메뉴 건너뛰기




Volumn 73, Issue 9, 2005, Pages 5685-5696

Identification of a protein subset of the anthrax spore immunome in humans immunized with the anthrax vaccine adsorbed preparation

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRAX VACCINE; ANTISERUM; BACTERIAL ANTIGEN; BACTERIAL PROTEIN; GENOMIC DNA;

EID: 23944438497     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.73.9.5685-5696.2005     Document Type: Article
Times cited : (33)

References (83)
  • 1
    • 0033027329 scopus 로고    scopus 로고
    • PlcR is a pleiotropic regulator of extracellular virulence factor gene expression in Bacillus thuringiensis
    • Agaisse, H., M. Gominet, O. A. Okstad, A. B. Kolsto, and D. Lereclus. 1999. PlcR is a pleiotropic regulator of extracellular virulence factor gene expression in Bacillus thuringiensis. Mol. Microbiol. 32:1043-1053.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1043-1053
    • Agaisse, H.1    Gominet, M.2    Okstad, O.A.3    Kolsto, A.B.4    Lereclus, D.5
  • 2
    • 4043057882 scopus 로고    scopus 로고
    • Mechanistic studies of a flavin-dependent thymidylate synthase
    • Agrawal, N., S. A. Lesley, P. Kuhn, and A. Kohen. 2004. Mechanistic studies of a flavin-dependent thymidylate synthase. Biochemistry 43:10295-10301.
    • (2004) Biochemistry , vol.43 , pp. 10295-10301
    • Agrawal, N.1    Lesley, S.A.2    Kuhn, P.3    Kohen, A.4
  • 3
    • 0030033931 scopus 로고    scopus 로고
    • Identification of a region of genetic variability among Bacillus anthracis strains and related species
    • Andersen, G. L., J. M. Simchock, and K. H. Wilson. 1996. Identification of a region of genetic variability among Bacillus anthracis strains and related species. J. Bacteriol. 178:377-384.
    • (1996) J. Bacteriol. , vol.178 , pp. 377-384
    • Andersen, G.L.1    Simchock, J.M.2    Wilson, K.H.3
  • 5
    • 0031899704 scopus 로고    scopus 로고
    • The katX gene, which codes for the catalase in spores of Bacillus subtilis, is a forespore-specific gene controlled by sigma F, and KatX is essential for hydrogen peroxide resistance of the germinating spore
    • Bagyan, I., L. Casillas-Martinez, and P. Setlow. 1998. The katX gene, which codes for the catalase in spores of Bacillus subtilis, is a forespore-specific gene controlled by sigma F, and KatX is essential for hydrogen peroxide resistance of the germinating spore. J. Bacteriol. 180:2057-2062.
    • (1998) J. Bacteriol. , vol.180 , pp. 2057-2062
    • Bagyan, I.1    Casillas-Martinez, L.2    Setlow, P.3
  • 6
    • 0037123780 scopus 로고    scopus 로고
    • Small talk. Cell-to-cell communication in bacteria
    • Bassler, B. L. 2002. Small talk. Cell-to-cell communication in bacteria. Cell 109:421-424.
    • (2002) Cell , vol.109 , pp. 421-424
    • Bassler, B.L.1
  • 7
    • 0038403691 scopus 로고    scopus 로고
    • The CHAP domain: A large family of amidases including GSP amidase and peptidoglycan hydrolases
    • Bateman, A., and N. D. Rawlings. 2003. The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases. Trends Biochem. Sci. 28:234-237.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 234-237
    • Bateman, A.1    Rawlings, N.D.2
  • 8
    • 0028215784 scopus 로고
    • Salmonella typhimurium loci involved in survival within macrophages
    • Baumler, A. J., J. G. Kusters, I. Stojiljkovic, and F. Heffron. 1994. Salmonella typhimurium loci involved in survival within macrophages. Infect. Immun. 62:1623-1630.
    • (1994) Infect. Immun. , vol.62 , pp. 1623-1630
    • Baumler, A.J.1    Kusters, J.G.2    Stojiljkovic, I.3    Heffron, F.4
  • 10
    • 2942702220 scopus 로고    scopus 로고
    • Characterisation of methionine adenosyltransferase from Mycobacterium smegmatis and M. tuberculosis
    • Berger, B. J., and M. H. Knodel. 2003. Characterisation of methionine adenosyltransferase from Mycobacterium smegmatis and M. tuberculosis. BMC Microbiol. 3:12.
