Bacillus anthracis protease InhA regulates BslA-mediated adhesion in human endothelial cells

Cellular Microbiology

Volumn 14, Issue 8, 2012, Pages 1219-1230

  Tonry, Jessica H ^a   Mcnichol, Beth A ^b,g   Ramarao, Nalini ^c   Chertow, Daniel S ^d   Kim, Kwang Sik ^e   Stibitz, Scott ^b   Schneewind, Olaf ^f   Kashanchi, Fatah ^a   Bailey, Charles L ^a   Popov, Serguei ^a   Chung, Myung Chul ^a  

^a GEORGE MASON UNIVERSITY   (United States)

^b CENTER FOR BIOLOGICS EVALUATION AND RESEARCH   (United States)

^c UMR1319 MICALIS   (France)

^d NATIONAL INSTITUTES OF HEALTH   (United States)

^e JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^f UNIVERSITY OF CHICAGO   (United States)

^g PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS ANTHRACIS S LAYER PROTEIN A; BACTERIAL ENZYME; BACTERIAL PROTEIN; IMMUNE INHIBITOR A; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BACILLUS ANTHRACIS; BACTERIAL STRAIN; CELL ADHESION; CELL INVASION; CONTROLLED STUDY; DOWN REGULATION; ENDOTHELIUM CELL; HUMAN; HUMAN CELL; HUMAN TISSUE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; WESTERN BLOTTING;

ADHESINS, BACTERIAL; ANIMALS; BACILLUS ANTHRACIS; BACTERIAL ADHESION; BICARBONATES; BRAIN; CULTURE MEDIA; ENDOTHELIAL CELLS; GENE EXPRESSION; GENE EXPRESSION REGULATION, BACTERIAL; GENE KNOCKOUT TECHNIQUES; HOST-PATHOGEN INTERACTIONS; HUMANS; MACROPHAGES; METALLOPROTEASES; MICE; MICROBIAL VIABILITY; MICROVESSELS; PHENANTHROLINES; PROTEASE INHIBITORS; PROTEOLYSIS; VIRULENCE FACTORS;

BACILLUS ANTHRACIS;

EID: 84864011333     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2012.01791.x     Document Type: Article

References (30)

