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Volumn 70, Issue 2, 2004, Pages 656-663

Growth Characteristics of Bartonella henselae in a Novel Liquid Medium: Primary Isolation, Growth-Phase-Dependent Phage Induction, and Metabolic Studies

Author keywords

[No Author keywords available]

Indexed keywords

INFECTIONS; ZOONOTIC PATHOGENS;

EID: 2342525868     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.70.2.656-663.2004     Document Type: Article
Times cited : (33)

References (27)
  • 2
    • 0032311392 scopus 로고    scopus 로고
    • Bioenergetics of the obligate intracellular parasite Rickettsia prowazekii
    • Andersson, S. G. 1998. Bioenergetics of the obligate intracellular parasite Rickettsia prowazekii. Biochim. Biophys. Acta 1365:105-111.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 105-111
    • Andersson, S.G.1
  • 3
    • 0034101605 scopus 로고    scopus 로고
    • A bacteriophage-like particle from Bartonella bacilliformis
    • Barbian, K. D., and M. F. Minnick. 2000. A bacteriophage-like particle from Bartonella bacilliformis. Microbiology 146:599-609.
    • (2000) Microbiology , vol.146 , pp. 599-609
    • Barbian, K.D.1    Minnick, M.F.2
  • 5
    • 0030726675 scopus 로고    scopus 로고
    • A null mutation in the Bacillus subtilis aconitase gene causes a block in Spo0A-phosphate-dependent gene expression
    • Craig, J. E., M. J. Ford, D. C. Blaydon, and A. L. Sonenshein. 1997. A null mutation in the Bacillus subtilis aconitase gene causes a block in Spo0A-phosphate-dependent gene expression. J. Bacteriol. 179:7351-7359.
    • (1997) J. Bacteriol. , vol.179 , pp. 7351-7359
    • Craig, J.E.1    Ford, M.J.2    Blaydon, D.C.3    Sonenshein, A.L.4
  • 6
    • 0347492357 scopus 로고
    • Glutamate dehydrogenase
    • Doherty, D. 1971. Glutamate dehydrogenase. Methods Enzymol. 17:850-856.
    • (1971) Methods Enzymol. , vol.17 , pp. 850-856
    • Doherty, D.1
  • 7
    • 0021254146 scopus 로고
    • Synthesis of oxaloacetate in Bacillus subtilis mutants lacking the 2-ketoglutarate dehydrogenase enzymatic complex
    • Fisher, S. H., and B. Magasanik. 1984. Synthesis of oxaloacetate in Bacillus subtilis mutants lacking the 2-ketoglutarate dehydrogenase enzymatic complex. J. Bacteriol. 158:55-62.
    • (1984) J. Bacteriol. , vol.158 , pp. 55-62
    • Fisher, S.H.1    Magasanik, B.2
  • 8
    • 0036790117 scopus 로고    scopus 로고
    • Improved culture from lymph nodes of patients with cat scratch disease and genotypic characterization of Bartonella henselae isolates in Australia
    • Fournier, P. E., J. Robson, Z. Zeaiter, R. McDougall, S. Byrne, and D. Raoult. 2002. Improved culture from lymph nodes of patients with cat scratch disease and genotypic characterization of Bartonella henselae isolates in Australia. J. Clin. Microbiol. 40:3620-3624.
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 3620-3624
    • Fournier, P.E.1    Robson, J.2    Zeaiter, Z.3    McDougall, R.4    Byrne, S.5    Raoult, D.6
  • 10
    • 0008992879 scopus 로고
    • Metabolic activity of the trench fever rickettsia, Rickettsia quintana
    • Huang, K. Y. 1967. Metabolic activity of the trench fever rickettsia, Rickettsia quintana. J. Bacteriol. 93:853-859.
    • (1967) J. Bacteriol. , vol.93 , pp. 853-859
    • Huang, K.Y.1
  • 11
