This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsNotes
- 1.
1 Upon histopathological examination of tissue sections stained with hematoxylin & eosin, apoptosis is typically described as a so-called single- or individual-cell death, which requires additional confirmation of its origin by other methods
References
Smith H, Keppie J, Stainley JL (1955) The chemical basis of the virulence of Bacillus anthracis. V. The specific toxin produced by B. anthracis in vivo. Br J Exp Pathol 36:460–472.
Lincoln RE, Walker JS, Klein F, Haines BW (1964) Anthrax. Adv Vet Sci 9:327–368.
Fellows PF, Linscott MK, Ivins BE, Pitt ML, Rossi CA, Gibbs PH, Friedlander AM (2001) Efficacy of a human anthrax vaccine in guinea pigs, rabbits, and rhesus macaques against challenge by Bacillus anthracis isolates of diverse geographical origin. Vaccine 19:3241–3247.
Smith H, Keppie JL (1954) Observations on experimental anthrax: demonstration of a lethal factor produced in vivo by Bacillus anthracis. Nature 163:869–870.
Thorne CB, Molnar DM, Strange RE (1960) Production of toxin in vitro by Bacillus anthracis and its separation into two components. J Bacteriol 79:450–455.
Fish DC, Lincoln RE (1967) Biochemical and biophysical characterization of anthrax toxin. Fed Proc 26:1534–1538.
Stanley JL, Smith H (1961) Purification of factor I and recognition of a third factor of the anthrax toxin. J Gen Microbiol 26:49–66.
Pezard C, Berche P, Mock M (1991) Contribution of individual toxin components to virulence of Bacillus anthracis. Infect Immun 59:3472–3477.
Welkos SL, Keener TJ, Gibbs PH (1986) Differences in susceptibility of inbred mice to Bacillus anthracis. Infect Immun 51:795–800.
Welkos SL (1991) Plasmid-associated virulence factors of non-toxigenic (pX01-) Bacillus anthracis. Microb Pathol 10:183–198.
Cataldi A, Mock M, Bentancor L (2000) Characterization of Bacillus anthracis strains used for vaccination. J Appl Micro-biol 88:648–654.
Mikshis NI, Eremin SA, Bolotnikova MF (1999)[[Correlation of the virulence of Bacillus anthracis with expression of signs, coded for by chromosomal genes][Article in Russian]. Mol Gen Mikrobiol Virusol 3:25–28.
Stepanov AS, Mikshis NI, Eremin SA, Bolotnikova MF (1999)[Contribution of determinants, located in Bacillus anthracis chromosomes, in realizing the pathogenic properties of the pathogen][Article in Russian] Mol Gen Mikrobiol Virusol 1:20–23.
Klichko VI, Miller J, Wu A, Popov SG, Alibek K (2003) Anaerobic induction of Bacillus anthracis hemolytic activity. Biochem Biophys Res Commun 303:855–862.
Drobniewski FA (1993) Bacillus cereus and related species. Clin Microbiol Rev 6:324–338.
Akesson A, Hedstrom SA, Ripa T (1991) Bacillus cereus: a significant pathogen in postoperative and post-traumatic wounds on orthopaedic wards. Scand J Infect Dis 23:71–77.
David DB, Kirkby GR, Noble BA (1994) Bacillus cereus endophthalmitis. Br J Ophthalmol 78:577–580.
Turnbull PC, French TA, Dowsett EG (1977) Severe systemic and pyogenic infections with Bacillus cereus. Br Med J 1:1628–1629.
Helgason E, Okstad OA, Caugant DA, Johansen HA, Fouet A, Mock M, (2000) Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis—one species on the basis of genetic evidence. Appl Environ Microbiol 66:2627–2630.
Read TD, Peterson SN, Tourasse N, Baillie LW, Paulsen IT, Nelson KE, et al (2003) The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria. Nature 423:81–86.
Ivanova N, Sorokin A, Anderson I, Galleron N, Candelon B, Kapatral V, et al (2003) Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis. Nature 423:87–91.
