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Volumn 46, Issue 1, 2009, Pages 43-52

Lactic acid is a potential virulence factor for group B Streptococcus

Author keywords

Acidemia; Acidosis; Fetal; infection; Invasive; Lung; Neonate; Pathogen; pH; Rat; Respiratory; Streptococcus agalactiae; Virulence

Indexed keywords

LACTIC ACID; VIRULENCE FACTOR;

EID: 57949102991     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2008.10.009     Document Type: Article
Times cited : (14)

References (50)
  • 1
    • 0037738521 scopus 로고    scopus 로고
    • Group B streptococcal conjugate vaccines
    • Baker C.J., and Edwards M.S. Group B streptococcal conjugate vaccines. Arch Dis Child 88 (2003) 375-378
    • (2003) Arch Dis Child , vol.88 , pp. 375-378
    • Baker, C.J.1    Edwards, M.S.2
  • 3
    • 4744351583 scopus 로고    scopus 로고
    • Molecular pathogenesis of neonatal group B streptococcal infection: no longer in its infancy
    • Doran K.S., and Nizet V. Molecular pathogenesis of neonatal group B streptococcal infection: no longer in its infancy. Mol Microbiol 54 (2004) 23-31
    • (2004) Mol Microbiol , vol.54 , pp. 23-31
    • Doran, K.S.1    Nizet, V.2
  • 4
    • 0036854515 scopus 로고    scopus 로고
    • The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells
    • Bolduc G.R., Baron M.J., Gravekamp C., Lachenauer C.S., and Madoff L.C. The alpha C protein mediates internalization of group B Streptococcus within human cervical epithelial cells. Cell Microbiol 4 (2002) 751-758
    • (2002) Cell Microbiol , vol.4 , pp. 751-758
    • Bolduc, G.R.1    Baron, M.J.2    Gravekamp, C.3    Lachenauer, C.S.4    Madoff, L.C.5
  • 5
    • 2642576820 scopus 로고    scopus 로고
    • Alpha C protein of group B Streptococcus binds host cell surface glycosaminoglycan and enters cells by an actin-dependent mechanism
    • Baron M.J., Bolduc G.R., Goldberg M.B., Auperin T.C., and Madoff L.C. Alpha C protein of group B Streptococcus binds host cell surface glycosaminoglycan and enters cells by an actin-dependent mechanism. J Biol Chem 279 (2004) 24714-24723
    • (2004) J Biol Chem , vol.279 , pp. 24714-24723
    • Baron, M.J.1    Bolduc, G.R.2    Goldberg, M.B.3    Auperin, T.C.4    Madoff, L.C.5
  • 6
    • 34249856725 scopus 로고    scopus 로고
    • Identification of a glycosaminoglycan binding region of the alpha C protein that mediates entry of group B Streptococci into host cells
    • Baron M.J., Filman D.J., Prophete G.A., Hogle J.M., and Madoff L.C. Identification of a glycosaminoglycan binding region of the alpha C protein that mediates entry of group B Streptococci into host cells. J Biol Chem 282 (2007) 10526-10536
    • (2007) J Biol Chem , vol.282 , pp. 10526-10536
    • Baron, M.J.1    Filman, D.J.2    Prophete, G.A.3    Hogle, J.M.4    Madoff, L.C.5
  • 7
    • 37448998872 scopus 로고    scopus 로고
    • The group B streptococcal alpha C protein binds alpha1beta1-integrin through a novel KTD motif that promotes internalization of GBS within human epithelial cells
    • Bolduc G.R., and Madoff L.C. The group B streptococcal alpha C protein binds alpha1beta1-integrin through a novel KTD motif that promotes internalization of GBS within human epithelial cells. Microbiology 153 (2007) 4039-4049
    • (2007) Microbiology , vol.153 , pp. 4039-4049
    • Bolduc, G.R.1    Madoff, L.C.2