    • (2003) BMC Microbiol. , vol.3 , pp. 12
    • Berger, B.J.1    Knodel, M.H.2
  • 11
    • 0035933529 scopus 로고    scopus 로고
    • A protein antibiotic in the phage qβ virion: Diversity in lysis targets
    • Bernhardt, T. G., I. N. Wang, D. K. Struck, and R. Young. 2001. A protein antibiotic in the phage qβ virion: diversity in lysis targets. Science 292:2326-2329.
    • (2001) Science , vol.292 , pp. 2326-2329
    • Bernhardt, T.G.1    Wang, I.N.2    Struck, D.K.3    Young, R.4
  • 13
    • 0034671801 scopus 로고    scopus 로고
    • The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA)
    • Blankenfeldt, W., M. Asuncion, J. S. Lam, and J. H. Naismith. 2000. The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA). EMBO J. 19:6652-6663.
    • (2000) EMBO J. , vol.19 , pp. 6652-6663
    • Blankenfeldt, W.1    Asuncion, M.2    Lam, J.S.3    Naismith, J.H.4
  • 14
    • 0034441194 scopus 로고    scopus 로고
    • OppA of Listeria monocytogenes, an oligopeptide-binding protein required for bacterial growth at low temperature and involved in intracellular survival
    • Borezee, E., E. Pellegrini, and P. Berche. 2000. OppA of Listeria monocytogenes, an oligopeptide-binding protein required for bacterial growth at low temperature and involved in intracellular survival. Infect. Immun. 68:7069-7077.
    • (2000) Infect. Immun. , vol.68 , pp. 7069-7077
    • Borezee, E.1    Pellegrini, E.2    Berche, P.3
  • 16
    • 0036151303 scopus 로고    scopus 로고
    • Anthrax spores make an essential contribution to vaccine efficacy
    • Brossier, F., M. Levy, and M. Mock, 2002. Anthrax spores make an essential contribution to vaccine efficacy. Infect. Immun. 70:661-664.
    • (2002) Infect. Immun. , vol.70 , pp. 661-664
    • Brossier, F.1    Levy, M.2    Mock, M.3
  • 17
    • 0031038834 scopus 로고    scopus 로고
    • The divIVA minicell locus of Bacillus subtilis
    • Cha, J. H., and G. C. Stewart. 1997. The divIVA minicell locus of Bacillus subtilis. J. Bacteriol. 179:1671-1683.
    • (1997) J. Bacteriol. , vol.179 , pp. 1671-1683
    • Cha, J.H.1    Stewart, G.C.2
  • 18
    • 0032870894 scopus 로고    scopus 로고
    • Characterization of the exosporium of Bacillus cereus
    • Charlton, S., A. J. Moir, L. Baillie, and A. Moir. 1999. Characterization of the exosporium of Bacillus cereus. J. Appl. Microbiol. 87:241-245.
    • (1999) J. Appl. Microbiol. , vol.87 , pp. 241-245
    • Charlton, S.1    Moir, A.J.2    Baillie, L.3    Moir, A.4
  • 19
    • 0027309277 scopus 로고
    • Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase
    • Chen, N. Y., S. Q. Jiang, D. A. Klein, and H. Paulus. 1993. Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase. J. Biol. Chem. 268:9448-9465.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9448-9465
    • Chen, N.Y.1    Jiang, S.Q.2    Klein, D.A.3    Paulus, H.4
  • 21
    • 0021398927 scopus 로고
    • Characterization of inhibitor A, a protease from Bacillus thuringiensis which degrades attacins and cecropins, two classes of antibacterial proteins in insects
    • Dalhammar, G., and H. Steiner. 1984. Characterization of inhibitor A, a protease from Bacillus thuringiensis which degrades attacins and cecropins, two classes of antibacterial proteins in insects. Eur. J. Biochem. 139:247-252.
    • (1984) Eur. J. Biochem. , vol.139 , pp. 247-252
    • Dalhammar, G.1    Steiner, H.2
  • 22
    • 0035674317 scopus 로고    scopus 로고
    • Increased sensitivity to protein synthesis inhibitors in cells lacking tmRNA
    • de la Cruz, J., and A. Vioque. 2001. Increased sensitivity to protein synthesis inhibitors in cells lacking tmRNA. RNA 7:1708-1716.