Pannucci J, Okinaka RT, Sabin R, Kuske CR (2002) Bacillus anthracis pXO1 plasmid sequence conservation among closely related bacterial species. J Bacteriol 184:134–41.
Hoffmaster AR, Hill KK, Gee JE, Marston CK, De BK, Popo-vic T, et al (2006) Characterization of Bacillus cereus isolates associated with fatal pneumonias: strains are closely related to Bacillus anthracis and harbor B. anthracis virulence genes. J Clin Microbiol 44:3352–3360.
Friedlander A (2001) Tackling anthrax. Nature 414:160–161.
Bonventre PF, Eckert NJ (1963) The biologic activities of Bacillus anthracis and Bacillus cereus culture filtrates. Am J Pathol 43:201–211.
Eckert NJ, Bonventre PF (1963) In vivo effects of Bacillus anthracis culture filtrates. J Inf Dis 112:226–232.
Ezepchuk IuV, Bobkova ED, Prosvetova NK (1969)[On the toxic and various biochemical properties of filtrates of B. anthracis and cereus][Article in Russian] Zh Mikrobiol Epidemiol Immunobiol 46:19–23.
Moayeri M, Haines D, Young HA, Leppla SH (2003) Bacillus anthracis lethal toxin induces TNF-alpha-independent hypoxia-mediated toxicity in mice. J Clin Invest 112:670–682.
Cui X, Moayeri M, Li Y L i X, Haley M, Fitz Y, et al (2004) Lethality during continuous anthrax lethal toxin infusion is associated with circulatory shock but not inflammatory cytokine or nitric oxide release in rats. Am J Physiol Regul Integr Comp Physiol 286:R699–709.
Inglesby TV, Henderson DA, Bartlett JG, Ascher MS, Eitzen E, Friedlander AM, et al (1999) Anthrax as a biological weapon: medical and public health management. Working Group on Civilian Biodefense. JAMA 281:1735–1745.
Grinberg LM, Abramova FA, Yampolskaya OV, Walker DH, Smith JH (2001) Quantitative pathology of inhalational anthrax I: quantitative microscopic findings. Mod Pathol 14:482–495.
Friedlander AM (1986) Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J Biol Chem 261:7123–7126.
Hanna PC, Acosta D, Collier RJ (1993) On the role of macrophages in anthrax. Proc Natl Acad Sci USA 90:10198–10201.
Hanna PC, Kruskal B, Ezekowitz R, et al(1994) Role of macrophages oxidative burst in the action of anthrax lethal toxin. Mol Med 1:7–18.
Klein F, Walker JS, Fitzpatrick DF, Lincoln RE, Mahlandt BG, Jones WI, et al. Jr(1966) Pathophysiology of anthrax. J Infect Dis 116:123–138.
Shannon JG, Ross CL, Koehler TM, Rest RF (2003) Characterization of anthrolysin O, the Bacillus anthracis cholesterol-dependent cytolysin. Infect Immun 71:3183–3189.
Brown ER, Moody MD, Treece EL, Smith CW (1958) Differential diagnosis of Bacillus cereus, Bacillus anthracis, and Bacillus cereus var. Mycoides J Bacteriol 75:499–509.
Nordberg BK, Schmiterlow CG, Hansen HJ (1961) Pathophysiological investigations into the terminal course of experimental anthrax in the rabbit. Acta Pathol Microbiol Scand 53: 295 – 318.
MacFarland. J (1907) Pathogenic Bacteria, fifth edition. Sounders Co., Philadelphia and London.
Henderson DW, Peacock S, Belton FC (1956) Observations on the prophylaxis of experimental pulmonary anthrax in the monkey. J Hyg (Lond) 54:28–36.
Little SF, Ivins BE, Fellows PF, Friedlander AM (1997) Passive protection by polyclonal antibodies against Bacillus anthracis infection in guinea pigs. Infect Immun 65:5171–5175.