    • 0029843193 scopus 로고    scopus 로고
    • Will the real agent of cat-scratch disease please stand up?
    • Jerris, R. C., and R. L. Regnery. 1996. Will the real agent of cat-scratch disease please stand up? Annu. Rev. Microbiol. 50:707-725.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 707-725
    • Jerris, R.C.1    Regnery, R.L.2
  • 12
    • 0016145744 scopus 로고
    • Succinate dehydrogenase of Escherichia coli membrane vesicles. Activation and properties of the enzyme
    • Kasahara, M., and Y. Anraku. 1974. Succinate dehydrogenase of Escherichia coli membrane vesicles. Activation and properties of the enzyme. J. Biochem. (Tokyo) 76:959-966.
    • (1974) J. Biochem. (Tokyo) , vol.76 , pp. 959-966
    • Kasahara, M.1    Anraku, Y.2
  • 13
    • 77957014496 scopus 로고
    • Intra- and extramitochondrial malate dehydrogenases from chicken and tuna heart
    • Kitto, G. B. 1969. Intra- and extramitochondrial malate dehydrogenases from chicken and tuna heart. Methods Enzymol. 13:106-116.
    • (1969) Methods Enzymol. , vol.13 , pp. 106-116
    • Kitto, G.B.1
  • 14
    • 0021264085 scopus 로고
    • Isolation and characterization of outer membranes of Bacteroides thetaiotaomicron grown on different carbohydrates
    • Kotarski, S. F., and A. A. Salyers. 1984. Isolation and characterization of outer membranes of Bacteroides thetaiotaomicron grown on different carbohydrates. J. Bacteriol. 158:102-109.
    • (1984) J. Bacteriol. , vol.158 , pp. 102-109
    • Kotarski, S.F.1    Salyers, A.A.2
  • 15
    • 0020031005 scopus 로고
    • Phage influence on the synthesis of extracellular toxins in group A streptococci
    • Nida, S. K., and J. J. Ferretti. 1982. Phage influence on the synthesis of extracellular toxins in group A streptococci. Infect. Immun. 36:745-750.
    • (1982) Infect. Immun. , vol.36 , pp. 745-750
    • Nida, S.K.1    Ferretti, J.J.2
  • 16
    • 0029071645 scopus 로고
    • Differentiation of Bartonella-like isolates at the species level by PCR-restriction fragment length polymorphism in the citrate synthase gene
    • Norman, A. F., R. Regnery, P. Jameson, C. Greene, and D. C. Krause. 1995. Differentiation of Bartonella-like isolates at the species level by PCR-restriction fragment length polymorphism in the citrate synthase gene. J. Clin. Microbiol. 33:1797-1803.
    • (1995) J. Clin. Microbiol. , vol.33 , pp. 1797-1803
    • Norman, A.F.1    Regnery, R.2    Jameson, P.3    Greene, C.4    Krause, D.C.5
  • 18
    • 0001772669 scopus 로고
    • Histidine ammonia-lyase (Pseudomonas)
    • Rechler, M. M., and H. Tabor. 1970. Histidine ammonia-lyase (Pseudomonas). Methods Enzymol. 17:63-69.
    • (1970) Methods Enzymol. , vol.17 , pp. 63-69
    • Rechler, M.M.1    Tabor, H.2
  • 19
    • 0026500582 scopus 로고
    • Characterization of a novel Rochalimaea species, R. henselae sp. nov., isolated from blood of a febrile, human immunodeficiency virus-positive patient
    • Regnery, R. L., B. E. Anderson, J. E. Clarridge III, M. C. Rodriguez-Barradas, D. C. Jones, and J. H. Carr. 1992. Characterization of a novel Rochalimaea species, R. henselae sp. nov., isolated from blood of a febrile, human immunodeficiency virus-positive patient. J. Clin. Microbiol. 30:265-274.
    • (1992) J. Clin. Microbiol. , vol.30 , pp. 265-274