    • (2001) RNA , vol.7 , pp. 1708-1716
    • De La Cruz, J.1    Vioque, A.2
  • 23
    • 0032969092 scopus 로고    scopus 로고
    • Bacillus subtilis spore coat
    • Driks, A. 1999. Bacillus subtilis spore coat. Microbiol. Mol. Biol. Rev. 63:1-20.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 1-20
    • Driks, A.1
  • 24
    • 0037312795 scopus 로고    scopus 로고
    • YfiK from Escherichia coli promotes export of O-acetylserine and cysteine
    • Franke, I., A. Resch, T. Dassler, T. Maier, and A. Bock. 2003. YfiK from Escherichia coli promotes export of O-acetylserine and cysteine. J. Bacteriol. 185:1161-1166.
    • (2003) J. Bacteriol. , vol.185 , pp. 1161-1166
    • Franke, I.1    Resch, A.2    Dassler, T.3    Maier, T.4    Bock, A.5
  • 25
    • 0033536997 scopus 로고    scopus 로고
    • Anthrax vaccine: Evidence for safety and efficacy against inhalational anthrax
    • Friedlander, A. M., P. R. Pittman, and G. W. Parker. 1999. Anthrax vaccine: evidence for safety and efficacy against inhalational anthrax. JAMA 282:2104-2106.
    • (1999) JAMA , vol.282 , pp. 2104-2106
    • Friedlander, A.M.1    Pittman, P.R.2    Parker, G.W.3
  • 26
    • 0033679563 scopus 로고    scopus 로고
    • Fumarate reductase is essential for Helicobacter pylori colonization of the mouse stomach
    • Ge, Z., Y. Feng, C. A. Dangler, S. Xu, N. S. Taylor, and J. G. Fox. 2000. Fumarate reductase is essential for Helicobacter pylori colonization of the mouse stomach. Microb. Pathog. 29:279-287.
    • (2000) Microb. Pathog. , vol.29 , pp. 279-287
    • Ge, Z.1    Feng, Y.2    Dangler, C.A.3    Xu, S.4    Taylor, N.S.5    Fox, J.G.6
  • 27
    • 0025099504 scopus 로고
    • Selective killing of Klebsiella pneumoniae by 5- trifluoromethylthioribose. Chemotherapeutic exploitation of the enzyme 5-methylthioribose kinase
    • Gianotti, A. J., P. A. Tower, J. H. Sheley, P. A. Conte, C. Spiro, A. J. Ferro, J. H. Fitchen, and M. K. Riscoe. 1990. Selective killing of Klebsiella pneumoniae by 5-trifluoromethylthioribose. Chemotherapeutic exploitation of the enzyme 5-methylthioribose kinase. J. Biol. Chem. 265:831-837.
    • (1990) J. Biol. Chem. , vol.265 , pp. 831-837
    • Gianotti, A.J.1    Tower, P.A.2    Sheley, J.H.3    Conte, P.A.4    Spiro, C.5    Ferro, A.J.6    Fitchen, J.H.7    Riscoe, M.K.8
  • 28
    • 0021205725 scopus 로고
    • Anthrax: The disease in relation to vaccines
    • Hambleton, P., J. A. Carman, and J. Melling. 1984. Anthrax: the disease in relation to vaccines. Vaccine 2:125-132.
    • (1984) Vaccine , vol.2 , pp. 125-132
    • Hambleton, P.1    Carman, J.A.2    Melling, J.3
  • 29
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 32
    • 4444368098 scopus 로고    scopus 로고
    • Identification of Bacillus anthracis proteins associated with germination and early outgrowth by proteomic profiling of anthrax spores
    • Huang, C. M., K. W. Foster, T. S. DeSilva, K. R. Van Kampen, C. A. Elmets, and D. C. Tang. 2004. Identification of Bacillus anthracis proteins associated with germination and early outgrowth by proteomic profiling of anthrax spores. Proteomics 4:2653-2661.
    • (2004) Proteomics , vol.4 , pp. 2653-2661
    • Huang, C.M.1    Foster, K.W.2    DeSilva, T.S.3    Van Kampen, K.R.4    Elmets, C.A.5    Tang, D.C.6
  • 33
    • 0033055035 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway
    • Huang, M, F. B. Oppermann-Sanio, and A. Steinbuchel. 1999. Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway. J. Bacteriol. 181:3837-3841.
