Proteomic studies of Bacillus anthracis

Future Microbiology

Volumn 4, Issue 8, 2009, Pages 983-998

  Chitlarut, Theodor ^a   Shafferman, Avigdor ^a  

^a ISRAEL INSTITUTE FOR BIOLOGICAL RESEARCH   (Israel)

Author keywords

Anthrax; Antigen; Bacillus anthracis; Immune response; Infection; Pathogenicity; Proteomics; Secretion; Serological analysis; Spore; Vaccine; Virulence

Indexed keywords

ANTHRAX TOXIN; ANTHRAX VACCINE;

ANTHRAX; BACILLUS ANTHRACIS; BACTERIAL ENDOSPORE; BACTERIAL VIRULENCE; DNA SEQUENCE; GENE LOCATION; HOST PATHOGEN INTERACTION; MOLECULAR INTERACTION; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN TARGETING; PROTEOMICS; REVIEW; SEQUENCE HOMOLOGY; VACCINE PRODUCTION;

ANIMALS; ANTHRAX; BACILLUS ANTHRACIS; BACTERIAL PROTEINS; GENE EXPRESSION PROFILING; HUMANS; MICE; PROTEOME; PROTEOMICS; SPORES, BACTERIAL; VIRULENCE FACTORS;

ANIMALIA; BACILLI (CLASS); BACILLUS ANTHRACIS; BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 70449449494     PISSN: 17460913     EISSN: None     Source Type: Journal    
DOI: 10.2217/fmb.09.73     Document Type: Review

References (144)

1. Mock M, Fouet A: Anthrax. Annu. Rev. Microbiol. 55, 647-671 (2001).
2. Passalacqua KD, Bergman NH: Bacillus anthracis: interactions with the host and establishment of inhalational anthrax. Future Microbiol. 1(4), 397-415 (2006).
3. Mock M, Mignot T: Anthrax toxins and the host: a story of intimacy. Cell. Microbiol. 5(1), 15-23 (2003).
4. Perego M, Hoch JA: Commingling regulatory systems following acquisition of virulence plasmids by Bacillus anthracis. Trends Microbiol. 16(5), 215-221 (2008). ■ Excellent review covering the regulatory systems of Bacillus anthracis virulence and chromosome-plasmid gene crosstalk.
5. Fouet A, Mock M: Regulatory networks for virulence and persistence of Bacillus anthracis. Curr. Opin. Microbiol. 9(2), 160-166 (2006). ■ Excellent, concise review covering the regulatory circuits of B. anthracis virulence, in particular the pivotal role of AtxA.
6. Koehler TM: Bacillus anthracis genetics and virulence gene regulation. Curr. Top. Microbiol. Immunol. 271, 144-164 (2002).
7. Brey RN: Molecular basis for improved anthrax vaccines. Adv. Drug Deliv. Rev. 57(9), 1266-1292 (2005).
8. Friedlander A, Welkos S, Ivins BE: Anthrax vaccines. Curr. Top. Microbiol. Immunol. 271, 33-60 (2002).
9. Scorpio A, Blank TE, Day WA, Chabot DJ: Anthrax vaccines: Pasteur to present. Cell. Mol. Life Sci. 63(19-20), 2237-2248 (2006).
10. Ferrari ME, Hemanson G, Rolland A: Development of anthrax DNA vaccines. Curr. Opin. Mol. Ther. 6(5), 506-512 (2004).
11. Tournier JN, Ulrich RG, Quesnel-Hellman A, Mohamadzadeh M, Stiles BG: Anthrax, toxins and vaccines: a 125-year journey targeting Bacillus anthracis. Expert Rev. Anti Infect. Ther. 7(2), 219-236 (2009).
12. Edwards KA, Clancy HA, Baeumner AJ: Bacillus anthracis: toxicology, epidemiology and current rapid-detection methods. Anal. Bioanal. Chem. 384(1), 73-84 (2006).
13. Kolsø AB, Lereclus D, Mock M: Genome structure and evolution of the Bacillus cereus group. Curr. Top. Microbiol. Immunol. 264(2), 95-108 (2002).
14. Vilas-Boas GT, Peruca APS, Arantes OMN: Biology and taxonomy of Bacillus cereus, Bacillus anthracis, and Bacillus thuringiensis. Can. J. Microbiol. 53(6), 673-687 (2007).
15. Pasteur L: Classics of biology and medicine. Summary report of the experiments conducted at Pouilly-le-Fort, near Melun, on the anthrax vaccination. Translation of the original 1881 article. Yale J. Biol. Med. 75(1), 59-62 (2002). ■■ Republished classical Pasteur paper translated into English, documenting the historical successful anthrax vaccination of domestic animals.