  • 8
    • 0345279861 scopus 로고    scopus 로고
    • The R28 protein of Streptococcus pyogenes is related to several group B streptococcal surface proteins, confers protective immunity and promotes binding to human epithelial cells
    • Stalhammar-Carlemalm M., Areschoug T., Larsson C., and Lindahl G. The R28 protein of Streptococcus pyogenes is related to several group B streptococcal surface proteins, confers protective immunity and promotes binding to human epithelial cells. Mol Microbiol 33 (1999) 208-219
    • (1999) Mol Microbiol , vol.33 , pp. 208-219
    • Stalhammar-Carlemalm, M.1    Areschoug, T.2    Larsson, C.3    Lindahl, G.4
  • 9
    • 0036428743 scopus 로고    scopus 로고
    • A fibrinogen receptor from group B Streptococcus interacts with fibrinogen by repetitive units with novel ligand binding sites
    • Schubert A., Zakikhany K., Schreiner M., Frank R., Spellerberg B., Eikmanns B.J., et al. A fibrinogen receptor from group B Streptococcus interacts with fibrinogen by repetitive units with novel ligand binding sites. Mol Microbiol 46 (2002) 557-569
    • (2002) Mol Microbiol , vol.46 , pp. 557-569
    • Schubert, A.1    Zakikhany, K.2    Schreiner, M.3    Frank, R.4    Spellerberg, B.5    Eikmanns, B.J.6
  • 10
    • 0030901174 scopus 로고    scopus 로고
    • A role for C5 and C5a-ase in the acute neutrophil response to group B streptococcal infections
    • Bohnsack J.F., Widjaja K., Ghazizadeh S., Rubens C.E., Hillyard D.R., Parker C.J., et al. A role for C5 and C5a-ase in the acute neutrophil response to group B streptococcal infections. J Infect Dis 175 (1997) 847-855
    • (1997) J Infect Dis , vol.175 , pp. 847-855
    • Bohnsack, J.F.1    Widjaja, K.2    Ghazizadeh, S.3    Rubens, C.E.4    Hillyard, D.R.5    Parker, C.J.6
  • 11
    • 2542558241 scopus 로고    scopus 로고
    • The novel fibrinogen-binding protein FbsB promotes Streptococcus agalactiae invasion into epithelial cells
    • Gutekunst H., Eikmanns B.J., and Reinscheid D.J. The novel fibrinogen-binding protein FbsB promotes Streptococcus agalactiae invasion into epithelial cells. Infect Immun 72 (2004) 3495-3504
    • (2004) Infect Immun , vol.72 , pp. 3495-3504
    • Gutekunst, H.1    Eikmanns, B.J.2    Reinscheid, D.J.3
  • 12
    • 21144455571 scopus 로고    scopus 로고
    • Sialylation of group B streptococcal capsular polysaccharide is mediated by cpsK and is required for optimal capsule polymerization and expression
    • Chaffin D.O., Mentele L.M., and Rubens C.E. Sialylation of group B streptococcal capsular polysaccharide is mediated by cpsK and is required for optimal capsule polymerization and expression. J Bacteriol 187 (2005) 4615-4626
    • (2005) J Bacteriol , vol.187 , pp. 4615-4626
    • Chaffin, D.O.1    Mentele, L.M.2    Rubens, C.E.3
  • 13
    • 12644274666 scopus 로고    scopus 로고
    • Inactivation of the alpha C protein antigen gene, bca, by a novel shuttle/suicide vector results in attenuation of virulence and immunity in group B Streptococcus
    • Li J., Kasper D.L., Ausubel F.M., Rosner B., and Michel J.L. Inactivation of the alpha C protein antigen gene, bca, by a novel shuttle/suicide vector results in attenuation of virulence and immunity in group B Streptococcus. Proc Natl Acad Sci USA 94 (1997) 13251-13256
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13251-13256