1. Charlton, S., Baillie, A.J., and Moir, A. (1999) Characterization of exosporium of Bacillus cereus. J Appl Microbiol 87: 241-245.
2. Chung, M.C., Popova, T.G., Millis, B.A., Mukherjee, D.V., Zhou, W., Liotta, L.A., etal. (2006) Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors. J Biol Chem 281: 31408-31418.
3. Collier, R.J., and Young, J.A. (2003) Anthrax toxin. Annu Rev Cell Dev Biol 19: 45-70.
4. Cybulski, R.J., Jr, Sanz, P., Alem, F., Stibitz, S., Bull, R.L., and O'Brien, A.D. (2009) Four superoxide dismutases contribute to Bacillus anthracis virulence and provides spores with redundant protection from oxidative stress. Infect Immun 77: 274-285.
5. Dixon, T.C., Fadl, A.A., Koehler, T.M., Swanson, J.A., and Hanna, P.C. (2000) Early Bacillus anthracis-macrophage interactions: intracellular survival and escape. Cell Microbiol 2: 453-463.
6. Drysdale, M., Heninger, S., Hutt, J., Chen, Y., Lyons, C.R., and Koehler, T.M. (2005) Capsule synthesis by Bacillus anthracis is required for dissemination in murine inhalation anthrax. EMBO J 24: 221-227.
7. Ebrahimi, C.M., Kern, J.W., Sheen, T.R., Ebrahimi-Fardooee, M.A., van Sorge, N.M., Schneewind, O., etal. (2009) Penetration of the blood-brain barrier by Bacillus anthracis requires the pXO1-encoded BslA protein. J Bacteriol 191: 7165-7173.
8. Grandvalet, C., Gominet, M., and Lereclus, D. (2001) Identification of genes involved in the activation of the Bacillus thuringiensis inhA metalloprotease gene at the onset of sporulation. Microbiology 147: 1805-1813.
9. Green, B.D., Battisti, L., Koehler, T.M., Thorne, C.B., and Ivins, B.E. (1985) Demonstration of a capsule plasmid in Bacillus anthracis. Infect Immun 49: 291-297.
10. Grinberg, L.M., Abramova, F.A., Yampolskaya, O.V., Walker, D.H., and Smith, J.H. (2001) Quantitative pathology of inhalational anthrax I: quantitative microscopic findings. Mod Pathol 5: 482-495.
11. Guidi-Rontani, C., Levy, M., Ohayon, H., and Mock, M. (2001) Fate of germinated Bacillus anthracis spores in primary murine macrophages. Mol Microbiol 4: 931-938.
12. Guillemet, E., Cadot, C., Tran, S.L., Guinebretière, M.H., Lereclus, D., and Ramarao, N. (2010) The InhA metalloproteases of Bacillus cereus contribute concomitantly to virulence. J Bacteriol 1: 286-294.
13. Hu, H., Sa, Q., Koehler, T.M., Aronson, A.I., and Zhou, D. (2006) Inactivation of Bacillus anthracis spores in murine primary macrophages. Cell Microbiol 10: 1634-1642.
14. Janes, B.K., and Stibitz, S. (2006) Routine markerless gene replacement in Bacillus anthracis. Infect Immun 74: 1949-1953.
15. Kang, T.J., Fenton, M.J., Weiner, M.A., Hibbs, S., Basu, S., Baillie, L., and Cross, A.S. (2005) Murine macrophages kill the vegetative for of Bacillus anthracis. Infect Immun 11: 7495-7501.
16. Kastrup, C.J., Boedicker, J.Q., Pomerantsev, A.P., Moayeri, M., Bian, Y., Pompano, R.R., etal. (2008) Spatial localization of bacteria controls coagulation of human blood by 'quorum acting'. Nat Chem Biol 4: 742-750.
17. Kern, J., and Schneewind, O. (2010) BslA, the S-layer of B.anthracis, is a virulence factor for anthrax pathogenesis. Mol Microbiol 75: 324-332.
18. Kern, J.W., and Schneewind, O. (2008) BslA, a pXO1-encoded adhesin of Bacillus anthracis. Mol Microbiol 68: 504-515.
19. Koch, R. (1876) Die Atiologie der Milzbrand-Krankheit, begrundet auf die Entwicklungsgeschichte des Bacillus anthracis. Beitrage zur Biologie der Pflanzen 2: 277-310.
20. Leppla, S.H. (1999) The anthrax toxin complex. In Sourcebook of Bacterial Protein Toxins. Alouf, J., and Freer, J.H. (eds). London, UK: Academic Press, pp. 277-302.
21. Lereclus, D., Arantes, O., Chaufaux, J., and Lecadet, M. (1989) Transformation and expression of a cloned-delta-endotoxin gene in Bacillus thuringiensis. FEMS Microbiol Lett 51: 211-217.
22. Mesnage, S., Tosi-Couture, E., Gounon, P., Mock, M., and Fouet, A. (1998) The capsule and S-layer: two independent and yet compatible macromolecular structures in Bacillus anthracis. J Bacteriol 1: 52-58.
23. 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.
24. Mock, M., and Fouet, A. (2001) Anthrax. Annu Rev Microbiol 55: 647-671.
25. Mukherjee, D., Tonry, J.H., Kim, K.S., Ramarao, N., Popova, T.G., Bailey, C., etal. (2011) Bacillus anthracis protease InhA increases blood-brain barrier permeability and contributes to cerebral hemorrhages. PLoS ONE 6: e17921.
26. Ramarao, N., and Lereclus, D. (2005) The InhA1 metalloprotease allows spores of the B.cereus group to escape macrophages. Cell Microbiol 9: 1357-1364.
27. Russell, B.H., Vasan, R., Keene, D.R., and Xu, Y. (2007) Bacillus anthracis internalization by human fibroblasts and epithelial cells. Cell Microbiol 9: 1262-1274.
28. Ruthel, G., Ribot, W.J., Bavari, S., and Hoover, T. (2004) Time-lapse confocal imaging of development of Bacillus anthracis in macrophages. J Infect Dis 189: 1313-1316.
29. Thanassi, D.G. (2011) The long and the short of bacterial adhesion regulation. J Bacteriol 193: 327-328.
30. Welkos, S., Friedlander, A., Weeks, S., Little, S., and Mendelson, I. (2002) In-vitro characterization of the phagocytosis and fate of anthrax spores in macrophages and the effects of anti-PA antibody. J Med Microbiol 10: 821-831.