16. Baillie L, Read T: Bacillus anthracis, a bug with attitude. Curr. Opin. Microbiol. 4(1), 78-81 (2001).
17. Turnbull PCB: Introduction: anthrax history, disease and ecology. Curr. Top. Microbiol. Immunol. 271, 34-60 (2002).
18. Blendon RJ, Benson JM, Des Roches CM, Pollard WE, Parvanta C, Herrmann MJ: The impact of anthrax attacks on the American public. Med. Gen. Med. 4(2), 1 (2002).
19. Rasko DA, Alther MR, Han CS, Ravel J: Genomics of the Bacillus cereus group of organisms. FEMS Microbiol. Rev. 29(2), 303-329 (2005).
20. Helgason E, Økstad OA, Caugant DA et al.: Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis - one species on the basis of genetic evidence. Appl. Environ. Microbiol. 66(6), 2627-2630 (2000).
21. 2-bicarbonate and aerobic atmospheres. PLoS One 4(3), e4904 (2009).
22. Hu X, Van der Auwera G, Timmery S, Zhu L, Mahillon J: Distribution, diversity, and potential mobility of extrachromosomal elements related to the Bacillus anthracis pXO1 and pXO2 virulence plasmids. Appl. Environ. Microbiol. 75(10), 3016-3028 (2009).
23. Hoffmaster AR, Ravel J, Rasko DA et al.: Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax. Proc. Natl Acad. Sci. USA 101(22), 8449-8454 (2004).
24. Gohar M, Faegri K, Perchat S et al.: The PlcR virulence regulon of Bacillus cereus. PLoS One 3(7), e2793 (2008).
25. Agaisse H, Gominet M, Okstad OA, Kolsto AB, Lereclus D: PlcR is a pleiotropic regulator of extracellular virulence factor gene expression in Bacillus thuringiensis. Mol. Microbiol. 32(5), 1043-1053 (1999). ■ Identification of the virulence regulatory factor PlcR of the cereus group of bacilli.
26. Lund T, De Buyser ML, Granum PE: A new cytotoxin from Bacillus cereus that may cause necrotic enteritis. Mol. Microbiol. 38(2), 254-261 (2000).
27. Okstad OA, Gominet M, Purnelle B, Ros M, Lereclus D, Kolsto AB: Sequence analysis of three Bacillus cereus locus carrying PlcR-regulated genes encoding degradative enzymes and enterotoxin. Microbiology 145(Pt 11), 3129-3138 (1999). (Pubitemid 29535033)
28. Mignot T, Mock M, Robichon D, Landier A, Lereclus D, Fouet A: The incompatibility between the PlcR- and AtxA-controlled regulons may have selected a nonsense mutation in Bacillus anthracis. Mol. Microbiol. 42(5), 1189-1198 (2001). ■■ Evidence of the dormant state of the PlcR regulon in B. anthracis and the importance of this evolutionary gene silencing for B. anthracis virulence.
29. Lacy TM, Collier RJ: Structure and function of anthrax toxin. Curr. Top. Microbiol. Immunol. 271, 62-85 (2002).
30. Cendrowski S, MacArthur W, Hanna P: Bacillus anthracis requires siderophore biosynthesis for growth in macrophages and mouse virulence. Mol. Microbiol. 51(2), 407-417 (2004).
31. Fisher N, Shetron-Rama L, Herring-Palmer A, Heffernan B, Bergman N, Hanna P: The dltABCD Operon of Bacillus anthracis Sterne is required for virulence and resistance to peptide, enzymatic, and cellular mediators of innate immunity. J. Bacteriol. 188(4), 1301-1309 (2006). (Pubitemid 43228663)
32. Heffernan B, Thomason B, Herring-Palmer A et al.: Bacillus anthracis phospholipases C facilitate macrophage-associated growth and contribute to virulence in a murine model of inhalation anthrax. Infect. Immun. 74 (7), 3756-3764 (2006).
33. Passalacqua KD, Bergman NH, Herring-Palmer A, Hanna P: The superoxide dismutase of Bacillus anthracis do not cooperatively protect against endogenous superoxide stress. J. Bacteriol. 188(11), 3837-3848 (2006). (Pubitemid 43825389)
34. Ross C, Koehler T: plcR papR-independent expression of anthrolysin O by Bacillus anthracis. J. Bacteriol. 188(22), 7823-7829 (2006). (Pubitemid 44764519)
35. 2/bicarbonate responsiveness of the virulence regulons of B. anthracis.