Ivins B, Fellows P, Pitt L, Estep J, Farchaus J, Friedlander A, Gibbs P (1995) Experimental anthrax vaccines: efficacy of adjuvants combined with protective antigen against an aerosol Bacillus anthracis spore challenge in guinea pigs. Vaccine 13:1779–1784.
Pitt ML, Little S, Ivins BE, Fellows P, Boles J, Barth J, et al (1999) In vitro correlate of immunity in an animal model of inhalational anthrax. J Appl Microbiol 87:304.
Welkos S, Little S, Friedlander A, Fritz D, Fellows P (2001) The role of antibodies to Bacillus anthracis and anthrax toxin components in inhibiting the early stages of infection by anthrax spores. Microbiology 147:1677–1685.
Cote CK, Rossi CA, Kang AS, Morrow PR, Lee JS, Welkos SL (2005) The detection of protective antigen (PA) associated with spores of Bacillus anthracis and the effects of anti-PA antibodies on spore germination and macrophage interactions. Microb Pathog 38:209–225.
Wintberry LK, Bondoc L, Park S, Simon L, Shih CN, Giri L (2000) Characterization of the US-licenced anthrax vaccine. Abstracts of Fourth International Conference on Anthrax. Annapolis, MD, p. 41.
Chaudry GJ, Moayeri M, Liu S, Leppla SH (2002) Quickening the pace of anthrax research: three advances point towards possible therapies. Trends Microbiol 10:58–62.
Tonello F, Seveso M, Marin O, Mock M, Montecucco C (2002) Screening inhibitors of anthrax lethal factor. Nature 418:386.
Mourez M, Lacy DB, Cunningham K, Legmann R, Sellman BR, Mogridge J, Collier RJ (2002) 2001: a year of major advances in anthrax toxin research Trends microbiol 10:287–298.
Sellman R, Mourez M, Collier J (2001) Dominant-negative mutants of a toxin subunit: an approach to therapy of anthrax. Science 292:695–697.
Min DH, Tang WJ, Mrksich M (2004) Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor. Nat Biotechnol 22:717–723.
Turk BE, Wong TY, Schwarzenbacher R, Jarrell ET, Leppla SH, Collier RJ, Liddington RC, Cantley LC (2004) The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor. Nat Struct Mol Biol 11:60–66.
Sarac MS, Peinado JR, Leppla SH, Lindberg I (2004) Protection against anthrax toxemia by hexa-D-arginine in vitro and in vivo. Infect Immun 72:602–605.
Popov SG, Popova TG, Grene E, Klotz F, Cardwell J, Bradburne C, et al (2004) Systemic cytokine response in murine anthrax. Cell Microbiol 6:226–233.
Popov SG, Villasmil R, Bernardi J, Grene E, Cardwell J W u A, et al (2002) Lethal toxin of Bacillus anthracis causes apoptosis of macrophages. Biochem Biopys Res Commun 293:349–355.
Popov SG, Villasmil R, Bernardi J, Grene E, Cardwell J, Pop-ova T, et al (2002) Effect of Bacillus anthracis lethal toxin on human peripheral blood mononuclear cells. FEBS Lett 527:211–215.
Forino M, Johnson S, Wong TY, Rozanov DV, Savinov AY, Li W, et al (2005) Efficient synthetic inhibitors of anthrax lethal factor. Proc Natl Acad Sci USA 102:9499–9504.
Shoop WL, Xiong Y, Wiltsie J, Woods A, Guo J, Pivnichny JV, et al (2005) Anthrax lethal factor inhibition. Proc Natl Acad Sci USA 102:7958–7963.
Pellizzari R, Guidi-Rontani C, Vitale G, Mock M, Montecucco C (1999) Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFN-γ-induced release of NO and TNF-α. FEBS Lett 462:199–204.
Erwin JL, DaSilva LM, Bavari S, Little SF, Freidlander AM, Chanh TC (2001) Macrophage-derived cell lines do not express proinflammatory cytokines after exposure to Bacillus anthracis lethal toxin. Inf Immun 69:1175–1177.
Hu H, Sa Q, Koehler TM, Aronson AI, Zhou D (2006) Inactivation of Bacillus anthracis spores in murine primary macrophages. Cell Microbiol 8:1634–1642.