    • (1999) J. Bacteriol. , vol.181 , pp. 3837-3841
    • Huang, M.1    Oppermann-Sanio, F.B.2    Steinbuchel, A.3
  • 34
    • 0036175411 scopus 로고    scopus 로고
    • Amino acid-and purine ribonucleoside-induced germination of Bacillus anthracis ΔSterne endospores: GerS mediates responses to aromatic ring structures
    • Ireland, J. A. W., and P. C. Hanna. 2002. Amino acid-and purine ribonucleoside-induced germination of Bacillus anthracis ΔSterne endospores: gerS mediates responses to aromatic ring structures. J. Bacteriol. 184:1296-1303.
    • (2002) J. Bacteriol. , vol.184 , pp. 1296-1303
    • Ireland, J.A.W.1    Hanna, P.C.2
  • 35
    • 0025174225 scopus 로고
    • -) mutants of Bacillus anthracis and with recombinant strains of Bacillus subtilis that produce anthrax protective antigen
    • -) mutants of Bacillus anthracis and with recombinant strains of Bacillus subtilis that produce anthrax protective antigen. Infect. Immun. 58:303-308.
    • (1990) Infect. Immun. , vol.58 , pp. 303-308
    • Ivins, B.E.1    Welkos, S.L.2    Knudson, G.B.3    Little, S.F.4
  • 37
    • 0037634243 scopus 로고    scopus 로고
    • Detection of a luxS-signaling molecule in Bacillus anthracis
    • Jones, M. B., and M. J. Blaser. 2003. Detection of a luxS-signaling molecule in Bacillus anthracis. Infect. Immun. 71:3914-3919.
    • (2003) Infect. Immun. , vol.71 , pp. 3914-3919
    • Jones, M.B.1    Blaser, M.J.2
  • 38
    • 0034056347 scopus 로고    scopus 로고
    • ssrA (tmRNA) plays a role in Salmonella enterica serovar Typhimurium pathogenesis
    • Julio, S. M., D. M. Helthoff, and M. J. Mahan. 2000. ssrA (tmRNA) plays a role in Salmonella enterica serovar Typhimurium pathogenesis. J. Bacteriol. 182:1558-1563.
    • (2000) J. Bacteriol. , vol.182 , pp. 1558-1563
    • Julio, S.M.1    Helthoff, D.M.2    Mahan, M.J.3
  • 39
    • 0033920288 scopus 로고    scopus 로고
    • Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis
    • Kanda-Nambu, K., Y. Yasuda, and K. Tochikubo. 2000. Isozymic nature of spore coat-associated alanine racemase of Bacillus subtilis. Amino Acids 18:375-387.
    • (2000) Amino Acids , vol.18 , pp. 375-387
    • Kanda-Nambu, K.1    Yasuda, Y.2    Tochikubo, K.3
  • 40
    • 0345465673 scopus 로고    scopus 로고
    • SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA)
    • Karzai, A. W., M. M. Susskind, and R. T. Sauer. 1999. SmpB, a unique RNA-binding protein essential for the peptide-tagging activity of SsrA (tmRNA). EMBO J. 18:3793-3799.
    • (1999) EMBO J. , vol.18 , pp. 3793-3799
    • Karzai, A.W.1    Susskind, M.M.2    Sauer, R.T.3
  • 41
    • 0036209592 scopus 로고    scopus 로고
    • Strains of Escherichia coli O157:H7 differ primarily by insertions or deletions, not single-nudeotide polymorphisms
    • Kudva, I. T., P. S. Evans, N. T. Perna, T. J. Barrett, F. M. Ausubel, F. R. Blattner, and S. B. Calderwood. 2002. Strains of Escherichia coli O157:H7 differ primarily by insertions or deletions, not single-nudeotide polymorphisms. J. Bacteriol. 184:1873-1879.
    • (2002) J. Bacteriol. , vol.184 , pp. 1873-1879
    • Kudva, I.T.1    Evans, P.S.2    Perna, N.T.3    Barrett, T.J.4    Ausubel, F.M.5    Blattner, F.R.6    Calderwood, S.B.7
  • 42
    • 0035878128 scopus 로고    scopus 로고
    • Protein secretion and the pathogenesis of bacterial infections
    • Lee, V. T., and O. Schneewind. 2001. Protein secretion and the pathogenesis of bacterial infections. Genes Dev. 15:1725-1752.