36. Gat O, Mendelson I, Chitlaru T et al.: The solute-binding component of a putative Mn(II) ABC transporter (MntA) is a novel Bacillus anthracis virulence determinant. Mol. Microbiol. 58(2), 533-551 (2005). ■■ Identification of a novel B. anthracis virulence factor.
37. Gat O, Zaide G, Inbar I et al.: Characterization of Bacillus anthracis iron-regulated surface determinant (Isd) proteins containing NEAT domains. Mol. Microbiol. 70(4), 983-999 (2008).
38. Bradley K, Mogridge J, Mourez M, Collier B, Young J: Identification of the cellular receptor for anthrax toxin. Nature 414(6860) 225-229 (2001). ■■ Identification of the cellular receptor for protective antigen (PA) on host target cells. (Pubitemid 33051239)
39. Klimpel KR, Arora N, Leppla SH: Anthrax toxin lethal factor contains a zinc metal loprotease consensus sequence which is required for lethal toxin activity. Mol. Microbiol. 13 (6), 1093-1100 (1994). ■ Identification of the biological role of the toxin subunit lethal factor.
40. Leppla S: Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl Acad. Sci. USA 79(10), 3162-3166 (1982). ■ Identification of the biological role of the toxin subunit edema factor.
41. Leppla S: The bifactorial B. anthracis lethal and oedema toxins. In: Comprehensive Sourcebook of Bacterial Protein Toxins. Alouf JE, Freer JH (Eds). Academic Press, London, UK, 243-263 (1999).
42. Singh Y, Klimpel K, Goel S, Swain P, Leppla S: Oligomerization of anthrax toxin protective antigen and binding of lethal factor during endocytic uptake into mammalian cells. Infect. Immun. 67(4), 1853-1859 (1999).
43. Drysdale M, Bourgogne A, Hilsenbeck SG, Koehler TM: AtxA controls Bacillus anthracis capsule synthesis via acpA and newly discovered regulator, acpB. J. Bacteriol. 186(2), 307-315 (2004). (Pubitemid 38076419)
44. Drysdale M, Bourgogne A, Koehler TM: Transcriptional analysis of the Bacillus anthracis capsule regulators. J. Bacteriol. 187(15), 5108-5114 (2005). (Pubitemid 41022928)
45. Mignot T, Mock M, Fouet A: A plasmid-encoded regulator couples the synthesis of toxins and surface structures in Bacillus anthracis. Mol. Microbiol. 47(4), 917-927 (2003). ■ Pioneering demonstration of a crosstalk mechanism linking the expression of plasmid- and chromosome-located genes in B. anthracis.
46. Saile E, Koehler TM: Control of anthrax toxin gene expression by the transition state regulator abrB. J. Bacteriol. 184(2), 370-380 (2002). (Pubitemid 34027376)
47. Strauch M, Ballar P, Rowshan AJ, Zoller KL: The DNA-binding specificity of the Bacillus anthracis AbrB protein. Microbiology 151(Pt 6), 1751-1759 (2005). (Pubitemid 40909019)
48. Abramova FA, Grinberg LM, Yampolskaya OV, Walker DH: Pathology of inhalation anthrax in 42 cases from the Sverdlovsk outbreak of 1979. Proc. Natl Acad. Sci. USA 90(6), 2291-2294 (1993).
49. Aronson AI, Bell C, Fulroth B: Plasmid-encoded regulator of extracellular proteases in Bacillus anthracis. J. Bacteriol. 187(9), 3133-3138 (2005). (Pubitemid 40571606)
50. Popov SG, Popova TG, Hopkins S et al.: Effective anti-protease treatment of experimental anthrax. BMCInfect. Dis. 5, 25 (2005).
51. Chung MC, Popova TG, Millis BA et al.: Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors. J. Biol. Chem. 281(42), 31408-31418 (2006).
52. Chung MC, Popova TG, Jorgensen SC et al.: Degradation of circulating von Willebrandt factor and its regulator ADAMTS13 implicates secreted Bacillus anthracis metalloproteases in anthrax consumptive coagulopathy. J. Biol. Chem. 283(15), 9531-9542 (2008).
53. Vasconcelos D, Barnewall R, Rabin M et al.: Pathology of inhalation anthrax in cynomolgus monkeys (Mecacafascicularis). Lab. Invest. 83, 1201-1209 (2003). (Pubitemid 37013055)
54. Miyoshi S, Shinoda S: Microbial metalloproteases in pathogenesis. Microbes Infect. 2(1), 91-98 (2000).
55. Ivins BE, Welkos SL: Recent advances in the development of an improved, human anthrax vaccine. Eur. J. Epidemiol. 4(1), 12-19 (1988).
