Monoclonal antibodies for Bacillus anthracis spore detection and functional analyses of spore germination and outgrowth

Journal of Immunology

Volumn 176, Issue 10, 2006, Pages 6076-6084

  Swiecki, Melissa K ^a,b   Lisanby, Mark W ^a,b   Shu, Fengyu ^a,b   Turnbough Jr , Charles L ^b   Kearney, John F ^a,b,c  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b University of Alabama at Birmingham   (United States)

^c The University of Alabama at Birmingham   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTHRAX; ARTICLE; BACILLUS ANTHRACIS; BACTERIAL SPORE; BACTERIAL STRAIN; BACTERIUM IDENTIFICATION; CONTROLLED STUDY; FEMALE; FLUORESCENCE ACTIVATED CELL SORTING; MOUSE; NONHUMAN; PRIORITY JOURNAL; SPORE GERMINATION;

EID: 33646466300     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.176.10.6076     Document Type: Article

References (44)

1. Priest, F. G. 1993. Systemics and ecology of Bacillus. In Bacillus subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Biology. A. L. Sonenshein, J. A. Hoch, and R. Losick, eds. American Society of Microbiology, Washington, DC, pp. 3-16.
2. Errington, J. 1993. Bacillus subtilis sporulation: regulation of gene expression and control of morphogenesis. Microbiol. Rev. 57: 1-33.
3. Foster, S. J., and D. L. Popham. 2002. Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers, and capsules. In Bacillus subtilis and Its Closest Relatives: From Genes to Cells. A. L. Sonenshein, J. A. Hoch, and R. Losick, eds. Am. Soc. Microbiol., Washington, DC, pp. 21-41.
4. Nicholson, W. L., and P. Setlow. 1990. Sporulation, germination and outgrowth. In Molecular Biological Methods for Bacillus. C. R. Harwood and S. M. Cutting, eds. John Wiley & Sons, Chichester, U.K., pp. 391-450.
5. Nicholson, W. L., N. Munakata, G. Horneck, H. J. Melosh, and P. Setlow. 2000. Resistance of Bacillus endospores to extreme terrestrial and extraterrestrial environments. Microbiol. Mol. Biol. Rev. 64: 548-572.
6. Keim, P., L. B. Price, A. M. Klevytska, K. L. Smith, J. M. Schupp, R. Okinaka, P. J. Jackson, and M. E. Hugh-Jones. 2000. Multiple-locus variable-number tandem repeat analysis reveals genetic relationships within Bacillus anthracis. J. Bacteriol. 182: 2928-2936.
7. Radnedge, L., P. G. Agron, K. K. Hill, P. J. Jackson, L. O. Ticknor, P. Keim, and G. L. Andersen. 2003. Genome differences that distinguish Bacillus anthracis from Bacillus cereus and Bacillus thuringiensis. Appl. Environ. Microbiol. 69: 2755-2764.
8. Hill, K. K., L. O. Ticknor, R. T. Okinaka, M. Asay, H. Blair, K. A. Bliss, M. Laker, P. E. Pardington, A. P. Richardson, M. Tonks, et al. 2004. Fluorescent amplified fragment length polymorphism analysis of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis isolates. Appl. Environ. Microbiol. 70: 1068-1080.
9. Steichen, C., P. Chen, J. F. Kearney, and C. L. Turnbough, Jr. 2003. Identification of the immunodominant protein and other proteins of the Bacillus anthracis exosporium. J. Bacteriol. 185: 1903-1910.
10. Steichen, C. T., J. F. Kearney, and C. L. Turnbough, Jr. 2005. Characterization of the exosporium basal layer protein BxpB of Bacillus anthracis. J. Bacteriol. 187: 5868-5876.
