Anthrax toxins

Cellular and Molecular Life Sciences

Volumn 55, Issue 12, 1999, Pages 1599-1609

  Duesbery, N S ^a,b   Vande Woude, G F ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b VAN ANDEL RESEARCH INSTITUTE   (United States)

Author keywords

Anthrax; Bacterial pathogens; Edema factor; Lethal factor; Mitogen activated protein kinases

Indexed keywords

ADENYLATE CYCLASE; ANTHRAX TOXIN; CELL RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; VIRULENCE FACTOR;

AMINO ACID SEQUENCE; ANTHRAX; BACILLUS ANTHRACIS; ENZYME INACTIVATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PATHOGENESIS; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; ANTHRAX; ANTIGENS, BACTERIAL; BACILLUS ANTHRACIS; BACTERIAL TOXINS; HUMANS; VIRULENCE;

EID: 0032827844     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050399     Document Type: Review

References (134)

1. Young G. A. Jr, Zelle M. R. and Lincoln R. E. (1946) Respiratory pathogenicity of Bacillus anthracis spores. I. Methods of study and observations on pathogenesis. J. Infect. Dis. 79: 233-246
2. Cromartie W. J., Bloom W. L. and Watson D. W. (1947) Studies on infection with Bacillus anthracis. I. A histopathological study of skin lesions produced by B. anthracis in susceptible and resistant animal species. J. Infect. Dis. 80: 1-13
3. Cromartie W. J., Watson D. W., Bloom W. L. and Heckly R. J. (1947) Studies on infection with Bacillus anthracis. II. The immunological and tissue damaging properties of extracts prepared from lesions of B. anthracis infection. J. Infect. Dis. 80: 14-27
4. Keppie J., Smith H. and Harris-Smith P. W. (1953) The chemical basis of the virulence of Bacillus anthracis. II. Some biological properties of bacterial products. Br. J. Exp. Pathol. 34: 486-496
5. Bloom W. L., McGhee W. J., Cromartie W. J. and Watson D. W. (1947) Studies on infection with Bacillus anthracis. VI. Physiological changes in experimental animals during the course of infection with B. anthracis. J. Infect. Dis. 80: 137-144
6. Smith H. and Keppie J. (1954) Observations on experimental anthrax: demonstration of a specific lethal factor produced in vivo by Bacillus anthracis. Nature 173: 869-870
7. Gladstone G. P. (1946) Immunity to anthrax: protective antigen present in cell-Free culture filtrates. Br. J. Exp. Pathol. 27: 394-418
8. Smith H., Tempest D. W., Stanley J. L., Harris-Smith P. W. and Gallop R. C. (1956) The chemical basis of the virulence of Bacillus anthracis. VII. Two components of the anthrax toxin: their relationship to known immunising aggressins. Br. J. Exp. Pathol. 37: 263-271
9. Harris-Smith P. W., Smith H. and Keppie J. (1958) Production in vitro of the toxin of Bacillus anthracis previously recognized in vivo. J. Gen. Microbiol. 19: 91-108
10. Thorne C. B., Molnar D. M. and Strange R. E. (1960) Production of toxin in vitro by Bacillus anthracis and its separation into two components. J. Bacteriol. 79: 450-455
11. Stanley J. L., Sargeant K. and Smith H. (1960) Purification of factors I and II of the anthrax toxin produced in vivo. J. Gen. Microbiol. 22: 206-218
12. Sargeant K., Stanley J. L. and Smith H. (1960) The serological relationship between purified preparations of factors I and II of the anthrax toxin produced in vivo and in vitro. J. Gen. Microbiol. 22: 219-228
13. Fish D. C., Klein F., Lincoln R. E., Walker J. S. and Dobbs J. P. (1968) Pathophysiological changes in the rat associated with anthrax toxin. J. Infect. Dis. 118: 114-124
14. Stanley J. L. and Smith H. (1961) Purification of factor I and recognition of a third factor of the anthrax toxin. J. Gen. Microbiol. 26: 49-66