56. Reuveny S, White M, Adar Y et al.: Search for correlates of protective immunity conferred by anthrax vaccine. Infect. Immunol. 69(5), 2888-2893 (2002).
57. Marcus H, Danieli R, Epstein E, Velan B, Shafferman A, Reuveny S: Contribution of immunological memory to protective immunity conferred by a Bacillus anthracis protective antigen-based vaccine. Infect. Immunol. 72(6), 3471-3477 (2004).
58. Pezard C, Berche P, Mock M: Contribution of individual toxin components to virulence of Bacillus anthracis. Infect. Immunol. 59(10), 3472-3477 (1991).
59. Pezard C, Weber M, Sirard JC, Berche P, Mock M: Protective immunity induced by Bacillus anthracis toxin-deficient strains. Infect. Immunol. 63(4), 1369-1372 (1995). ■ Demonstration that bacterial constituents other than PA may contribute to immune protection.
60. Leppla S, Robbins J, Schneerson R, Shiloach J: Development of an improved vaccine for anthrax. J. Clin. Invest. 110(2), 141-144 (2002).
61. Price BM, Liner AL, Park S, Leppla SH, Mateczun A, Galloway DR: Protection against lethal toxin challenge by genetic immunization with a plasmid encoding the lethal factor protein. Infect. Immun. 69(7), 4509-4515 (2001).
62. Schneerson R, Kubler-Kielb J, Liu TY et al.: Poly-D-glutamic acid protein conjugates induce IgG antibodies in mice to the capsule of Bacillus anthracis: a potential addition to the anthrax vaccine. Proc. Natl Acad. Sci. USA 100(15), 8945-8950 (2003).
63. Rhie GE, Roehrl MH, Mourez M, Collier RJ, Mekalanos JJ, Wang JY: A dually active anthrax vaccine that confers protection against both bacilli and toxins. Proc. Natl Acad. Sci. USA 100(19), 10925-10930 (2003). ■ Improvement of the PA-based vaccine by anticapsule immune response.
64. Cohen S, Mendelson I, Altboum Z et al.: Attenuated nontoxinogenic and nonencapsulated recombinant Bacillus anthracis spore vaccines protect against anthrax. Infect. Immunol. 68(8), 4549-4558 (2000).
65. Mendelson I, Gat O, Aloni-Grinstein R et al.: Efficacious, nontoxigenic Bacillus anthracis spore vaccines based on strains expressing mutant variants of lethal toxin components. Vaccine 23(48-49), 5688-5697 (2005). (Pubitemid 41608618)
66. Aloni-Grinstein R, Gat O, Altboum Z, Velan B, Cohen S, Shafferman A: Oral spore vaccine based on live attenuated nontoxinogenic Bacillus anthracis expressing recombinant mutant protective antigen. Infect. Immun. 73 (7), 4043-4053 (2005).
67. Brassier F, Levy M, Mock M: Anthrax spores make an essential contribution to vaccine efficacy. Infect. Immunol. 70(2), 661-664 (2002). ■ Demonstration that spore-associated constituents may contribute to immune protection.
68. Fellows PF, Linscott MK, Ivins BE et al.: 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(23-24), 3241-3247 (2001).
69. Chakravarti D, Fiske M, Fletcher L, Zagursky R: Application of genomics and proteomics for identification of bacterial gene products as potential vaccine candidates. Vaccine 19(6), 601-612 (2001). (Pubitemid 30821730)
70. Grandi G: Rational antibacterial vaccine design through genomic technologies. Int. J. Parasitol. 33, 615-620 (2003).
71. Sinchaikul S, Sookkheo B, Topanuruk S, Juan HF, Phutrakul S, Chen ST: Bioinformatics, functional genomics, and proteomics study of Bacillus sp. J. Chromatogr. 771(1-2), 261-287 (2002). (Pubitemid 34457732)
72. Godovak-Zimmerman J, Brown LR: Perspectives for mass spectrometry and functional proteomics. Mass Spectrom. Rev. 20(1), 1-57 (2001).
73. Wu HJ, Wang AH, Jennings MP: Discovery of virulence factors of pathogenic bacteria. Curr. Opin. Chem. Biol. 12(1), 93-101 (2008).
74. Tonella L, Hoogland C, Binz PA, Appel R, Hochstrasser D, Sanchez JC: New perspectives in the E. coli proteome investigation. Proteomics 1(3), 409-423 (2001). (Pubitemid 33585114)
75. Ueberle B, Frank R, Hermann R: The proteome of the bacterium Mycoplasma pneumoniae: comparing predicted open reading frames to identified gene products. Proteomics 2(6), 754-764 (2002). (Pubitemid 34693578)
76. Nowens A, Cordwell SJ, Larsen MR et al.: Complementing genomics with proteomics: the membrane subproteome of Pseudomonas aeruginosa PAO1. Electrophoresis 21(17), 3797-3809 (2000).