11. Daubenspeck, J. M., H. Zeng, P. Chen, S. Dong, C. T. Steichen, N. R. Krishna, D. G. Pritchard, and C. L. Turnbough, Jr. 2004. Novel oligosaccharide side chains of the collagen-like region of BclA, the major glycoprotein of the Bacillus anthracis exosporium. J. Biol. Chem. 279: 30945-30953.
12. Kearney, J. F., A. Radbruch, B. Liesegang, and K. Rajewsky. 1979. A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. J. Immunol. 123: 1548-1550.
13. + mice. Int. Immunol. 7: 807-819.
14. Phillips, A. P., and K. L. Martin. 1988. Investigation of spore surface antigens in the genus Bacillus by the use of polyclonal antibodies in immunofluorescence tests. J. Appl. Bacteriol. 64: 47-55.
15. Henderson, D. W., S. Peacock, and F. C. Belton. 1956. Observations on the prophylaxis of experimental pulmonary anthrax in the monkey. J. Hyg. 54: 28-36.
16. Lai, E. M., N. D. Phadke, M. T. Kachman, R. Giorno, S. Vazquez, J. A. Vazquez, J. R. Maddock, and A. Driks. 2003. Proteomic analysis of the spore coats of Bacillus subtilis and Bacillus anthracis. J. Bacteriol. 185: 1443-1454.
17. Liu, H., N. H. Bergman, B. Thomason, S. Shallom, A. Hazen, J. Crossno, D. A. Rasko, J. Ravel, T. D. Read, S. N. Peterson, et al. 2004. Formation and composition of the Bacillus anthracis endospore. J. Bacteriol. 186: 164-178.
18. Williams, D. D., and C. L. Turnbough, Jr. 2004. Surface layer protein EA1 is not a component of Bacillus anthracis spores but is a persistent contaminant in spore preparations. J. Bacteriol. 186: 566-569.
19. Boydston, J. A., P. Chen, C. T. Steichen, and C. L. Turnbough, Jr. 2005. Orientation within the exosporium and structural stability of the collagen-like glycoprotein BclA of Bacillus anthracis. J. Bacteriol. 187: 5310-5317.
20. Martin, F., and J. F. Kearney. 2002. Marginal-zone B cells. Nat. Rev. Immunol. 2: 323-335.
21. Bachmann, M. F., and R. M. Zinkernagel. 1997. Neutralizing antiviral B cell responses. Annu. Rev. Immunol. 15: 235-270.
22. Sylvestre, P., E. Couture-Tosi, and M. Mock. 2002. A collagen-like surface glycoprotein is a structural component of the Bacillus anthracis exosporium. Mol. Microbiol. 45: 169-178.
23. Ezzell, J. W., Jr., T. G. Abshire, S. F. Little, B. C. Lidgerding, and C. Brown. 1990. Identification of Bacillus anthracis by using monoclonal antibody to cell wall galactose-N-acetylglucosamine polysaccharide. J. Clin. Microbiol. 28: 223-231.
24. Phillips, A. P., K. L. Martin, and A. J. Capey. 1987. Direct and indirect immunofluorescence analysis of bacterial populations by flow cytometry. J. Immunol. Methods 101: 219-228.
25. Phillips, A. P., A. M. Campbell, and R. Quinn. 1988. Monoclonal antibodies against spore antigens of Bacillus anthracis. FEMS Microbiol. Immunol. 1: 169-178.
26. Slack, J., G. P. Der-Balian, M. Nahm, and J. M. Davie. 1980. Subclass restriction of murine antibodies. II. The IgG plaque-forming cell response to thymus-independent type 1 and type 2 antigens in normal mice and mice expressing an X-linked immunodeficiency. J. Exp. Med. 151: 853-862.
27. Mongini, P. K., K. E. Stein, and W. E. Paul. 1981. T cell regulation of IgG subclass antibody production in response to T-independent antigens. J. Exp. Med. 153: 1-12.
28. Oliver, A. M., F. Martin, G. L. Gartland, R. H. Carter, and J. F. Kearney. 1997. Marginal zone B cells exhibit unique activation, proliferative and immunoglobulin secretory responses. Eur. J. Immunol. 27: 2366-2374.