15. Beall F. A., Taylor M. J. and Thorne C. B. (1962) Rapid lethal effect in rats of a third component found upon fractionating the toxin of Bacillus anthracis. J. Bacteriol. 83: 1274-1280
16. Fish D. C. and Lincoln R. E. (1968) In vivo-produced anthrax toxin. J. Bacteriol. 95: 919-924
17. Lincoln R. E. and Fish D. C. (1970) Anthrax toxin. In: Microbial Toxins, vol. 3, pp. 361-414, Montie T. C., Kadis S. and Ajl S. J. (eds), Academic Press, New York
18. Friedlander A. M. (1986) Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J. Biol. Chem. 261: 7123-7126
19. Mikesell P., Ivins B. E., Ristroph J. D. and Dreier T. M. (1983) Evidence for plasmid-mediated toxin production in Bacillus anthracis. Infect. Immun. 39: 371-376
20. Vodkin M. H. and Leppla S. H. (1983) Cloning of the protective antigen gene of Bacillus anthracis. Cell 34: 693-697
21. Welkos S. L., Lowe J. R., Eden-McCutchan F., Vodkin M., Leppla S. H. and Schmidt J. J. (1988) Sequence and analysis of the DNA encoding protective antigen of Bacillus anthracis. Gene 69: 287-300
22. Molnar D. M. and Altenbern R. A. (1963) Alterations in the biological activity of protective antigen of Bacillus anthracis toxin. Soc. Exp. Biol. Med. 114: 294-297
23. Gill D. M. Seven toxin peptides that cross cell membranes. (1978) In: Bacterial Toxins and Cell Membranes, pp. 291-332, Jeljaszewicz J. and Wadstrom T. (eds), Academic Press, New York
24. Leppla S. H. (1982) Anthrax toxin edema factor a bacterial adenylate cyclase that increases cyclic AMP concentrations of cukaryotic cells. Proc. Natl. Acad. Sci. USA 79: 3162-3166
25. Molloy S. S., Bresnahan P. A., Leppla S. H., Klimpel K. R. and Thomas G. (1992) Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J. Biol. Chem. 267: 16396-16402
26. Klimpel K. R., Molloy S. S., Thomas G. and Leppla S. H. (1992) Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin. Proc. Natl. Acad. Sci. USA 89: 10277-10281
27. Singh Y., Chaudhary V. K. and Leppla S. H. (1989) A deleted variant of Bacillus anthracis protective antigen is non-toxic and blocks anthrax toxin action in vivo. J. Biol. Chem. 264: 19103-19107
28. Singh Y., Klimpel K. R., Quinn C. P., Chaudhary V. K. and Leppla S. H. (1991) The carboxyl-terminal end of protective antigen is required for receptor binding and anthrax toxin activity. J. Biol. Chem. 266: 15493-15497
29. Novak J. M., Stein M.-P., Little S. F., Leppla S. H. and Friedlander A. M. (1992) Functional characterization of protease-treated Bacillus anthracis protective antigen. J. Biol. Chem. 267: 17186-17193
30. Blaustein R. O., Koehler T. M., Collier R. J. and Finkelstein A. (1989) Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers. Proc. Natl. Acad. Sci. USA. 86: 2209-2213
31. Leppla S. H. (1991) The anthrax toxin complex. In: Sourcebook of Bacterial Protein Toxins, pp. 277-302, Freer A. A. (ed.). Academic Press, London
32. Milne J. C., Furlong D., Hanna P. C., Wall J. S. and Collier R. J. (1994) Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J. Biol. Chem. 269: 20607-20612
33. Petosa C., Collier R. J., Klimpel K. R., Leppla S. H. and Liddington R. C. (1997) Crystal structure of the anthrax toxin protective antigen. Nature 385: 833-838
34. Gordon V. M., Leppla S. H. and Hewlett E. L. (1988) Inhibitors of receptor-mediated endocytosis block the entry Bacillus anthracis adenylate cyclase toxin but not that of Bordetella pertussis adenylate cyclase toxin. Infect. Immun. 56: 1066-1069
35. Mock M., Labruyere E., Glaser P., Danchin A. and Ullmann A. (1988) Cloning and expression of the calmodulin-sensitive Bacillus anthracis adenylate cyclase in Escherichia coli. Gene 64: 277-284