    • Regnery, R.L.1    Anderson, B.E.2    Clarridge III, J.E.3    Rodriguez-Barradas, M.C.4    Jones, D.C.5    Carr, J.H.6
  • 20
    • 0027325332 scopus 로고
    • Development and evaluation of a blood-free medium for determining growth curves and optimizing growth of Rochalimaea henselae
    • Schwartzman, W. A., C. A. Nesbit, and E. J. Baron. 1993. Development and evaluation of a blood-free medium for determining growth curves and optimizing growth of Rochalimaea henselae. J. Clin. Microbiol. 31:1882-1885.
    • (1993) J. Clin. Microbiol. , vol.31 , pp. 1882-1885
    • Schwartzman, W.A.1    Nesbit, C.A.2    Baron, E.J.3
  • 21
    • 77957010982 scopus 로고
    • Citrate synthase
    • Srere, P. A. 1969. Citrate synthase. Methods Enzymol. 13:3-11.
    • (1969) Methods Enzymol. , vol.13 , pp. 3-11
    • Srere, P.A.1
  • 23
    • 0017944085 scopus 로고
    • Vole agent identified as a strain of the trench fever Rickettsia, Rochalimaea quintana
    • Weiss, E., G. A. Dasch, D. R. Woodman, and J. C. Williams. 1978. Vole agent identified as a strain of the trench fever Rickettsia, Rochalimaea quintana. Infect. Immun. 19:1013-1020.
    • (1978) Infect. Immun. , vol.19 , pp. 1013-1020
    • Weiss, E.1    Dasch, G.A.2    Woodman, D.R.3    Williams, J.C.4
  • 24
    • 0026567310 scopus 로고
    • Rochalimaea henselae sp. nov., a cause of septicemia, bacillary angiomatosis, and parenchymal bacillary peliosis
    • Welch, D. F., D. A. Pickett, L. N. Slater, A. G. Steigerwalt, and D. J. Brenner. 1992. Rochalimaea henselae sp. nov., a cause of septicemia, bacillary angiomatosis, and parenchymal bacillary peliosis. J. Clin. Microbiol. 30:275-280.
    • (1992) J. Clin. Microbiol. , vol.30 , pp. 275-280
    • Welch, D.F.1    Pickett, D.A.2    Slater, L.N.3    Steigerwalt, A.G.4    Brenner, D.J.5
  • 25
    • 77957001185 scopus 로고
    • Assays of intermediates of the citric acid cycle and related compounds by flourometric enzyme methods
    • Williamson, J. R., and B. E. Corkey. 1969. Assays of intermediates of the citric acid cycle and related compounds by flourometric enzyme methods. Methods Enzymol. 13:434-513.
    • (1969) Methods Enzymol. , vol.13 , pp. 434-513
    • Williamson, J.R.1    Corkey, B.E.2
  • 26
    • 0028817148 scopus 로고
    • A chemically defined liquid medium that supports primary isolation of Rochalimaea (Bartonella) henselae from blood and tissue specimens
    • Wong, M. T., D. C. Thornton, R. C. Kennedy, and M. J. Dolan. 1995. A chemically defined liquid medium that supports primary isolation of Rochalimaea (Bartonella) henselae from blood and tissue specimens. J. Clin. Microbiol. 33:742-744.
    • (1995) J. Clin. Microbiol. , vol.33 , pp. 742-744
    • Wong, M.T.1    Thornton, D.C.2    Kennedy, R.C.3    Dolan, M.J.4
  • 27
    • 0034758223 scopus 로고    scopus 로고
    • Conformational change, aggregation and fibril formation induced by detergent treatments of cellular prion protein
    • Xiong, L. W., L. D. Raymond, S. F. Hayes, G. J. Raymond, and B. Caughey. 2001. Conformational change, aggregation and fibril formation induced by detergent treatments of cellular prion protein. J. Neurochem. 79:669-678.
    • (2001) J. Neurochem. , vol.79 , pp. 669-678
    • Xiong, L.W.1    Raymond, L.D.2    Hayes, S.F.3    Raymond, G.J.4    Caughey, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.