    • (2001) Genes Dev. , vol.15 , pp. 1725-1752
    • Lee, V.T.1    Schneewind, O.2
  • 44
    • 0000530294 scopus 로고
    • Anthrax toxin
    • T. C. Monte, S. Kadig, and S. I. Ajl (ed.). Academic Press, Inc., New York, N.Y.
    • Lincoln, R., and D. C. Fish. 1970. Anthrax toxin, p. 361-414. In T. C. Monte, S. Kadig, and S. I. Ajl (ed.), Microbial toxins. Academic Press, Inc., New York, N.Y.
    • (1970) Microbial Toxins , pp. 361-414
    • Lincoln, R.1    Fish, D.C.2
  • 45
    • 0022655565 scopus 로고
    • Comparative efficacy of Bacillus anthracis live spore vaccine and protective antigen vaccine against anthrax in the guinea pig
    • Little, S. F., and G. B. Knudson. 1986. Comparative efficacy of Bacillus anthracis live spore vaccine and protective antigen vaccine against anthrax in the guinea pig. Infect. Immun. 52:509-512.
    • (1986) Infect. Immun. , vol.52 , pp. 509-512
    • Little, S.F.1    Knudson, G.B.2
  • 48
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: Protein domain annotations on the fly
    • Marchler-Bauer, A., and S. H. Bryant. 2004. CD-Search: protein domain annotations on the fly. Nucleic Acids Res. 32:W327-W331.
    • (2004) Nucleic Acids Res. , vol.32
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 49
    • 3342965783 scopus 로고    scopus 로고
    • Mouse susceptibility to anthrax lethal toxin is influenced by genetic factors in addition to those controlling macrophage sensitivity
    • Moayeri, M., N. W. Martinez, J. Wiggins, H. A. Young, and S. H. Leppla. 2004. Mouse susceptibility to anthrax lethal toxin is influenced by genetic factors in addition to those controlling macrophage sensitivity. Infect. Immun. 72:4439-4447.
    • (2004) Infect. Immun. , vol.72 , pp. 4439-4447
    • Moayeri, M.1    Martinez, N.W.2    Wiggins, J.3    Young, H.A.4    Leppla, S.H.5
  • 50
    • 85047692288 scopus 로고    scopus 로고
    • Bacillus anthracis lethal toxin induces TNF-α-independent hypoxia-mediated toxicity in mice
    • Moayeri, M., D. Haines, H. A. Young, and S. H. Leppla. 2003. Bacillus anthracis lethal toxin induces TNF-α-independent hypoxia-mediated toxicity in mice. J. Clin. Investig. 112:670-682.
    • (2003) J. Clin. Investig. , vol.112 , pp. 670-682
    • Moayeri, M.1    Haines, D.2    Young, H.A.3    Leppla, S.H.4
  • 52
    • 0036855348 scopus 로고    scopus 로고
    • Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis
    • Morimoto, T., P. C. Loh, T. Hirai, K. Asai, K. Kobayashi, S. Moriya, and N. Ogasawara. 2002. Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis. Microbiology 148:3539-3552.
    • (2002) Microbiology , vol.148 , pp. 3539-3552
    • Morimoto, T.1    Loh, P.C.2    Hirai, T.3    Asai, K.4    Kobayashi, K.5    Moriya, S.6    Ogasawara, N.7
  • 53
    • 0037135520 scopus 로고    scopus 로고
    • Cloning and characterization of a leucyl aminopeptidase from three pathogenic Leishmania species
    • Morty, R. E., and J. Morehead. 2002. Cloning and characterization of a leucyl aminopeptidase from three pathogenic Leishmania species. J. Biol. Chem. 277:26057-26065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26057-26065
    • Morty, R.E.1    Morehead, J.2
  • 54
    • 0027440247 scopus 로고
    • Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages
    • Nunoshiba, T., T. DeRojas-Walker, J. S. Wishnok, S. R. Tannenbaum, and B. Demple. 1993. Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages. Proc. Natl. Acad. Sci. USA 90:9993-9997.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9993-9997
    • Nunoshiba, T.1    DeRojas-Walker, T.2    Wishnok, J.S.3    Tannenbaum, S.R.4    Demple, B.5
  • 55
    • 0030004206 scopus 로고    scopus 로고
    • Mutation in the structural gene for release factor 1 (RF-1) of Salmonella typhimurium inhibits cell division
    • Olafsson, O., J. U. Ericson, R. VanBogelen, and G. R. Bjork, 1996. Mutation in the structural gene for release factor 1 (RF-1) of Salmonella typhimurium inhibits cell division. J. Bacteriol. 178:3829-3839.