36. Tippetts M. T. and Robertson D. L. (1988) Molecular cloning and expression of the Bacillus anthracis edema factor toxin gene: a calmodulin-dependent adenylate cyclase. J. Bacteriol. 170: 2263-2266
37. Robertson D. L., Tippetts M. T. and Leppla S. H. (1988) Nucleotide sequence of the Bacillus anthracis edema factor gene (cya): a calmodulin-dependent adenylate cyclase. Gene 73: 363-371
38. Arora N. and Leppla S. H. (1994) Fusions of anthrax toxin lethal factor with shiga toxin and diphtheria toxin enzymatic domains are toxic to mammalian cells. Infect. Immun. 62: 4955-4961
39. Craig J. P. (1965) A permeability factor (toxin) found in cholera stools and culture filtrates and its neutralization by convalescent cholera scra. Nature 207: 614-616
40. Johnson G. S., Friedman R. M. and Pastan T. (1971) Restoration of several morphological characteristics of normal fibroblasts in sarcoma cells treated with adenosine-3′:5′cyclic monophosphate and its derivatives. Proc. Natl. Acad. Sci. USA 68: 425-429
41. Leppla S. H. (1984) Bacillus anthracis calmodulin-dependent adenylate cyclase: chemical and enzymatic properties and interactions with cucaryotic cells. In: Advances in Cyclic Nucleotide and Protein Phosphorylation Research, vol. 17, pp. 189-198, Greengard P. (ed.), Raven, New York
42. Labruyere E., Mock M., Ladant D., Michelson S., Gilles A.-M., Laoide B. et al. (1990) Characterization of ATP and calmodulin-binding properties of a truncated form of Bacillus anthracis adenylate cyclase. Biochemistry 29: 4922-4928
43. Escuyer V., Duflot E., Sezer O., Danchin A. and Mock M. (1988) Structural homology between virulence-associated bacterial adenylate cyclases. Gene 71: 293-298
44. Betsou F., Sismeiro O., Danchin A. and Guiso N. (1995) Cloning and sequence of the Bordetella bronchiseptica adenylate cyclase-hemolysin-encoding gene: comparison with the Bordetella pertussis gene. Gene 162: 165-166
45. Robertson D. L. and Leppla S. H. (1986) Molecular cloning and expression in Escherichia coli of the lethal factor gene of Bacillus anthracis. Gene 44: 71-78
46. Bragg T. S. and Robertson D. L. (1989) Nucleotide sequence and analysis of the lethal factor gene (lef) from Bacillus anthracis. Gene 81: 45-54
47. Leppla S. H. (1995) Anthrax Toxins. In: Handbook of Natural Toxins: Bacterial Toxins and Virulence Factors in Disease, vol. 8, pp. 543-572, Moss J. Iglewski B., Vaughan M. and Tu A. T. (eds.), Dekker, New York
48. Singh Y., Leppla S. H., Bhatnagar R. and Friedlander A. M. (1989) Internalization and processing of Bacillus anthracis lethal toxin by toxin-sensitive and -resistant cells. J. Biol. Chem. 264: 11099-11102
49. Swain P. K., Sarkar N. K., Sharma M., Goel S., Singh R. P. and Singh Y. (1997) Cytotoxicity of anthrax lethal factor microinjected into macrophage cells through sendai virus envelopes. Indian J. Biochem. Biophys. 34: 186-191
50. Duesbery N. S., Webb C. P., Leppla S. H., Gordon V. M., Klimpel K. R. and Copeland T. D. (1998) Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science 280: 734-737
51. Friedlander A. M., Bhatnagar R., Leppla S. H., Johnson L. and Singh Y. (1993) Characterization of macrophage sensitivity and resistance to anthrax lethal toxin. Infect. Immun. 61: 245-252
52. Quinn C. P., Singh Y., Klimpel K. R. and Leppla S. H. (1991) Functional mapping of anthrax toxin lethal factor by in-frame insertion mutagenesis. J. Biol. Chem. 266: 20124-20130
53. Klimpel K. R., Arora N. and Leppla S. H. (1994) Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol. Microbiol. 13: 1093-1100
54. Hanna P. (1998) Anthrax pathogenesis and host response. Curr. Top. Microbiol. Immunol. 225: 13-35