77. Nouwens AS, Willcox MDP, Walsh BJ, Cordwell SJ: Proteomic comparison of membrane and extracellularproteins from invasive (PAO1) and cytotoxic (6206) strains of Pseudomonas aeruginosa. Proteomics 2(19), 1325-1346 (2002).
78. Butner K, Bernhardt J, Scharf C et al.: A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis. Electrophoresis 22(14), 2908-2935 (2001).
79. Eymann C, Homuth G, Scharf C, Hecker M: Bacillus subtilis functional genomics: Global characterization of the stringent response by proteome and transcriptome analysis. J. Bacteriol. 184(9), 2500-2520 (2002). (Pubitemid 34311144)
80. Bambini S, Rappuoli R: The use of genomics in microbial vaccine development. Drug Discov. Today 14(5-6), 253-260 (2009).
81. Wack A, Rappuoli R: Vaccinology at the beginning of the 21st century. Curr. Opin. Immunol. 17(4), 411-418 (2005).
82. Rappuoli R: Reverse vaccinology, a genome based approach to vaccine development. Vaccine 19(17-19), 2688-2691 (2001).
83. Khan AS, Mujer CV, Alefantis TG et al.: Proteomics and bioinformatics strategies to design countermeasures against infectious threats agents. J Chem. Inf. Model. 46(1), 111-115 (2006).
84. Klade CS, Voss T, Krystek E et al.: Identification of tumor antigens in renal cell carcinoma by serological proteome analysis. Proteomics 1(7), 890-898 (2001). (Pubitemid 33587414)
85. Read TD, Peterson SN, Tourasse N et al.: The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria. Nature 423(6935), 81-86 (2003). ■ DNA sequence and functional annotation of the B. anthracis chromosome. (Pubitemid 36569586)
86. Okinaka R, Cloud K, Hampton O et al.: Sequence, assembly and analysis of pXO1 and pXO2. J. Appl. Microbiol. 87(2), 261-262 (1999). ■ DNA sequence and functional annotation of the B. anthracis native virulence plasmids.
87. Ariel N, Zvi A, Grosfeld H et al.: Search for potential vaccine candidate ORFs in the B. anthracis virulence plasmid pXO1 - in silico and in vitro screening. Infect. Immun. 70 (12), 6817-6827 (2002). ■ Bioinformatic analysis of the B. anthracis native virulence plasmid pXO1 with emphasis on identification of vaccine candidates.
88. Ariel N, Zvi A, Makarova K et al.: Genome-based bioinformatic selection of chromosomal B. anthracis putative vaccine candidates coupled with proteomic identification of surface-associated antigens. Infect. Immun. 71(8), 4563-4579 (2003). ■ Provides a list of 500 vaccine candidates identified by bioinformatic analysis of the B. anthracis chromosomal genes, confirmed by a limited proteomic inspection of membrane proteins.
89. Bourgogne A, Drysdale M, Hilsenbeck SH, Peterson SN, Koehler TM: Global effects of virulence gene regulators in Bacillus anthracis strain with both virulence plasmids. Infect. Immun. 71(5), 2736-2743 (2003).
90. Chitlaru T, Ariel N, Zvi A et al.: Identification of chromosomally encoded membranal polypeptides of Bacillus anthracis by a proteomic analysis: prevalence of proteins containing S-layer homology domains. Proteomics 4(3), 677-691 (2004). ■ First study addressing the membrane proteome of B. anthracis and identification of the most abundant surface proteins. Established the prevalent utilization of S-layer homology domain-mediated docking for surface localization of exported proteins. (Pubitemid 38339148)
91. 2-dependent cross-talk mechanisms modulate extracellular proteolytic activities. J. Bacteriol. 188(10), 3551-3571 (2006). ■■ Proteomic examination of secreted proteins by several B. anthracis strains under various culturing conditions, providing a list of the 71 most abundant secreted proteins, their patterns of expression and theoretical relatedness to virulence. (Pubitemid 43726220)
92. Chitlaru T, Gat O, Gozlan Y, Grosfeld H, Inbar I, Shafferman A: Identification of in vivo expressed immunogenic proteins by serological proteome analysis of Bacillus anthracis secretome. Infect. Immunol. 75(6), 2841-2852 (2007). ■ Serological proteome analysis providing a list of 80 immunogenic proteins expressed during infection. Describes pilot studies of protection involving proteomically identified targets.