    • (1996) J. Bacteriol. , vol.178 , pp. 3829-3839
    • Olafsson, O.1    Ericson, J.U.2    VanBogelen, R.3    Bjork, G.R.4
  • 57
    • 0028294944 scopus 로고
    • Peptide transport by micro-organisms
    • Payne, J. W., and M. W. Smith. 1994. Peptide transport by micro-organisms. Adv. Microb. Physiol. 36:1-80.
    • (1994) Adv. Microb. Physiol. , vol.36 , pp. 1-80
    • Payne, J.W.1    Smith, M.W.2
  • 58
    • 0026031219 scopus 로고
    • The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation
    • Perego, M., C. F. Higgins, S. R. Pearce, M. P. Gallagher, and J. A. Hoch. 1991. The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation. Mol. Microbiol. 5:173-185.
    • (1991) Mol. Microbiol. , vol.5 , pp. 173-185
    • Perego, M.1    Higgins, C.F.2    Pearce, S.R.3    Gallagher, M.P.4    Hoch, J.A.5
  • 59
    • 0028935459 scopus 로고
    • Protective immunity induced by Bacillus anthracis toxin-deficient strains
    • Pezard, C., M. Weber, J. C. Sirard, P. Berche, and M. Mock. 1995. Protective immunity induced by Bacillus anthracis toxin-deficient strains. Infect. Immun. 63:1369-1372.
    • (1995) Infect. Immun. , vol.63 , pp. 1369-1372
    • Pezard, C.1    Weber, M.2    Sirard, J.C.3    Berche, P.4    Mock, M.5
  • 61
    • 0348196787 scopus 로고    scopus 로고
    • In vivo functional genomics of Pseudomonas aeruginosa for high-throughput screening of new virulence factors and antibacterial targets
    • Potvin, E., D. E. Lehoux, I. Kukavica-Ibrulj, K. L. Richard, F. Sanschagrin, G. W. Lau, and R. C. Levesque. 2003. In vivo functional genomics of Pseudomonas aeruginosa for high-throughput screening of new virulence factors and antibacterial targets. Environ. Microbiol. 5:1294-1308.
    • (2003) Environ. Microbiol. , vol.5 , pp. 1294-1308
    • Potvin, E.1    Lehoux, D.E.2    Kukavica-Ibrulj, I.3    Richard, K.L.4    Sanschagrin, F.5    Lau, G.W.6    Levesque, R.C.7
  • 62
    • 0032870733 scopus 로고    scopus 로고
    • Abiotic surface sensing and biofilm-dependent regulation of gene expression in Escherichia coli
    • Prigent-Combaret, C., O. Vidal, C. Dorel, and P. Lejeune. 1999. Abiotic surface sensing and biofilm-dependent regulation of gene expression in Escherichia coli. J. Bacteriol. 181:5993-6002.
    • (1999) J. Bacteriol. , vol.181 , pp. 5993-6002
    • Prigent-Combaret, C.1    Vidal, O.2    Dorel, C.3    Lejeune, P.4
  • 63
    • 0030034520 scopus 로고    scopus 로고
    • Antimycobacterial activities of antisense oligodeoxynucleotide phosphorothioates in drug-resistant strains
    • Rapaport, E., A. Levina, V. Metelev, and P. C. Zamecnik. 1996. Antimycobacterial activities of antisense oligodeoxynucleotide phosphorothioates in drug-resistant strains. Proc. Natl. Acad. Sci. USA 93:709-713.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 709-713
    • Rapaport, E.1    Levina, A.2    Metelev, V.3    Zamecnik, P.C.4
  • 65
    • 0025971265 scopus 로고
    • The spo0K locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence
    • Rudner, D. Z., J. R. LeDeaux, K. Ireton, and A. D. Grossman. 1991. The spo0K locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence. J. Bacteriol. 173:1388-1398.