55. Kochi S. K., Schiavo G., Mock M. and Montecucco C. (1994) Zinc content of the Bacillus anthracis lethal factor. FEMS Microbiol. Lett. 124: 343-348
56. Vitale G., Pellizzari R., Recchi C., Napolitani G., Mock M. and Montecucco C. (1998) Anthrax lethal factor cleaves the n-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 248: 706-711
57. Lewis T. S., Shapiro P. S., and Ahn N. G. (1998) Signal transduction through MAP kinase cascades. In: Advances in Cancer Research, vol. 74, pp. 49-139, Vande Woude G. F. and Klein G. (eds), Academic Press, San Diego
58. Masui Y. and Markert C. L. (1971) Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes. J. Exp. Zool. 177: 129-145
59. Ishikawa K., Hanaoka Y., Kondo Y. and Imai K. (1977) Primary action of steroid hormone at the surface of amphibian oocyte in the induction of GVBD. Mol. Cell. Endocrinol. 9: 91-100
60. Godeau J. F., Schorderet-Slatkine S., Hubert P. and Baulieu E.-E. (1978) Induction of maturation in Xenopus laeris oocytes by a steroid linked to a polymer. Proc. Natl. Acad. Sci. USA 75: 2353-2357
61. Gebauer F., Xu W., Cooper G. M. and Richter J. D. (1994) Translational control by cytoplasmic polyadenylation of c-mos mRNA is necessary for oocyte maturation in the mouse. EMBO J. 13: 5712-5720
62. Sheets M. D., Wu M. and Wickens M. (1994) Polyadenylation of c-mos mRNA as a control point in Xenopus meiotic maturation. Nature 374: 511-516
63. Barkoff A., Ballantyne S. and Wickens M. (1998) Meiotic maturation in Xenopus requires polyadenylation of multiple mRNAs. EMBO J. 17: 3168-3175
64. Sagata N., Oskarsson M., Copeland T., Brumbaugh J. and Vande Woude G. F. (1988) Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes. Nature 335: 519-525
65. Posada J., Yew N., Ahn N. G., Vande Woude G. F. and Cooper J. A. (1993) Mos stimulates MAP kinase in Xenopus oocytes and activates a MAP kinase kinase in vitro. Mol. Cell. Biol. 13: 2546-2553
66. Nebreda A. R., Hill C., Gomez N., Cohen P. and Hunt T. (1993) The protein kinase mos activates MAP kinase kinase in vitro and stimulates the MAP kinase pathway in mammalian somatic cells in vivo. FEBS Lett. 333: 183-187
67. Shibuya E. K. and Ruderman J. V. (1993) Mos induces the in vitro activation of mitogen-activated protein kinases in lysates of frog oocytes and mammalian somatic cells. Mol. Biol. Cell 4: 781-790
68. Mansour S. J., Resing K. A., Candi J. M., Hermann A. S., Gloor J. W., Herskind K. R. et al. (1994) Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis. J. Biochem. (Tokyo) 116: 304-314
69. Chen M. and Cooper J. A. (1995) Ser-3 is important for regulating Mos interaction with and stimulation of mitogen-activated protein kinase kinase. Mol. Cell. Biol. 15: 4727-4734
70. cdc2 inhibitory kinase Mytl. EMBO J. 17: 5037-5047
71. Mueller P. R., Coleman T. R., Kumagai A. and Dunphy W. G. (1995) Mytl: a membrane-associated inhibitory kinase that phosphorylates cdc2 on both threonine-14 and tyrosine-15. Science 270: 86-90
72. Kahan C., Seuwen K., Meloche S. and Pouyssegur J. (1992) Coordinate, biphasic activation of p44 mitogen-activated protein kinase and S6 kinase by growth factors in hamster fibroblasts: evidence for thrombin-induced signals different from phosphoinositide turnover and adenylylcyclase inhibition. J. Biol. Chem. 267: 13369-13375
73. Meloche S., Seuwen K., Pages G. and Pouyssegur J. (1992) Biphasic and synergistic activation of p44mapk (ERK1) by growth factors: correlation between late phase activation and mitogenicity. Mol. Endocrinol. 6: 845-854
74. Pages G., Lenormand P., L'Allemain G., Chambard J. C., Meloche S. and Pouyssegur J. (1993) Mitogen-activated protein kinases p42mapk and p44mapk are required for fibroblast proliferation. Proc. Natl. Acad. Sci. USA 90: 8319-8323