93. Gat O, Grosfeld H, Ariel N et al.: Search for Bacillus anthracis potential vaccine candidates by a functional genomic-serologic screen. Infect. Immun. 74(7), 3987-4001 (2006). ■ Serological analysis of over 200 bio-informatically selected open reading frames. Provides a functional and structural analysis of bacterial proteins expressed during infection.
94. Gat O, Grosfeld H, Shafferman A: In vitro screen of bioinformatically selected Bacillus anthracis vaccine candidates by coupled transcription, translation and immunoprecipitation analysis. Methods Mol. Biol. 375, 211-233 (2007).
95. Liu H, Bergman NH, Thomason B et al.: Formation and composition of the Bacillus anthracis endospore. J. Bacteriol. 186(1), 164-178 (2004). ■ Extensive transcriptomic and proteomic analysis of spores. Provides a list of 750 proteins present in a spore-enriched preparation. (Pubitemid 38020298)
96. Huang CM, Foster KW, DeSilva TS, Van Kampen KR, Elmets CA, Tang DC: Identification of Bacillus anthracis proteins associated with germination and early outgrowth by proteomic profiling of anthrax spores. Proteomics 4(9), 2653-2661 (2004). ■ Limited proteomic study of cultures at an early postgermination phase.
97. Francis AW, Ruggiero CE, Koppisch AT et al.: Proteomic analysis ofBacillus anthracis Sterne vegetative cells. Biochim. Biophys. Acta 1748(2), 191-200 (2005). ■ Shotgun whole-cell proteomic analysis of vegetative cells. Provides a list of over 1000 proteins.
98. Wang J, Ying T, Wang Z et al.: 2-D reference map of Bacillus anthracis vaccine strain A16R proteins. Proteomics 5(17), 4488-4495 (2005). ■ Limited whole-cell proteomics for mapping purposes. Identified 300 proteins. (Pubitemid 41739926)
99. Antelmann H, Williams RC, Miethke M et al.: The extracellular and cytoplasmic proteomes of the non-virulent Bacillus anthracis strain UM23C1-2. Proteomics 5(14), 3684-3695 (2005). ■ Identified 64 abundant secreted proteins. (Pubitemid 41393301)
100. Gohar M, Gilois N, Graveline R, Garreau C, Sanchis V, Lereclus D: A comparative study of B. cereus, B. thuringiensis and B. anthracis extracellular proteomes. Proteomics 5(14), 3696-3711 (2005). ■ Comparative proteomic analysis showing the uniqueness of the B. anthracis secretome versus that of related cereus strains.
101. Lamonica JM, Wagner M, Eschenbrenner M et al.: Comparative secretome analyses of three Bacillus anthracis strains with variant plasmid contents. Infect. Immunol. 73(6), 3646-3658 (2005). ■ Limited differential proteomic study of secreted proteins in the presence/absence of virulence plasmids. Identified 26 secreted proteins.
102. Walz A, Mujer C, Connolly JP et al.: Bacillus anthracis secretome time course under host-simulated conditions and identification of immunogenic proteins. Proteome Sci. 5, 11 (2007). ■ Provides a list of 275 secreted proteins. Serological analysis using human convalescent sera identifies three immunodominant antigens. (Pubitemid 47308272)
103. Del Vecchio VG, Connolly JP, Alefantis TG et al.: Proteomic profiling and identification of immunodominant spore antigens of Bacillus anthracis, Bacillus cereus and Bacillus thuringiensis. Appl. Environ. Microbiol. 72(9), 6355-6363 (2006). ■ Serological proteome analysis of secretomes identifies 15 immunogens, two of which are specific for B. anthracis.
104. Lai EM, Phadke ND, Katcman MT et al.: Proteomic analysis of the spore coats of Bacillus subtillis and Bacillus anthracis. J. Bacteriol. 185(4), 1443-1454 (2003). ■ First proteomic analysis of spore coats.
105. Park SH, Oh HB, Seong WK, Kim CW, Cho SY, Yoo CK: Differential analysis of Bacillus anthracis after pXO1 plasmid curing and comprehensive data on Bacillus anthracis infection in macrophages and glial cells. Proteomics 7(20), 3743-3758 (2007). ■ Identification of over 1700 proteins by whole-cell analysis and more than 70 differentially expressed upon pXO1 curing.
106. Guidi-Rontani C, Weber-Levy M, Labruyere E, Mock M: Germination of Bacillus anthracis spores within alveolar macrophages. Mol. Microbiol. 31(1), 9-17 (1999).
107. Welkos SL, Trotter RW, Becker DM, Nelson GO: Resistance to the Sterne strain of B. anthracis: phagocytic cell responses of resistant and susceptible mice. Microb. Pathog. 7(20), 15-36 (1989).