    • Li, J.1    Kasper, D.L.2    Ausubel, F.M.3    Rosner, B.4    Michel, J.L.5
  • 14
    • 5144229510 scopus 로고    scopus 로고
    • Sword and shield: linked group B streptococcal beta-hemolysin/cytolysin and carotenoid pigment function to subvert host phagocyte defense
    • Liu G.Y., Doran K.S., Lawrence T., Turkson N., Puliti M., Tissi L., et al. Sword and shield: linked group B streptococcal beta-hemolysin/cytolysin and carotenoid pigment function to subvert host phagocyte defense. Proc Natl Acad Sci USA 101 (2004) 14491-14496
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14491-14496
    • Liu, G.Y.1    Doran, K.S.2    Lawrence, T.3    Turkson, N.4    Puliti, M.5    Tissi, L.6
  • 15
    • 0035808397 scopus 로고    scopus 로고
    • Functional analysis in type Ia group B Streptococcus of a cluster of genes involved in extracellular polysaccharide production by diverse species of streptococci
    • Cieslewicz M.J., Kasper D.L., Wang Y., and Wessels M.R. Functional analysis in type Ia group B Streptococcus of a cluster of genes involved in extracellular polysaccharide production by diverse species of streptococci. J Biol Chem 276 (2001) 139-146
    • (2001) J Biol Chem , vol.276 , pp. 139-146
    • Cieslewicz, M.J.1    Kasper, D.L.2    Wang, Y.3    Wessels, M.R.4
  • 17
    • 53649084492 scopus 로고    scopus 로고
    • Molecular characterization of human-colonizing Streptococcus agalactiae strains isolated from throat, skin, anal margin and genital body sites
    • van der Mee-Marquet N., Fourny L., Arnault L., Domelier A.S., Salloum M., Lartigue M.F., et al. Molecular characterization of human-colonizing Streptococcus agalactiae strains isolated from throat, skin, anal margin and genital body sites. J Clin Microbiol 46 (2008) 2906-2911
    • (2008) J Clin Microbiol , vol.46 , pp. 2906-2911
    • van der Mee-Marquet, N.1    Fourny, L.2    Arnault, L.3    Domelier, A.S.4    Salloum, M.5    Lartigue, M.F.6
  • 18
    • 12844278673 scopus 로고    scopus 로고
    • Surface proteins of Streptococcus agalactiae and related proteins in other bacterial pathogens
    • Lindahl G., Stalhammar-Carlemalm M., and Areschoug T. Surface proteins of Streptococcus agalactiae and related proteins in other bacterial pathogens. Clin Microbiol Rev 18 (2005) 102-127
    • (2005) Clin Microbiol Rev , vol.18 , pp. 102-127
    • Lindahl, G.1    Stalhammar-Carlemalm, M.2    Areschoug, T.3
  • 20
    • 0014103776 scopus 로고
    • Aerobic metabolism of Streptococcus agalactiae
    • Mickelson M.N. Aerobic metabolism of Streptococcus agalactiae. J Bacteriol 94 (1967) 184-191
    • (1967) J Bacteriol , vol.94 , pp. 184-191
    • Mickelson, M.N.1
  • 21
    • 0019255882 scopus 로고
    • Cariogenic potential in vitro in man and in vivo in the rat of lactate dehydrogenase mutants of Streptococcus mutans
    • Johnson C.P., Gross S.M., and Hillman J.D. Cariogenic potential in vitro in man and in vivo in the rat of lactate dehydrogenase mutants of Streptococcus mutans. Arch Oral Biol 25 (1980) 707-713
    • (1980) Arch Oral Biol , vol.25 , pp. 707-713
    • Johnson, C.P.1    Gross, S.M.2    Hillman, J.D.3
  • 22
    • 0036693737 scopus 로고    scopus 로고
    • Genetically modified Streptococcus mutans for the prevention of dental caries
    • Hillman J.D. Genetically modified Streptococcus mutans for the prevention of dental caries. Antonie Van Leeuwenhoek 82 (2002) 361-366