75. cdc2 and a microtubule-associated protein kinase homolog in Xenopus oocytes and eggs. Mol. Cell. Biol. 11: 1965-1971
76. Gotoh Y., Moriyama K., Matsuda S., Okumura E., Kishimoto T., Kawasaki H. et al. (1991) Xenopus M phase MAP kinase: isolation of its cDNA and activation by MPF. EMBO J. 10: 2661-2668
77. cdc2 and p42 during meiotic maturation of Xenopus oocyte. Development 111: 813-820
78. Posada J., Sanghera J., Pelech S., Aebersold R. and Cooper J. A. (1991) Tyrosine phosphorylalion and activation of homologous protein kinases during oocyte maturation and mitogenic activation of fibroblasts. Mol. Cell. Biol. 11: 2517-2528
79. Haccard O., Sarcevic B., Lewellyn A., Hartley R., Roy L., Izumi T. et al. (1993) Induction of metaphase arrest in cleaving Xenopus embryos by MAP kinase. Science 262: 1262-1265
80. Colledge W. H., Carlton M. B., Udy G. B. and Evans M. J. (1994) Disruption of c-mos causes parthenogenetic development of unfertilized moose eggs. Nature 370: 65-68
81. Hashimoto N., Watanabe N., Furuta Y., Tamemoto H., Sagata N., Yokoyama M. et al. (1994) Parthenogenetic activation of oocytes in c-mos-deficient mice. Nature 370: 68-71
82. Vande Woude G. F. (1994) On the loss of Mos. Nature 370: 20-21
83. Guadagno T. M. and Ferrell J. E. Jr (1998) Requirement for MAPK activation for normal mitotic progression in Xenopus egg extracts. Science 282: 1312-1315
84. Verlhac M.-H., Kubiak J. Z., Weber M., Geraud G., Colledge W. H., Evans M. J. et al. (1996) Mos is required for MAP kinase activation and is involved in microtubule organization during meiotic maturation in the mouse. Development 122: 815-822
85. Choi T., Rulong S., Resau J., Fukasawa K., Matten W., Kuriyama R. et al. (1996) Mos/MAPK can induce early meiotic phenotypes in the absence of MPF: a novel system for analyzing spindle formation during meiosis I. Proc. Natl. Acad. Sci. USA 93: 4730-4735
86. Choi T., Fukasawa K., Zhou R., Tessarollo L., Borror K., Resau J. et al. (1996) The Mos/MAPK pathway regulates the size and degradation of the first polar body in maturing mouse oocytes. Proc. Natl. Acad. Sci. USA 93: 7032-7035
87. Duesbery N. S., Choi T., Brown K. D., Wood K. W., Resau J., Fukasawa K. et al. (1997) CENP-E is an essential kinetochore motor in maturing oocytes and is masked during Mos-dependent, cell cycle arrest at metaphase II. Proc. Natl. Acad. Sci. USA 94: 9165-9170
88. Shapiro P. S., Vaisberg E., Hunt A. J., Tolwinski N. S., Whalen A. M., McIntosh J. R. et al. (1998) Activation of the MKK/ERK pathway during somatic cell mitosis: direct interactions of active ERK with kinetochores and regulation of the mitotic 3F3/2 phosphoantigen. J. Cell Biol. 142: 1533-1545
89. Zecevic M., Catling A. D., Eblen S. T., Renzi L., Hittle J. C., Yen T. J. et al. (1998) Active MAP kinase in mitosis: localization at kinetochores and association with the motor protein CENP-E. J. Cell Biol. 142: 1547-1558
90. Mansour S. J., Matten W. T., Hermann A. S., Candia J. M., Rong S., Fukasawa K. et al. (1994) Transformation of mammalian cells by constitutively active MAP kinase kinase. Science 265: 966-970
91. Mansour S., Candia J. M., Gloor K. K. and Ahn N. G. (1996) Constitutively active mitogen-activated protein kinase kinase 1 (MAPKK1) and MAPKK2 mediate similar transcriptional and morphological responses. Cell Growth Differ. 7: 243-250
92. Webb C. P., Van Aelst L., Wigler M. H. and Vande Woude G. F. (1998) Signaling pathways in ras-mediated tumorigenicity and metastasis. Proc. Natl. Acad. Sci. USA 95: 8773-8778
93. Elion E. A. (1998) Routing MAP kinase cascades. Science 281: 1625-1626