    • (1991) J. Bacteriol. , vol.173 , pp. 1388-1398
    • Rudner, D.Z.1    LeDeaux, J.R.2    Ireton, K.3    Grossman, A.D.4
  • 66
    • 0034897764 scopus 로고    scopus 로고
    • The LuxS family of bacterial autoinducers: Biosynthesis of a novel quorum-sensing signal molecule
    • Schauder, S., K. Shokat, M. G. Surette, and B. L. Bassler. 2001. The LuxS family of bacterial autoinducers: biosynthesis of a novel quorum-sensing signal molecule. Mol. Microbiol. 41:463-476.
    • (2001) Mol. Microbiol. , vol.41 , pp. 463-476
    • Schauder, S.1    Shokat, K.2    Surette, M.G.3    Bassler, B.L.4
  • 67
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell, M. A. 1993. Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol. 47:597-626.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 68
    • 0031787909 scopus 로고    scopus 로고
    • Aminoacyl tRNA synthetases as targets for new anti-infectives
    • Schimmel, P., J. Tao, and J. Hill. 1998. Aminoacyl tRNA synthetases as targets for new anti-infectives. FASEB J. 12:1599-1609.
    • (1998) FASEB J. , vol.12 , pp. 1599-1609
    • Schimmel, P.1    Tao, J.2    Hill, J.3
  • 69
    • 0034819978 scopus 로고    scopus 로고
    • Generation of a proton potential by succinate dehydrogenase of Bacillus subtilis functioning as a fumarate reductase
    • Schnorpfeil, M., I. G. Janausch, S. Biel, A. Kroger, and G. Unden. 2001. Generation of a proton potential by succinate dehydrogenase of Bacillus subtilis functioning as a fumarate reductase. Eur. J. Biochem. 268:3069-3074.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3069-3074
    • Schnorpfeil, M.1    Janausch, I.G.2    Biel, S.3    Kroger, A.4    Unden, G.5
  • 70
    • 19044394765 scopus 로고    scopus 로고
    • MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus sublitis
    • Sekowska, A., L. Mulard, S. Krogh, J. K. Tse, and A. Danchin. 2001. MtnK, methylthioribose kinase. is a starvation-induced protein in Bacillus sublitis. BMC Microbiol. 1:15.
    • (2001) BMC Microbiol. , vol.1 , pp. 15
    • Sekowska, A.1    Mulard, L.2    Krogh, S.3    Tse, J.K.4    Danchin, A.5
  • 72
    • 0032898513 scopus 로고    scopus 로고
    • The medium-/long-chain fatty acyl-CoA dehydrogenase (fadF) gene of Salmonella typhimurium is a phase 1 starvation-stress response (SSR) locus
    • Spector, M. P., C. C. DiRusso, M. J. Pallen, F. Garcia del Portillo, G. Dougan, and B. B. Finlay. 1999. The medium-/long-chain fatty acyl-CoA dehydrogenase (fadF) gene of Salmonella typhimurium is a phase 1 starvation-stress response (SSR) locus. Microbiology 145:15-31.
    • (1999) Microbiology , vol.145 , pp. 15-31
    • Spector, M.P.1    DiRusso, C.C.2    Pallen, M.J.3    Garcia Del Portillo, F.4    Dougan, G.5    Finlay, B.B.6
  • 73
    • 0037334891 scopus 로고    scopus 로고
    • Identification of the immunodominant protein and other proteins of the Bacillus anthracis exosporium
    • 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.
    • (2003) J. Bacteriol. , vol.185 , pp. 1903-1910
    • Steichen, C.1    Chen, P.2    Kearney, J.F.3    Turnbough Jr., C.L.4
  • 75
    • 0242298623 scopus 로고    scopus 로고
    • An mRNA structure in bacteria that controls gene expression by binding lysine
    • Sudarsan, N., J. K. Wickiser, S. Nakamura, M. S. Ebert, and R. R. Breaker. 2003. An mRNA structure in bacteria that controls gene expression by binding lysine. Genes Dev. 17:2688-2697.