29. Kearney, J. F., and A. R. Lawton. 1975. B lymphocyte differentiation induced by lipopolysaccharide. I. Generation of cells synthesizing four major immunoglobulin classes. J. Immunol. 115: 671-676.
30. Schofield, L. 1990. The circumsporozoite protein of Plasmodium: a mechanism of immune evasion by the malaria parasite? Bull. W.H.O. 68(Suppl): 66-73.
31. Bull, P. C., M. Kortok, O. Kai, F. Ndungu, A. Ross, B. S. Lowe, C. I. Newbold, and K. Marsh. 2000. Plasmodium falciparum-infected erythrocytes: agglutination by diverse Kenyan plasma is associated with severe disease and young host age. J. Infect. Dis. 182: 252-259.
32. Bull, P. C., B. S. Lowe, N. Kaleli, F. Njuga, M. Kortok, A. Ross, F. Ndungu, R. W. Snow, and K. Marsh. 2002. Plasmodium falciparum infections are associated with agglutinating antibodies to parasite-infected erythrocyte surface antigens among healthy Kenyan children. J. Infect. Dis. 185: 1688-1691.
33. Fouet, A., J.-C. Sirard, and M. Mock. 1996. Virulence gene determinants. Salisbury Med. Bull. 87(Suppl): 84-86.
34. Ross, J. M. 1957. The pathogenesis of anthrax following administration of spores by the respiratory route. J. Pathol. Bacteriol. 73: 485-494.
35. Shafa, F., B. J. Moberly, and P. Gerhardt. 1966. Cytological features of anthrax spores phagocytized in vitro by rabbit alveolar macrophages. J. Infect. Dis. 116: 401-413.
36. Guidi-Rontani, C., M. Weber-Levy, E. Labruyere, and M. Mock. 1999. Germination of Bacillus anthracis spores within alveolar macrophages. Mol. Microbiol. 31: 9-17.
37. Hanna, P. C., and J, A. Ireland. 1999. Understanding Bacillus anthracis pathogenesis. Trends Microbiol. 7: 180-182.
38. Ticknor, L. O., A. B. Kolsto, K. K. Hill, P. Keim, M. T. Laker, M. Tonks, and P. J. Jackson. 2001. Fluorescent amplified fragment length polymorphism analysis of Norwegian Bacillus cereus and Bacillus thuringiensis soil isolates. Appl. Environ. Microbiol. 67: 4863-4873.
39. Hernandez, E., F. Ramisse, T. Cruel, R. le Vagueresse, and J. D. Cavallo. 1999. Bacillus thuringiensis serotype H34 isolated from human and insecticidal strains serotypes 3a3b and H14 can lead to death of immunocompetent mice after pulmonary infection. FEMS Immunol. Med. Microbiol. 24: 43-47.
40. Welkos, S. L., C. K. Cote, K. M. Rea, and P. H. Gibbs. 2004. A microtiter fluorometric assay to detect the germination of Bacillus anthracis spores and the germination inhibitory effects of antibodies. J. Microbiol. Methods 56: 253-265.
41. Cohen, S., I. Mendelson, Z. Altboum, D. Kobiler, E. Elhanany, T. Bino, M. Leitner, I. Inbar, H. Rosenberg, Y. Gozes, et al. 2000. Attenuated nontoxinogenic and nonencapsulated recombinant Bacillus anthracis spore vaccines protect against anthrax. Infect. Immun. 68: 4549-4558.
42. Brossier, F., M. Levy, and M. Mock. 2002. Anthrax spores make an essential contribution to vaccine efficacy. Infect. Immun. 70: 661-664.
43. Little, S. F., B. E. Ivins, P. F. Fellows, and A. M. Friedlander. 1997. Passive protection by polyclonal antibodies against Bacillus anthracis infection in guinea pigs. Infect. Immun. 65: 5171-5175.
44. Kobiler, D., Y. Gozes, H. Rosenberg, D. Marcus, S. Reuveny, and Z. Altboum. 2002. Efficiency of protection of guinea pigs against infection with Bacillus anthracis spores by passive immunization. Infect. Immun. 70: 544-560.