94. Schaeffer H. J., Catling A. D., Eblen S. T., Collier L. S., Krauss A. and Weber M. J. (1998) MPI: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade. Science 281: 1668-1671
95. Whitmarsh A. J., Cavanagh J., Tournier C., Yasuda J. and Davis R. J. (1998) A mammalian scaffold complex that selectively mediates MAP kinase activation. Science 281: 1671-1674
96. Hammond S. F. and Hanna P. C. (1998) Lethal factor active-site mutations affect catalytic activity in vitro. Infect. Immun. 66: 2374-2378
97. Raingeaud J., Whitmarsh A. J., Barren T., Derijard B. and Davis R. J. (1996) MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. Mol. Cell. Biol. 16: 1247-1255
98. Derijard B., Raingeaud J., Barrett T., Wu I. H., Han J., Ulevitch R. J. et al. (1995) Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. Science 267: 682-685
99. Han J., Lee J. D., Bibbs L. and Ulevitch R. J. (1994) A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265: 808-811
100. Lee J. C., Laydon J. T., McDonnell P. C., Gallagher T. F., Kumar S., Green D. et al. (1994) A protein kinase involved in the regulation of inflammatory cytokine biosynthesis. Nature 372: 739-746
101. Rouse J., Cohen P., Trigon S., Morange M., Alonso-Llamazares A., Zamanillo D, el al. (1994) A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase 2 and phosphorylation of the small heat shock proteins. Cell 78: 1027-1037
102. Freshney N. W., Rawlinson L., Guesdon F., Jones E., Cowley S., Hsuan J. et al. (1994) Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27. Cell 78: 1039-1049
103. Takenaka K., Moriguchi T. and Nishida E. (1998) Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest. Science 280: 599-602
104. Zhou G., Bao Z. Q. and Dixon J. E. (1995) Components of a new human protein kinase signal transduction. J. Biol. Chem. 270: 12665-12669
105. Kato Y., Kravchenko V. V., Tapping R. I., Han J., Ulevitch R. J. and Lee J. D. (1997) BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C. EMBO J. 16: 7054-7066
106. Kato Y., Tapping R. I., Huang S., Watson M. H., Ulevitch R. J. and Lee J. D. (1998) Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor. Nature 395: 713-716
107. Cataldi A., Labruyere E. and Mock M. (1990) Construction and characterization of a protective antigen-deficient Bacillus anthracis strain. Mol. Microbiol. 4: 1111-1117
108. Pezard C., Berche P. and Mock M. (1991) Contribution of individual toxin components to virulence of Bacillus anthracis. Infect. Immun. 59: 3472-3477
109. Pezard C., Duflot E. and Mock M. (1993) Construction of Bacillus anthracis mutant strains producing a single toxin component. J. Gen. Microbiol. 139: 2459-2463
110. O'Brien J., Friedlander A., Dreier T., Ezzell J. and Leppla S. (1985) Effects of anthrax toxin components on human neutrophils. Infect. Immun. 47: 306-310
111. Okuda K., Takahashi T., Tadokoro I. and Noguchi Y. (1976) Effects of cytochalasin B and dibutyryl cyclic AMP on intraleukocytic bactericidal activity. Jpn. J. Exp. Med. 46: 101-110
112. Rossi A. G., McCutcheon J. C., Roy N., Chilvers E. R., Haslett C. and Dransfield T. (1998) Regulation of macrophage phagocytosis of apoptotic cells by cAMP. J. Immunol. 160: 3562-3568
113. Smith H. and Stoner H. B. (1967) Anthrax toxic complex. Fed. Proc. 26: 1554-1557
114. Morrill G. A., Schatz F., Kostellow A. B. and Poupko J. M. (1977) Changes in cyclic AMP levels in amphibian ovarian follicle following progesterone induction of meiotic maturation. Differentiation 8: 97-104
115. Sneaker M. G. and Butcher F. R. (1977) Cyclic nucleotide fluctuations during steroid induced meiotic maturation of frog oocytes. Nature 267: 848-849