    • (2002) Antonie Van Leeuwenhoek , vol.82 , pp. 361-366
    • Hillman, J.D.1
  • 23
    • 0017878110 scopus 로고
    • Growth and amino acid requirements of various strains of group B streptococci
    • Milligan T.W., Doran T.I., Straus D.C., and Mattingly S.J. Growth and amino acid requirements of various strains of group B streptococci. J Clin Microbiol 7 (1978) 28-33
    • (1978) J Clin Microbiol , vol.7 , pp. 28-33
    • Milligan, T.W.1    Doran, T.I.2    Straus, D.C.3    Mattingly, S.J.4
  • 24
    • 0030909642 scopus 로고    scopus 로고
    • Characterization of two distinct opsonic and protective epitopes within the alpha C protein of the group B Streptococcus
    • Kling D.E., Gravekamp C., Madoff L.C., and Michel J.L. Characterization of two distinct opsonic and protective epitopes within the alpha C protein of the group B Streptococcus. Infect Immun 65 (1997) 1462-1467
    • (1997) Infect Immun , vol.65 , pp. 1462-1467
    • Kling, D.E.1    Gravekamp, C.2    Madoff, L.C.3    Michel, J.L.4
  • 25
    • 0014429554 scopus 로고
    • Chemical characterization of d-lactate dehydrogenase from Escherichia coli B
    • Tarmy E.M., and Kaplan N.O. Chemical characterization of d-lactate dehydrogenase from Escherichia coli B. J Biol Chem 243 (1968) 2579-2586
    • (1968) J Biol Chem , vol.243 , pp. 2579-2586
    • Tarmy, E.M.1    Kaplan, N.O.2
  • 26
    • 0024485336 scopus 로고
    • Mutants of Escherichia coli deficient in the fermentative lactate dehydrogenase
    • Mat-Jan F., Alam K.Y., and Clark D.P. Mutants of Escherichia coli deficient in the fermentative lactate dehydrogenase. J Bacteriol 171 (1989) 342-348
    • (1989) J Bacteriol , vol.171 , pp. 342-348
    • Mat-Jan, F.1    Alam, K.Y.2    Clark, D.P.3
  • 27
    • 0017749210 scopus 로고
    • Glucose transport in Streptococcus agalactiae and its inhibition by lactoperoxidase-thiocyanate-hydrogen peroxide
    • Mickelson M.N. Glucose transport in Streptococcus agalactiae and its inhibition by lactoperoxidase-thiocyanate-hydrogen peroxide. J Bacteriol 132 (1977) 541-548
    • (1977) J Bacteriol , vol.132 , pp. 541-548
    • Mickelson, M.N.1
  • 28
    • 0015251749 scopus 로고
    • Glucose degradation, molar growth yields, and evidence for oxidative phosphorylation in Streptococcus agalactiae
    • Mickelson M.N. Glucose degradation, molar growth yields, and evidence for oxidative phosphorylation in Streptococcus agalactiae. J Bacteriol 109 (1972) 96-105
    • (1972) J Bacteriol , vol.109 , pp. 96-105
    • Mickelson, M.N.1
  • 29
    • 17144388984 scopus 로고    scopus 로고
    • Respiration metabolism of Group B Streptococcus is activated by environmental haem and quinone and contributes to virulence
    • Yamamoto Y., Poyart C., Trieu-Cuot P., Lamberet G., Gruss A., and Gaudu P. Respiration metabolism of Group B Streptococcus is activated by environmental haem and quinone and contributes to virulence. Mol Microbiol 56 (2005) 525-534
    • (2005) Mol Microbiol , vol.56 , pp. 525-534
    • Yamamoto, Y.1    Poyart, C.2    Trieu-Cuot, P.3    Lamberet, G.4    Gruss, A.5    Gaudu, P.6
  • 30
    • 0013956593 scopus 로고
    • Blood glucose concentration in the perinatal period
    • Russell G., and McKay E. Blood glucose concentration in the perinatal period. Arch Dis Child 41 (1966) 496-502