108. Cleret A, Quesncl-Hellmann A, Vallon-Eberhard A et al.: Lung dendritic cells rapidly mediate anthrax spore entry through the pulmonary route. J. Immunol. 178, 7994-8001 (2007). (Pubitemid 46898070)
109. Sanz P, Teel LD, Alem F, Carvalho HM, Darnell SC, O'Brien AD: Detection of Bacillus anthracis spore germination in vivo by bioluminescence imaging. Infect. Immunol. 76(3), 1036-1047 (2008).
110. Cote CK, Bozue J, Twenhafel N, Welkos SL: Effects of altering the germination potential of Bacillus anthracis spores by exogenous means in a mouse model. J. Med. Microbiol. 58(Pt 6), 816-825 (2009).
111. Gossens PL, Sylvestre P, Mock M: Of spore opsonization and passive protection against anthrax. Microbiology 153(2), 301-302 (2007). (Pubitemid 46306476)
112. Welkos S, Little S, Friedlander A, Fritz D, Fellows P: The role of antibodies to Bacillus anthracis and anthrax toxin components in inhibiting the early stages of infection by anthrax spores. Microbiology 147(Pt 6), 1677-1685 (2001). (Pubitemid 32544833)
113. Kudva IT, Griffin RW, Garren JM, Calderwood SB, John M: Identification of a protein subset of the anthrax spore immunome in humans immunized with the anthrax vaccine adsorbed preparation. Infect. Immun. 73(9), 5685-5696 (2005). ■ Identification of immunogenic proteins present in the human PA-based (US) vaccine.
114. Whiting GC, Rijpkema S, Adams T, Corbel M: Characterization of adsorbed anthrax vaccine by two-dimensional gel electrophoresis. Vaccine 22(31-32), 4245-4251 (2004). ■ Identification of immunogenic proteins present in the human PA-based (UK) vaccine. (Pubitemid 39330347)
115. Cote CK, Bozue J, Moody KL, DiMezzo TL, Chapman CE, Welkos SL: Analysis of novel spore antigen in Bacillus anthracis that contributes to spore opsonization. Microbiology 154(Pt 2), 619-632 (2008). (Pubitemid 351292315)
116. Cossart P, Sansonetti P: Bacterial invasion: the paradigms of enteroinvasive pathogens. Science 304(5668), 242-246 (2004). (Pubitemid 38452169)
117. Cybulski RJ, Sanz P, McDaniel D, Darnell S, Bull RL, O'Brian AD: Recombinant Bacillus anthracis spore proteins enhance protection pf mice primed with suboptimal amounts of protective antigen. Vaccine 26(38), 4927-4939 (2008).
118. Driks A: The Bacillus subtilis spore coat. Microbiol. Mol. Biol. Rev. 63(1), 1-20 (1999).
119. Driks A: Proteins of the spore core and coat. In: Bacillus subtilis and its Closest Relatives. Sonenshein AL, Hoch JA, Losick R (Eds). ASM Press, Washington DC, USA, 527-536 (2002).
120. Steichen C, Chen P, Kearney JF, Turnbough CL: Identification of the immunodominant protein and other proteins of the Bacillus anthracis exosporium. J. Bacteriol. 185(6), 1903-1910 (2003). ■ First identification of immunodominant spore antigens.
121. Todd S, Moir AJC, Johnson MJ, Moir A: Genes of Bacillus anthracis encoding proteins of the exosporium. J. Bacteriol. 185(11), 3373-3378 (2003).
122. Redmond C, Baillie LWJ, Hibbs S, Moir AJC, Moir A: Identification of proteins in the exosporium of B. anthracis. Microbiology 150(Pt 2), 355-363 (2004).
123. Sylvestre P, Couture-Torsi E, Mock M: A collagen-like surface glycoprotein is a structural component of the Bacillus anthracis exosporium. Mol. Microbiol. 45(1), 169-178 (2002). ■ Identification of the prevalent immuodominant exosporium protein.
124. Bozue J, Moody KL, Cote CK et al.: Bacillus anthracis spores of the bclA mutant exhibit increased adherence to epithelial cells, fibroblasts, and endothelial cells but not to macrophages. Infect. Immun. 75(9), 4498-4505 (2007).
125. Brahmbatt TN, Darnell SC, Carvalho HM et al.: Recombinant exosporium protein BclA of Bacillus anthracis is effective as a booster for mice primed with suboptimal amounts of protective antigen. Infect. Immunol. 75(11), 5240-5247 (2007).
126. Ramarao N, Lereclus D: The InhA1 metalloprotease allows spores of the B. cereus group to escape macrophages. Cell. Microbiol. 7(9), 1357-1364 (2005).