116. Maller J. L., Butcher F. R. and Krebs E. G. (1979) Early effect of progesterone on levels of cyclic adenosine 3′:5′-monophosphate in Xenopus oocytes. J. Biol. Chem. 254: 579-582
117. Cicirelli M. F. and Smith L. D. (1985) Cyclic AMP levels during the maturation of Xenapus oocytes. Dev. Biol. 108: 254-258
118. Daar I., Yew N. and Vande Woude G. F. (1993) Inhibition of mos-induced oocyte maturation by protein kinase A. J. Cell. Biol. 120: 1197-1202
119. Matten W., Daar I. and Vande Woude G. F. (1994) Protein kinase A acts at multiple points to inhibit Xenopus oocyte maturation. Mol. Cell. Biol. 14: 4419-4426
120. VanRenterghem B., Browning M. D. and Maller J. L. (1994) Regulation or mitogen-activated protein kinase activation by protein kinases A and C in a cell-free system. J. Biol. Chem. 269: 24666-24672
121. Matten W. T., Copeland T. D., Ahn N. G. and Vande Woude G. F. (1996) Positive feedback between MAP kinase and Mos during Xenopus oocyte maturation. Dev. Biol. 179: 485-492
122. Miller M. J., Rioux L., Prendergast G. V., Cannon S., White M. A. and Meinkoth J. L. (1998) Differential effects of protein kinase A on Ras effector pathways. Mol. Cell. Biol. 18: 3718-3726
123. Dousa T. P. (1998) Signaling role of PDE isozymes in pathobiology of glomerular mesangial cells: studies in vitro and in vivo. Cell. Biochem. Biophys. 29: 19-34
124. Moroo I., Tatsuno I., Uchida D., Tanaka T., Saito J., Saito Y. et al. (1998) Pituitary adenylate cyclase activating polypeptide (PACAP) stimulates mitogen-activated protein kinase (MAPK) in cultured rat astrocytes. Brain Res. 795: 191-196
125. Webster C. R. and Anwer M. S. (1998) Cyclic adenosine monophosphate-mediated protection against bile acid-induced apoptosis in cultured rat hepatocytes. Hepatology 27: 1324-1331
126. D'Angelo G., Lee H. and Weiner R. I. (1997) cAMP-dependent protein kinase inhibits the mitogenic action of vascular endothelial growth factor and fibroblast growth factor in capillary endothelial cells by blocking Raf activation. J. Cell Biochem. 67: 353-366
127. Welkos S. L., Keener T. J. and Gibbs P. H. (1986) Differences in susceptibility of inbred mice to Bacillus anthracis. Infect. Immun. 51: 795-800
128. Hanna P. C., Acosta D. and Collier R. J. (1993) On the role of macrophages in anthrax. Proc. Natl. Acad. Sci. USA 90: 10198-10201
129. Hanna P. C., Kruskal B. A., Alien R., Ezekowitz B., Bloom B. R. and Collier R. J. (1994) Role of macrophage oxidative burst in the action of anthrax lethal toxin. Mol. Med. I: 7-18
130. Ding A., Sanchez E. and Nathan C. F. (1993) Taxol shares the ability of bacterial lipopolysaccharide lo induce tyrosine phosphorylation of microtubule-associated protein kinase. J. Immunol. 151: 5596-5602
131. Liu M. K., Herrera-Velit P., Brownsey R. W. and Reiner N. E. (1994) CD14-dependent activation of protein kinase C and mitogen-activated protein kinases (p42 and p44) in human monocytes treated with bacterial lipopolysaccharide. J. Immunol. 153: 2642-2652
132. Geppert T. D., Whitehurst C. E., Thompson P. and Beutler B. (1994) Lipopolysaccharide signals activation of tumor necrosis factor biosynthesis through the ras/raf-1/MEK/ MAPK pathway. Mol. Med. 1: 93-103
133. Buscher D., Hipskind R. A., Krautwald S., Reimann T. and Baccarini M. (1995) Ras-dependent and -independent pathways target the mitogen-activated protein kinase network in macrophages. Mol. Cell. Biol. 15: 466-475
134. Kugler S., Schuller S. and Goebel W. (1997) Involvement of MAP-kinases and -phosphatases in uptake and intracellular replication of Listeria monocytogenes in J774 macrophage cells. FEMS Microbiol. Lett. 157: 131-136