The dltABCD operon of Bacillus anthracis sterne is required for virulence and resistance to peptide, enzymatic, and cellular mediators of innate immunity

Journal of Bacteriology

Volumn 188, Issue 4, 2006, Pages 1301-1309

  Fisher, Nathan ^a   Shetron Rama, Lynne ^a   Herring Palmer, Amy ^a   Heffernan, Brian ^a   Bergman, Nicholas ^a   Hanna, Philip ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACITRACIN; CARBENICILLIN; COLISTIN; DEXTRO ALANINE; ENZYME; GRAMICIDIN D; MAGAININ 2; NISIN; PEPTIDE; POLYMYXIN B; VANCOMYCIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTHRAX; ARTICLE; BACILLUS ANTHRACIS; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIAL VIRULENCE; CELLULAR IMMUNITY; CONTROLLED STUDY; DLTABCD GENE; ESTERIFICATION; GENE LOCUS; GENE MUTATION; GRAM POSITIVE BACTERIUM; HOST; MOUSE; NONHUMAN; OPERON; PRIORITY JOURNAL; SPORE GERMINATION; TRANSCRIPTION INITIATION;

ALANINE; ANIMALS; ANTHRAX; BACILLUS ANTHRACIS; BACTERIAL PROTEINS; GENOME, BACTERIAL; IMMUNITY, NATURAL; MICE; MICE, INBRED DBA; OPERON; PEPTIDES; SPORES, BACTERIAL; TRANS-ACTIVATION (GENETICS); VIRULENCE;

ANIMALIA; BACILLUS ANTHRACIS; BACILLUS ANTHRACIS STR. STERNE; BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 32444449199     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.4.1301-1309.2006     Document Type: Article

References (34)