127. Mukhopadyay S, Akmal A, Stewart A, Hsia R, Read TD: Identification of Bacillus anthracis spore component antigens conserved across diverse Bacillus cereus sensu lato strains. Mol. Cell. Proteomics 8(6), 1174-1191 (2009). ■ In silico selection of 200 potential targets combined with functional and proteomic/serological analysis of spore preparations; identifies two potential diagnostic markers.
128. Sutcliffe I, Harrington D: Pattern searches for the identification of putative lipoprotein genes in Gram-positive bacterial genomes. Microbiology 148(Pt 7), 2065-2077 (2002). (Pubitemid 34785291)
129. Mesnage S, Tosi-Couture E, Mock M, Gounon P, Fouet A: Molecular characterization of the Bacillus anthracis main S-layer component: evidence that it is the major cell-associated antigen. Mol. Microbiol. 23(6), 1147-1155 (1997). ■ Demonstration that the S-layer components are major antigens.
130. Fouet A, Mesnage S, Tosi-Couture E, Gounon P, Mock M: Bacillus anthracis surface: capsule and S-layer. J. Appl. Microbiol. 87(2), 251-255 (1999).
131. Fouet A, Mesnage S: Bacillus anthracis cell envelope components. Curr. Top. Microbiol. Immunol. 271, 87-113 (2002).
132. Mignot T, Mesnage S, Couture-Tosi E, Mock M, Fouet A: Developmental switch of S-layer protein synthesis in B. anthracis. Mol. Microbiol. 43(6), 1615-1627 (2002).
133. Lee VT, Schneewind O: Protein secretion and the pathogenesis of bacterial infections. Genes Dev. 15(14), 1725-1752 (2001). ■ Excellent review covering bacterial secretion systems and their role in pathogenesis.
134. Tjalsma H, Antelman H, Jongbloed JDH et al.: Proteomics of protein secretion by Bacillus subtilis: separating the "secrets" of the secretome. Microbiol. Mol. Biol. Rev. 68(2), 207-233 (2004). ■ Excellent review covering secretion in Bacillus subtilis and the contribution of proteomics to dissection of the secretome.
135. Sibbald MJJB, Ziebandt AK, Engelman S et al.: Mapping the pathways to staphylococcal pathogenesis by comparative secretomics. Microbiol. Mol. Biol. Rev. 70(3), 755-788 (2006).
136. Braunstein M, Espinosa BJ, Chan J, Belisle JT, Jakobs WR Jr: Sec A2 functions in the secretion of the superoxide dismutase A and in the virulence of Mycobacterium tuberculosis. Mol. Microbiol. 48(2), 453-464 (2003).
137. Lenz L, Mohammadi S, Geissler A, Portnoy DA: SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis. Proc. Natl Acad. Sci. USA 100(21), 12432-12437 (2003).
138. Sela-Abramovich S, Chitlaru T, Gat O, Grosfeld H, Cohen O, Shafferman A: Novel and unique diagnostic biomarkers for Bacillus anthracis infection. Appl. Environ. Microbiol. 75(19), 6157-6167 (2009). ■ Feasibility study addressing the search for novel biomarkers of infection and the use of three proteomically identified targets as diagnostic markers.
139. Wiese S, Reidegeld KA, Meyer HE, Warscheid B: Protein labeling by iTRAQ: a new tool for quantitative mass spectrometry in proteome research. Proteomics 7(3), 340-350 (2007). (Pubitemid 46293976)
140. Ravel J, Jiang L, Stanley ST et al.: The complete genome sequence of Bacillus anthracis Ames "ancestor". J. Bacteriol. 191(1), 445-446 (2009).
141. Haas G, Karaali G, Ebermayer K et al.: Immunoproteomics of Helicobacter pylori infection and relation to gastric disease. Proteomics 2(3), 313-324 (2002). (Pubitemid 34269985)
142. Havlasova J, Hernychova L, Halada P et al.: Mapping of immunoreactive antigens of Francisella tularensis live vaccine strain. Proteomics 2(7), 857-867 (2002). (Pubitemid 34803969)
143. Twine SM, Mykytczuk NC, Petit MD et al.: In vivo proteomic analysis of the intracellular bacterial pathogen, Francisella tularensis, isolated from mouse spleen. Biochem. Biophys. Res. Commun. 345(4), 1621-1633 (2006).
144. Vytvytska O, Nagy E, Blüggel M et al.: Identification of vaccine candidate antigens of Staphylococcus aureus by serological proteome analysis. Proteomics 2(5), 580-590 (2002). (Pubitemid 34526174)