Cite C, Rooijen NV, Welkos S (2006) Roles of macrophages and neutrophils in the early host response to bacillus anthracis spores in a mouse model of infection. Inf Immun 74:469–480.
Hanna PC, Acosta D, Collier RJ (1993) On the role of macrophages in anthrax. Proc Natl Acad Sci USA 90:10198–10201.
Hanna PC, Kruskal B, Ezekowitz R, et al (1994) Role of macrophages oxidative burst in the action of anthrax lethal toxin. Mol Med 1:7–18.
Friedlander AM (1986) Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J Biol Chem 261:7123–7126.
Moayeri M, Leppla S (2004) The role of anthrax lethal toxin in pathogenesis. Curr Opinion Microb 7:19–24.
Duesbery NS, Webb CP, Leppla SH, Gordon VM, Klimpel KR, Copeland TD, et al (1998) Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science 280:734–737.
Duffield JS. (2003) The inflammatory macrophage: a story of Jekyll and Hyde. Clin Sci (Lond) 104:27–38.
Kim SO, Jing Q, Hoebe K, Beutler B, Duesbery NS, Han J (2003) Sensitizing anthrax lethal toxin-resistant macrophages to lethal toxin-induced killing by tumor necrosis factor-alpha. J Biol Chem 278:7413–7421.
Park JM, Greten FR, Li Z-W, Karin M (2002) Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition. Science 297:2048–2051.
Holmstrom TH, Chow SC, Elo I, Coffey ET, Orrenius S, Sistonen L, Eriksson JE (1998) Suppression of Fas/APO-1-mediated apoptosis by mitogen-activated kinase signaling. J Immunol 160:2626–2636.
Pickering AK, Osorio M, Lee GM, Grippe VK, Bray M, Merkel TJ (2004) Cytokine response to infection with Bacillus anthracis spores. Infect Immun 72:6382–6389.
Hughes MA, Green CS, Lowchyj L, Lee GM, Grippe VK, Smith MF et al (2005) MyD88-dependent signaling contributes to protection following Bacillus anthracis spore challenge of mice: implications for Toll-like receptor signaling. Infect Immun 73:7535–7540.
Guidi-Rontani C, Weber-Levy M, Labruyere E, Mock M (1999) Germination of Bacillus anthracis spores within alveolar macrophages. Mol Microbiol 31:9–17.
Dixon TC, Fadl AA, Koehler TM, Swanson JA, Hanna PC (2000) Early Bacillus anthracis-macrophage interactions: intracellular survival and escape. Cell Microbiol 2:453–463.
Tournier JN, Quesnel-Hellmann A, Mathieu J, Montecucco J, Tang WJ, Mock M et al (2005) Anthrax edema toxin cooperates with lethal toxin impair cytokine secretion during infection of dendritic cells. J Immunol 174:4934–4941.
Heffernan BJ, Thomason B, Herring-Palmer A, Hanna PC (in press) Functional interactions of Bacillus anthracis anthrolysin O and three phospholipases C in a murine model of inhalation anthrax.
Grinberg LM, Abramova FA, Yampolskaya OV, Walker DH, Smith JH (2001) Quantitative pathology of inhalational anthrax I: quantitative microscopic findings. Mod Pathol 14:482–495.
Szabo G, Romics L JrFrendl G (2002) Liver in sepsis and systemic inflammatory response syndrome. Clin Liver Dis 6:1045–1046.
Phillips MJ, Poucell S, Patterson J, Valencia P (1987) The Liver: An Atlas and Text of Structural Pathology, pp. 1–32, Raven Press, New York.
Savill J, Fadok V, Henson P, Haslett C (1993) Phagocyte recognition of cells undergoing apoptosis. Immunol Today 14:131–136.
Platt N, Silva RP, daGordon S (1998) Recognizing death: the phagocytosis of apoptotic cells. Trends Cell Biol 8:365–372.