    • (1966) Arch Dis Child , vol.41 , pp. 496-502
    • Russell, G.1    McKay, E.2
  • 31
    • 0000280555 scopus 로고
    • Carbohydrate reserves in the newborn infant
    • Shelley H.J. Carbohydrate reserves in the newborn infant. Br Med J 1 (1964) 273-275
    • (1964) Br Med J , vol.1 , pp. 273-275
    • Shelley, H.J.1
  • 32
    • 0029383642 scopus 로고
    • Designer vaccines to prevent infections due to group B Streptococcus
    • Kasper D.L. Designer vaccines to prevent infections due to group B Streptococcus. Proc Assoc Am Physicians 107 (1995) 369-373
    • (1995) Proc Assoc Am Physicians , vol.107 , pp. 369-373
    • Kasper, D.L.1
  • 34
    • 0020367390 scopus 로고
    • Utilization of glycogen for phospholipid synthesis in fetal rat lung
    • Bourbon J.R., Rieutort M., Engle M.J., and Farrell P.M. Utilization of glycogen for phospholipid synthesis in fetal rat lung. Biochim Biophys Acta 712 (1982) 382-389
    • (1982) Biochim Biophys Acta , vol.712 , pp. 382-389
    • Bourbon, J.R.1    Rieutort, M.2    Engle, M.J.3    Farrell, P.M.4
  • 35
    • 0019966197 scopus 로고
    • Delay in pulmonary glycogen degradation in fetuses of streptozotocin diabetic rats
    • Gewolb I.H., Barrett C., Wilson C.M., and Warshaw J.B. Delay in pulmonary glycogen degradation in fetuses of streptozotocin diabetic rats. Pediatr Res 16 (1982) 869-873
    • (1982) Pediatr Res , vol.16 , pp. 869-873
    • Gewolb, I.H.1    Barrett, C.2    Wilson, C.M.3    Warshaw, J.B.4
  • 36
    • 0034817210 scopus 로고    scopus 로고
    • Origins of vaginal acidity: high D/L lactate ratio is consistent with bacteria being the primary source
    • Boskey E.R., Cone R.A., Whaley K.J., and Moench T.R. Origins of vaginal acidity: high D/L lactate ratio is consistent with bacteria being the primary source. Hum Reprod 16 (2001) 1809-1813
    • (2001) Hum Reprod , vol.16 , pp. 1809-1813
    • Boskey, E.R.1    Cone, R.A.2    Whaley, K.J.3    Moench, T.R.4
  • 37
    • 0032879164 scopus 로고    scopus 로고
    • Acid production by vaginal flora in vitro is consistent with the rate and extent of vaginal acidification
    • Boskey E.R., Telsch K.M., Whaley K.J., Moench T.R., and Cone R.A. Acid production by vaginal flora in vitro is consistent with the rate and extent of vaginal acidification. Infect Immun 67 (1999) 5170-5175
    • (1999) Infect Immun , vol.67 , pp. 5170-5175
    • Boskey, E.R.1    Telsch, K.M.2    Whaley, K.J.3    Moench, T.R.4    Cone, R.A.5
  • 38
    • 12344312035 scopus 로고    scopus 로고
    • Estrogen acidifies vaginal pH by up-regulation of proton secretion via the apical membrane of vaginal-ectocervical epithelial cells
    • Gorodeski G.I., Hopfer U., Liu C.C., and Margles E. Estrogen acidifies vaginal pH by up-regulation of proton secretion via the apical membrane of vaginal-ectocervical epithelial cells. Endocrinology 146 (2005) 816-824
    • (2005) Endocrinology , vol.146 , pp. 816-824
    • Gorodeski, G.I.1    Hopfer, U.2    Liu, C.C.3    Margles, E.4
  • 39
    • 0033955403 scopus 로고    scopus 로고
    • Construction and characterization of an effector strain of Streptococcus mutans for replacement therapy of dental caries
    • Hillman J.D., Brooks T.A., Michalek S.M., Harmon C.C., Snoep J.L., and van Der Weijden C.C. Construction and characterization of an effector strain of Streptococcus mutans for replacement therapy of dental caries. Infect Immun 68 (2000) 543-549