1. Abachin, E., C. Poyart, E. Pellegrini, E. Milohanic, F. Fiedler, P. Berche, and P. Cuot. 2002. Formation of D-alanyl-lipoteichoic acid is required for adhesion and virulence of Listeria monocytogenes. Mol. Microbiol. 43:1-14.
2. Cheung, H. S., J. Cui, and S. Sun. 1999. Real-time monitoring of Bacillus subtilis endospore components by attenuated total reflection Fourier-transform infrared spectroscopy during germination. Microbiology 145:1043-1048.
3. Collins, L. V., S. A. Kristian, C. Weidenmaier, M. Faigle, K. P. Kessel, J. A. Strijp, F. Gotz, B. Neumeister, and A. Peschel. 2002. Staphylococcus aureus strains lacking D-alanine modifications of teichoic acids are highly susceptible to human neutrophil killing and are virulence attenuated in mice. J. Infect. Dis. 186:214-219.
4. Cutting, S. M., and P. B. Vander Horn. 1990. Genetic analysis, p. 27-74. In C. R. Harwood and S. M. Cutting (ed.), Molecular biological methods for Bacillus. John Wiley, Chichester, England.
5. Dixon, T. C., A. A. Fadl, T. M. Koehler, J. A. Swanson, and P. C. Hanna. 2000. Early Bacillus anthracis-macrophage interactions: intracellular survival and escape. Cell. Microbiol. 2:453-463.
6. Dixon, T. C., M. Meselson, J. Guillemin, and P. C. Hanna. 1999. Anthrax. N. Engl. J. Med. 341:815-826.
7. Driks, A. 2002. Maximum shields: the assembly and function of the bacterial spore coat. Trends Microbiol. 10:251-254.
8. Feng, Z., B. Jiang, J. Chandra, M. Ghannoum, S. Nelson, and A. Weinberg. 2005. Human beta-defensins: differential activity against candidal species and regulation by Candida albicans. J. Dent. Res. 84:445-450.
9. Fisher, N. A., and P. C. Hanna. 2005. Characterization of Bacillus anthracis germinant receptors in vitro. J. Bacteriol. 187:8055-8062.
10. Grangette, C., S. Nutten, E. Palumbo, C. Moreth, J. Dewulf, B. Pot, T. Hartung, P. Hols, and A. Mercenier. 2005. Enhanced anti-inflammatory capacity of a Lactobacillus plantarum mutant synthesizing modified teichoic acids. Proc. Natl. Acad. Sci. USA 102:10321-10326.
11. Guidi-Rontani, C., M. Levy, E. Labruyere, and M. Mock. 1999. Germination of Bacillus anthracis spores within alveolar macrophages. Mol. Microbiol. 31:9-17.
12. Gundmundsson, G. H., and B. Agerberth. 1999. Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system. J. Immunol. Methods 232:45-54.
13. Hanna, P. C., and J. A. Ireland. 1999. Understanding Bacillus anthracis pathogenesis. Trends Microbiol. 7:180-182.
14. Hyyrylainen, H. L., M. Vitikainen, J. Thwaite, H. Wu, M. Sarvas, C. R. Harwood, V. P. Kommen, and K. Stephenson. 2000. D-Alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis. J. Biol. Chem. 275:20696-26703.
15. Iwasaki, H., A. Shimada, and E. Ito. 1986. Comparative studies of lipoteichoic acids from several Bacillus strains. J. Bacteriol. 167:508-516.
16. Iwasaki, H., A. Shimada, K. Yokoyama, and E. Ito. 1989. Structure and glycosylation of lipoteichoic acids in Bacillus strains. J. Bacteriol. 171:424-429.
17. Kim, H. U., and J. M. Goepfort. 1974. A sporulation medium for Bacillus anthracis. J. Appl. Bacteriol. 37:265-267.
18. Koprivnjak, T., A. Peschel, M. H. Gelb, N. S. Liang, and J. P. Weiss. 2002. Role of charge properties of bacterial envelope in bactericidal action of human group UA phospholipase A2 against Staphylococcus aureus. J. Biol. Chem. 277:47636-47644.
19. Kristian, S. A., V. Datta, C. Weidenmaier, R. Kansal, I. Fedtke, A. Peschel, R. L. Gallo, and V. Nizet. 2005. D-Alanylation of teichoic acids promotes group a streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion. J. Bacteriol. 187:6719-6725.
20. Molnar, J., and B. Pragai. 1971. Attempts to detect the presence of teichoic acid in Bacillus anthracis. Acta Microbiol. Acad. Sci. Hung. 18:105-108.
21. Murazumi, N., Y. Sasaki, J. Okada, Y. Araki, and E. Ito. 1981. Biosynthesis of glycerol teichoic acid in Bacillus cereus: formation of linkage unit disaccharide on a lipid intermediate. Biochem. Biophys. Res. Commun. 99:504-510.
22. Neuhaus, F. C., and J. Baddiley. 2003. A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria. Microbiol. Mol. Biol. Rev. 67:686-723.
23. Ouhara, K., H. Komatsuzawa, S. Yamada, H. Shiba, T. Fujiwara, M. Ohara, K. Sayama, K. Hashimoto, H. Kurihara, and M. Sugai. 2005. Susceptibilities of periodontopathogenic and cariogenic bacteria to antibacterial peptides, β-defensins and LL37, produced by human epithelial cells. J. Antimicrob. Chemother. 55:888-896.
24. Perego, M., P. Glaser, A. Minutello, M. A. Strauch, K. Leopold, and W. Fischer. 1995. Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation. J. Biol. Chem. 270:15598-15606.
25. Peschel, A., M. Otto, R. Jack, H. Kalbacher, G. Jung, and F. Gotz. 1999. Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J. Biol. Chem. 274:8405-8410.
26. Popham, D. L. 2002. Specialized peptidoglycan of the bacterial endospore: the inner wall of the lockbox. Cell. Mol. Life Sci. 59:426-433.
27. Read, T. D., S. N. Peterson, N. Tourasse, L. W. Baillie, et al. 2003. The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria. Nature 423:81-86.
28. Ross, J. M. 1955. On the histopathology of experimental anthrax in the guinea-pig. Br. J. Exp. Pathol. 36:336-339.
29. Sasaki, Y., Y. Araki, and E. Ito. 1980. Structure of linkage region between glycerol teichoic acid and peptidoglycan in Bacillus cereus AHU 1030 cell walls. Biochem. Biophys. Res. Commun. 96:529-534.
30. Sasaki, Y., Y. Araki, and E. Ito. 1983. Structure of teichoic-acid- glycopeptide complexes from cell walls of Bacillus cereus AHU 1030. Eur. J. Biochem. 132:207-213.
31. Setlow, P. 2003. Spore germination. Curr. Opin. Microbiol. 6:550-556.
32. Shimada, A., and E. Ito. 1986. Studies on glucosyltransferase and endogenous glucosyl acceptor in Bacillus cereus AHU1030 membranes. J. Biochemistry 100:1507-1521.
33. Sun, A. N., A. Camilli, and D. A. Portnoy. 1990. Isolation of Listeria monocytogenes small-plaque mutants defective for intracellular growth and cell-to-cell spread. Infect. Immun. 58:3770-3778.
34. Weidenmaier, C., S. A. Kristian, and A. Peshcel. 2003. Bacterial resistance to antimicrobial host defenses-an emerging target for novel antiinfective strategies? Curr. Drug Targets 4:643-647.