Giles KM, Hart SP, Haslett C, Rossi AG, Dransfield I (2000) An appetite for apoptotic cells? Controversies and challenges. Br J Haematol 109:1–12.
Faouzi S, Burckhardt BE, Hanson JC, Campe CB, Schrum L W, Rippe RA, Maher JJ (2001) Anti-Fas induces hepatic chemokines and promotes inflammation by an NF-kappa B-independent, caspase-3-dependent pathway. J Biol Chem 276:49077–49082.
Hohlbaum AM, Gregory MS, Ju ST, Marshak-Rothstein A (2001) Fas ligand engagement of resident peritoneal macrophages in vivo induces apoptosis and the production of neutrophil chemotactic factors. J Immunol 167:6217–6224.
Bozic CR, Kolakowski LF Jr, Gerard NP, Garcia-Rodriguez C, von Uexkull-Guldenband C, Conklyn MJ, et al (1995) Expression and biologic characterization of the murine chemokine KC. J Immunol 154:6048–6057.
Wade BH, Wright GG, Hewlett EL, Leppla SH, Mandell GL (1985) Anthrax toxin components stimulate chemotaxis of human polymorphonuclear neutrophils. Proc Soc Exp Biol Med 179:159–162.
Wanner GA, Mica L, Wanner-Schmid E, Kolb SA, Hentze H, Trentz O, Ertel W (1999) Inhibition of caspase activity prevents CD95-mediated hepatic microvascular perfusion failure and restores Kupffer cell clearance capacity. FASEB J 13:1239–1248.
Greaves P, Edwards R, Cohen GM, MacFarlane M (2001) ‘Have you seen this?’ Diffuse hepatic apoptosis. Toxicol Pathol 29:398–400.
Abramova FA, Grinberg LM, Yampolskaya OV, Walker DH (1993) Pathology of inhalational anthrax in 42 cases from the Sverdlovsk outbreak of 1979. Proc Natl Acad Sci USA 90:2291–2294.
Stearns-Kurosawa DJ, Lupu F, Taylor FB Jr Kinasewitz G, Kurosawa S (2006) Sepsis and pathophysiology of anthrax in a nonhuman primate model. Am J Pathol 169:433–444.
Smith H, Stoner HB (1967) Anthrax toxic complex. Fed Proc 26:1554–1557.
Warfel JM, Steele AD, D'Agnillo F (2005) Anthrax lethal toxin induces endothelial barrier dysfunction. Am J Pathol 166:1871–1881.
Culley NC, Pinson DM, Chakrabarty A, Mayo MS, Levine SM (2005) Pathophysiological manifestations in mice exposed to anthrax lethal toxin. Infect Immun 73:7006–7010.
Mikshis NI, Stepanov AS, Shevchenko OV, Eremin SA (1999)[The intrastrain heterogeneity of the causative agent of anthrax].[Article in Russian] Zh Mikrobiol Epidemiol Immunobiol 3:78–79.
Mignot T, Mock M, Robichon D, Landier A, Lereclus D, Fouet A (2001) The incompatibility between the PlcR- and AtxA-controlled regulons may have selected a nonsense mutation in Bacillus anthracis. Mol Microbiol 42:1189–1198.
Klichko VI, Miller J, Wu A, Popov SG, Alibek K (2003) Anaerobic induction of Bacillus anthracis hemolytic activity. Biochem Biophys Res Commun 303:855–862.
Thorne CB, Molnar DM, Stranger RE (1960) Production of toxin in vitro by Bacillus anthracis and its separation into two components. J Bacteriol 79:450–455.
Shannon JG, Ross CL, Koehler TM, Rest RF (2003) Characterization of anthrolysin O, the Bacillus anthracis cholesterol-dependent cytolysin. Infect Immun 71:3183–3189.
Popova TG, Millis B, Bradburne C, Nazarenko S, Bailey C, Chandhoke V, Popov SG (2006) Acceleration of epithelial cell syndecan-1 shedding by anthrax hemolytic virulence factors. BMC Microbiol 6:8–14.
