathogenesis. J Immunol 2005;174:5545–52
   PubMed Web of Science ®Google Scholar
• Rosenberger CM, Finlay BB. Phagocyte sabotage: disruption of macrophage signalling by bacterial pathogens. Nat Rev Mol Cell Biol 2003;4:385–96
   PubMed Web of Science ®Google Scholar
• Dixon TC, Meselson M, Guillemin J, et al. Anthrax. N Engl J Med 1999;341:815–26
   PubMed Web of Science ®Google Scholar
• Tonello F, Montecucco C. The anthrax lethal factor and its MAPK kinase-specific metalloprotease activity. Mol Aspects Med 2009;30:431–8
   PubMed Web of Science ®Google Scholar
• Mastrolorenzo A, Supuran CT. Botulinus toxin, tetanus toxin, and anthrax lethal factor inhibitors. In: Supuran CT, Winum J-Y, eds. Drug design of zinc-enzyme inhibitors. Hoboken (NJ): John Wiley & Sons, Inc.; 2009:705–20
   Google Scholar
• Mock M, Fouet A. Anthrax. Ann Rev Microbiol 2001;55:647–71
   PubMed Web of Science ®Google Scholar
• Brossier F, Mock M. Toxins of Bacillus anthracis. Toxicon 2001;39:1747–55
   PubMed Web of Science ®Google Scholar
• Ezzell JW, Jr Abshire TG. Serum protease cleavage of Bacillus anthracis protective antigen. J Gen Microbiol 1992;138:543–9
   PubMedGoogle Scholar
• Abrami L, Liu S, Cosson P, et al. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J Cell Biol 2003;160:321–8
   PubMed Web of Science ®Google Scholar
• Hellmich KA, Levinsohn JL, Fattah R, et al. Anthrax lethal factor cleaves mouse nlrp1b in both toxin-sensitive and toxin-resistant macrophages. PLoS ONE 2012;7:e49741
   PubMed Web of Science ®Google Scholar
• Levinsohn JL, Newman ZL, Hellmich KA, et al. Anthrax lethal factor cleavage of Nlrp1 is required for activation of the inflammasome. PLoS Pathog 2012;8:e1002638
   PubMed Web of Science ®Google Scholar
• Pannifer AD, Wong TY, Schwarzenbacher R, et al. Crystal structure of the anthrax lethal factor. Nature 2001;414:229–33
   PubMed Web of Science ®Google Scholar
• Spyroulias GA, Galanis AS, Pairas G, et al. Structural features of angiotensin-I converting enzyme catalytic sites: conformational studies in solution, homology models and comparison with other zinc metallopeptidases. Curr Top Med Chem 2004;4:403–29
   PubMed Web of Science ®Google Scholar
• Popov SG, Popova TG, Hopkins S, et al. Effective antiprotease-antibiotic treatment of experimental anthrax. BMC Infect Dis 2005;5:25
   PubMed Web of Science ®Google Scholar
• Supuran CT, Scozzafava A, Clare BW. Bacterial protease inhibitors. Med Res Rev 2002;22:329–72
   PubMed Web of Science ®Google Scholar
• Gupta SC, Prasad S, Kim JH, et al. Multitargeting by curcumin as revealed by molecular interaction studies. Nat Prod Rep 2011;28:1937–55
   PubMed Web of Science ®Google Scholar
• Zhang Y, Golub LM, Johnson F, et al. pKa, zinc- and serum albumin-binding of curcumin and two novel biologically-active chemically-modified curcumins. Curr Med Chem 2012;19:4367–75
   PubMed Web of Science ®Google Scholar
• Ammon HP, Wahl MA. Pharmacology of curcuma longa. Planta Med 1991;57:1–7
   PubMed Web of Science ®Google Scholar
• Kunwar A, Barik A, Mishra B, et al. Quantitative cellular uptake, localization and cytotoxicity of curcumin in normal and tumor cells. Biochim Biophys Acta 2008;1780:673–9
   PubMed Web of Science ®Google Scholar
• Kocer SS, Walker SG, Zerler B, et al. Metalloproteinase inhibitors, nonantimicrobial chemically modified tetracyclines, and ilomastat block Bacillus anthracis lethal factor activity in viable cells. Infect Immun 2005;73:7548–57
   PubMed Web of Science ®Google Scholar
• Zhang Y, Gu Y, Lee HM, et al. Design, synthesis and biological activity of new polyenolic inhibitors of matrix metalloproteinases: a focus on chemically-modified curcumins. Curr Med Chem 2012;19:4348–58
   PubMed Web of Science ®Google Scholar
• Dell’Aica I, Dona M, Tonello F, et al. Potent inhibitors of anthrax lethal factor from green tea. EMBO Rep 2004;5:418–22
   PubMed Web of Science ®Google Scholar
• Gaddis BD, Rubert Perez CM, Chmielewski J. Inhibitors of anthrax lethal factor based upon N-oleoyldopamine. Bioorg Med Chem Lett 2008;18:2467–70
   PubMed Web of Science ®Google Scholar
• Numa MM, Lee LV, Hsu CC, et al. Identification of novel anthrax lethal factor inhibitors generated by combinatorial Pictet--Spengler reaction followed by screening in situ. ChemBioChem 2005;6:1002–6
   PubMed Web of Science ®Google Scholar
• Kochi SK, Schiavo G, Mock M, et al. Zinc content of the Bacillus anthracis lethal factor. FEMS Microbiol Lett 1994;124:343–8
   PubMed Web of Science ®Google Scholar
• Ezzell JW, Ivins BE, Leppla SH. Immunoelectrophoretic analysis, toxicity, and kinetics of in vitro production of the protective antigen and lethal factor components of Bacillus anthracis toxin. Infect Immun 1984;45:761–7
   PubMed Web of Science ®Google Scholar