    • (2003) Genes Dev. , vol.17 , pp. 2688-2697
    • Sudarsan, N.1    Wickiser, J.K.2    Nakamura, S.3    Ebert, M.S.4    Breaker, R.R.5
  • 76
    • 0023302148 scopus 로고
    • Factors affecting the germination of spores of Bacillus anthracis
    • Titball, R. W., and R. J. Manchee. 1987. Factors affecting the germination of spores of Bacillus anthracis. J. Appl. Bacteriol. 62:269-273.
    • (1987) J. Appl. Bacteriol. , vol.62 , pp. 269-273
    • Titball, R.W.1    Manchee, R.J.2
  • 77
    • 0025868227 scopus 로고
    • Anthrax vaccines: Past, present and future
    • Turnbull, P. C. 1991. Anthrax vaccines: past, present and future. Vaccine 9:533-539.
    • (1991) Vaccine , vol.9 , pp. 533-539
    • Turnbull, P.C.1
  • 78
    • 0034969908 scopus 로고    scopus 로고
    • The role of antibodies to Bacillus anthracis and anthrax toxin components in inhibiting the early stages of infection by anthrax spores
    • Welkos, S., S. Little, A. Friedlander, D. Fritz, and P. Fellows. 2001. The role of antibodies to Bacillus anthracis and anthrax toxin components in inhibiting the early stages of infection by anthrax spores. Microbiology 147:1677-1685.
    • (2001) Microbiology , vol.147 , pp. 1677-1685
    • Welkos, S.1    Little, S.2    Friedlander, A.3    Fritz, D.4    Fellows, P.5
  • 79
    • 4944256095 scopus 로고    scopus 로고
    • Characterization of adsorbed anthrax vaccine by two-dimensional gel electrophoresis
    • Whiting, G. C., S. Rypkema, T. Adams, and M. J. Corbel. 2004. Characterization of adsorbed anthrax vaccine by two-dimensional gel electrophoresis. Vaccine 22:4245-4251.
    • (2004) Vaccine , vol.22 , pp. 4245-4251
    • Whiting, G.C.1    Rypkema, S.2    Adams, T.3    Corbel, M.J.4
  • 80
    • 0037206833 scopus 로고    scopus 로고
    • Thiamine derivatives bind messenger RNAs directly to regulate bacterial gene expression
    • Winkler, W., A. Nahvi, and R. R. Breaker. 2002. Thiamine derivatives bind messenger RNAs directly to regulate bacterial gene expression. Nature 419:952-956.
    • (2002) Nature , vol.419 , pp. 952-956
    • Winkler, W.1    Nahvi, A.2    Breaker, R.R.3
  • 81
    • 10644269821 scopus 로고    scopus 로고
    • Identification and biochemical characterization of two novel collagen binding MSCRAMMs of Bacillus anthracis
    • Xu, Y., X. Liang, Y. Chen, T. M. Koehler, and M. Hook. 2004. Identification and biochemical characterization of two novel collagen binding MSCRAMMs of Bacillus anthracis. J. Biol. Chem. 279:51760-51768.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51760-51768
    • Xu, Y.1    Liang, X.2    Chen, Y.3    Koehler, T.M.4    Hook, M.5
  • 82
    • 0034778624 scopus 로고    scopus 로고
    • Histopathological studies on virulence of dipeptidyl aminopeptidase IV (DPPIV) of Porphyromonas gingivalis in a mouse abscess model: Use of a DPPIV-deficient mutant
    • Yagishita, H., Y. Kumagai, K. Konishi, Y. Takahashi, T. Aoba, and M. Yoshikawa. 2001. Histopathological studies on virulence of dipeptidyl aminopeptidase IV (DPPIV) of Porphyromonas gingivalis in a mouse abscess model: use of a DPPIV-deficient mutant. Infect. Immun. 69:7159-7161.
    • (2001) Infect. Immun. , vol.69 , pp. 7159-7161
    • Yagishita, H.1    Kumagai, Y.2    Konishi, K.3    Takahashi, Y.4    Aoba, T.5    Yoshikawa, M.6
  • 83
    • 0030902603 scopus 로고    scopus 로고
    • Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis
    • Zhang, Y., S. V. Taylor, H. J. Chiu, and T. P. Begley. 1997. Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis. J. Bacteriol. 179:3030-3035.
    • (1997) J. Bacteriol. , vol.179 , pp. 3030-3035
    • Zhang, Y.1    Taylor, S.V.2    Chiu, H.J.3    Begley, T.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.