Mosser EM, Rest RF (2006) The Bacillus anthracis cholesterol-dependent cytolysin, Anthrolysin O, kills human neutrophils, monocytes and macrophages. BMC Microbiol 6:56–60.
Park JM, Ng VH, Maeda S, Rest RF, Karin M (2004) Anthrolysin O and other gram-positive cytolysins are toll-like receptor 4 agonists. J Exp Med 200:1647–1655.
Popov SG, Popova TG, Hopkins S, Weinstein RS, MacAfee R, Fryxell K, et al (2005) Effective antiprotease-antibiotic treatment of experimental anthrax. BMC Infect Dis 5:25–39.
Chung MC, Popova TG, Millis BA, Mukherjee DV, Zhou W, Liotta LA, et al (2006) Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors. J Biol Chem 281:31408–31418.
Ramarao N, Lereclus D (2005) The InhA1 metalloprotease allows spores of the B. cereus group to escape macrophages. Cell Microbiol 7:1357–1364.
Park PW, Pier GB, Preston MJ, Goldberger O, Fitzgerald ML, Bernfield M (2000) Syndecan-1 shedding is enhanced by LasA, a secreted virulence factor of Pseudomonas aeruginosa. J Biol Chem 275:3057–3064.
Park PW, Pier GB, Hinkes MT, Bernfield M (2001) Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence. Nature 411:98–102.
Park PW, Foster TJ, Nishi E, Duncan SJ, Klagsbrun M, Chen Y (2004) Activation of syndecan-1 ectodomain shedding by Staphylococcus aureus alpha-toxin and beta-toxin. J Biol Chem 279:251–258.
Vasconcelos D,Barnewall R,BabinM,HuntR, Estep J, Nielsen C, et al (2003) Pathology of inhalation anthrax in cynomolgus monkeys (Macaca fascicularis). Lab Invest 83:1201–1209.
Mun-Bryce S, Rosenberg GA (1998) Matrix metalloproteinases in cerebrovascular disease. J Cereb Blood Flow Metab 18:1163–1172.
Li L, Chaikof EL (2002) Mechanical stress regulates syndecan-4 expression and redistribution in vascular smooth muscle cells. Arterioscler Thromb Vasc Biol 22:61–68.
Higashiyama S, Nanba D (2005) ADAM-mediated ectodomain shedding of HB-EGF in receptor cross-talk. Biochim Biophys Acta 1751:110–117.
Timmermann M, Hogger P (2005) Oxidative stress and 8-iso-prostaglandin F(2alpha) induce ectodomain shedding of CD163 and release of tumor necrosis factor-alpha from human monocytes. Free Radic Biol Med 39:98–107.
Aktories K, Barbieri JT (2005) Bacterial cytotoxins: targeting eukaryotic switches. Nat Rev Microbiol 3:397–410.
Kato M, Saunders S, Nguyen H, Bernfield M (1995) Loss of cell surface syndecan-1 causes epithelia to transform into anchorage-independent mesenchyme-like cells. Mol Biol Cell 6:559–576.
Beauvais DM, Rapraeger AC (2004) Syndecans in tumor cell adhesion and signaling. Reprod Biol Endocrinol 2:3–15.
Moayeri M, Webster JI, Wiggins JF, Leppla SH, Sternberg EM (2005) Endocrine perturbation increases susceptibility of mice to anthrax lethal toxin. Infect Immun 73:4238–4244.
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 2008 Humana Press, a part of Springer Science+Business Media, LLC
About this paper
Cite this paper
Popov, S.G. (2008). New Candidate Anthrax Pathogenic Factors. In: Georgiev, V.S., Western, K.A., McGowan, J.J. (eds) National Institute of Allergy and Infectious Diseases, NIH. Infectious Disease. Humana Press. https://doi.org/10.1007/978-1-59745-569-5_4
Download citation
DOI: https://doi.org/10.1007/978-1-59745-569-5_4
Publisher Name: Humana Press
Print ISBN: 978-1-934115-77-0
Online ISBN: 978-1-59745-569-5
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)