    • (2000) Infect Immun , vol.68 , pp. 543-549
    • Hillman, J.D.1    Brooks, T.A.2    Michalek, S.M.3    Harmon, C.C.4    Snoep, J.L.5    van Der Weijden, C.C.6
  • 40
    • 0028235911 scopus 로고
    • Adherence of group B streptococci to cultured epithelial cells: roles of environmental factors and bacterial surface components
    • Tamura G.S., Kuypers J.M., Smith S., Raff H., and Rubens C.E. Adherence of group B streptococci to cultured epithelial cells: roles of environmental factors and bacterial surface components. Infect Immun 62 (1994) 2450-2458
    • (1994) Infect Immun , vol.62 , pp. 2450-2458
    • Tamura, G.S.1    Kuypers, J.M.2    Smith, S.3    Raff, H.4    Rubens, C.E.5
  • 41
    • 0037341048 scopus 로고    scopus 로고
    • Early pregnancy threshold vaginal pH and Gram stain scores predictive of subsequent preterm birth in asymptomatic women
    • Hauth J.C., Macpherson C., Carey J.C., Klebanoff M.A., Hillier S.L., Ernest J.M., et al. Early pregnancy threshold vaginal pH and Gram stain scores predictive of subsequent preterm birth in asymptomatic women. Am J Obstet Gynecol 188 (2003) 831-835
    • (2003) Am J Obstet Gynecol , vol.188 , pp. 831-835
    • Hauth, J.C.1    Macpherson, C.2    Carey, J.C.3    Klebanoff, M.A.4    Hillier, S.L.5    Ernest, J.M.6
  • 42
    • 0033019732 scopus 로고    scopus 로고
    • Subcellular fractionation of group B Streptococcus
    • 28
    • Kling D.E., Madoff L.C., and Michel J.L. Subcellular fractionation of group B Streptococcus. Biotechniques 27 (1999) 24-26 28
    • (1999) Biotechniques , vol.27 , pp. 24-26
    • Kling, D.E.1    Madoff, L.C.2    Michel, J.L.3
  • 44
    • 0029736810 scopus 로고    scopus 로고
    • Variation in repeat number within the alpha C protein of group B Streptococcus alters antigenicity and protective epitopes
    • Gravekamp C., Horensky D.S., Michel J.L., and Madoff L.C. Variation in repeat number within the alpha C protein of group B Streptococcus alters antigenicity and protective epitopes. Infect Immun 64 (1996) 3576
    • (1996) Infect Immun , vol.64 , pp. 3576
    • Gravekamp, C.1    Horensky, D.S.2    Michel, J.L.3    Madoff, L.C.4
  • 45
    • 35148826082 scopus 로고    scopus 로고
    • Interaction with human plasminogen system turns on proteolytic activity in Streptococcus agalactiae and enhances its virulence in a mouse model
    • Magalhaes V., Veiga-Malta I., Almeida M.R., Baptista M., Ribeiro A., Trieu-Cuot P., et al. Interaction with human plasminogen system turns on proteolytic activity in Streptococcus agalactiae and enhances its virulence in a mouse model. Microbes Infect 9 (2007) 1276-1284
    • (2007) Microbes Infect , vol.9 , pp. 1276-1284
    • Magalhaes, V.1    Veiga-Malta, I.2    Almeida, M.R.3    Baptista, M.4    Ribeiro, A.5    Trieu-Cuot, P.6
  • 47
    • 26244459662 scopus 로고    scopus 로고
    • Glycoconjugates of choroidal neovascular membranes in age-related macular degeneration
    • Mullins R.F., Grassi M.A., and Skeie J.M. Glycoconjugates of choroidal neovascular membranes in age-related macular degeneration. Mol Vis 11 (2005) 509-517
    • (2005) Mol Vis , vol.11 , pp. 509-517
    • Mullins, R.F.1    Grassi, M.A.2    Skeie, J.M.3


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