메뉴 건너뛰기




Volumn 4, Issue 4, 2009, Pages

Inactivation of DltA modulates virulence factor expression in Streptococcus pyogenes

Author keywords

[No Author keywords available]

Indexed keywords

AEROBIC RESPIRATION CONTROL PROTEIN A; ALANINE; BACTERIAL PROTEIN; CATABOLITE CONTROL PROTEIN A; LIPOTEICHOIC ACID; M PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN EMM; PROTEIN RGG; PROTEIN ROFA; PROTEIN SIC; UNCLASSIFIED DRUG; VIRULENCE FACTOR; ALANYL LIPOTEICHOIC ACID; ALANYL-LIPOTEICHOIC ACID; BACTERIAL ANTIGEN; BACTERIAL DNA; CARRIER PROTEIN; OUTER MEMBRANE PROTEIN; PRIMER DNA; STREPTOCOCCAL M PROTEIN; TEICHOIC ACID;

EID: 65549098067     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0005366     Document Type: Article
Times cited : (35)

References (65)
  • 1
    • 0347479228 scopus 로고    scopus 로고
    • A continuum of anionic charge: Structures and functions of D-alanyl-teichoic acids in gram-positive bacteria
    • Neuhaus FC, Baddiley J (2003) A continuum of anionic charge: Structures and functions of D-alanyl-teichoic acids in gram-positive bacteria. Microbiol Mol Biol Rev 67: 686-723.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 686-723
    • Neuhaus, F.C.1    Baddiley, J.2
  • 2
    • 34347269622 scopus 로고    scopus 로고
    • Synthesis of glycerol phosphate lipoteichoic acid in Staphylococcus aureus
    • Gründling A, Schneewind O (2007) Synthesis of glycerol phosphate lipoteichoic acid in Staphylococcus aureus. Proc Natl Acad Sci U S A 104: 8478-8483.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 8478-8483
    • Gründling, A.1    Schneewind, O.2
  • 3
    • 0028982844 scopus 로고
    • Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation
    • Perego M, Glaser P, Minutello A, Strauch MA, Leopold K, et al. (1995) Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation. J Biol Chem 270: 15598-15606.
    • (1995) J Biol Chem , vol.270 , pp. 15598-15606
    • Perego, M.1    Glaser, P.2    Minutello, A.3    Strauch, M.A.4    Leopold, K.5
  • 4
    • 0033605557 scopus 로고    scopus 로고
    • Inactivaton of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel A, Otto M, Jack RW, Kalbacher H, Jung G, et al. (1999) Inactivaton of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J Biol Chem 274: 8405-8410.
    • (1999) J Biol Chem , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5
  • 5
    • 0015926870 scopus 로고
    • The alanine ester content and magnesium binding capacity of walls of Staphylococcus aureus H grown at different pH values
    • Archibald AR, Baddiley J, Heptinstall S (1973) The alanine ester content and magnesium binding capacity of walls of Staphylococcus aureus H grown at different pH values. Biochim Biophys Acta 291: 629-634.
    • (1973) Biochim Biophys Acta , vol.291 , pp. 629-634
    • Archibald, A.R.1    Baddiley, J.2    Heptinstall, S.3
  • 6
    • 0036192372 scopus 로고    scopus 로고
    • Formation of D-alanyl-lipoteichoic acid is required for adhesion and virulence of Listeria monocytogenes
    • Abachin E, Poyart C, Pelligrini E, Milohanic E, Fiedler F, et al. (2002) Formation of D-alanyl-lipoteichoic acid is required for adhesion and virulence of Listeria monocytogenes. Mol Microbiol 43: 1-14.
    • (2002) Mol Microbiol , vol.43 , pp. 1-14
    • Abachin, E.1    Poyart, C.2    Pelligrini, E.3    Milohanic, E.4    Fiedler, F.5
  • 7
    • 0033763124 scopus 로고    scopus 로고
    • Defects in D-alanyl-lipoteichoic acid synthesis in Streptococcus mutans result in acid sensitivity
    • Boyd DA, Cvitkovitch DG, Bleiweis AS, Kiriukhin MY, Debabov DV, et al. (2000) Defects in D-alanyl-lipoteichoic acid synthesis in Streptococcus mutans result in acid sensitivity. J Bacteriol 182: 6055-6065.
    • (2000) J Bacteriol , vol.182 , pp. 6055-6065
    • Boyd, D.A.1    Cvitkovitch, D.G.2    Bleiweis, A.S.3    Kiriukhin, M.Y.4    Debabov, D.V.5
  • 8
    • 0038817866 scopus 로고    scopus 로고
    • Enhanced secretion of heterologous cyclodextrin glycosyltransferase by a mutant of Bacillus licheniformis defective in the D-alanylation of teichoic acids
    • Craynest M, Jørgensen S, Sarvas M, Kontinen VP (2003) Enhanced secretion of heterologous cyclodextrin glycosyltransferase by a mutant of Bacillus licheniformis defective in the D-alanylation of teichoic acids. Lett Appl Microbiol 37: 75-80.
    • (2003) Lett Appl Microbiol , vol.37 , pp. 75-80
    • Craynest, M.1    Jørgensen, S.2    Sarvas, M.3    Kontinen, V.P.4
  • 9
    • 0035059332 scopus 로고    scopus 로고
    • Key role of teichoic acid net charge in Stapylococcus aureus colonization of artificial surfaces
    • Gross M, Cramton SE, Götz F, Peschel A (2001) Key role of teichoic acid net charge in Stapylococcus aureus colonization of artificial surfaces. Infect Immun 69: 3423-3426.
    • (2001) Infect Immun , vol.69 , pp. 3423-3426
    • Gross, M.1    Cramton, S.E.2    Götz, F.3    Peschel, A.4
  • 10
    • 33645786299 scopus 로고    scopus 로고
    • Effect of D-alanylatioin of (lipo)teichoic acids of Staphylococcus aureus on host secretory phospholipase A2 action before and after phagocytosis by human neutrophils
    • Hunt CL, Nauseef WM, Weiss JP (2006) Effect of D-alanylatioin of (lipo)teichoic acids of Staphylococcus aureus on host secretory phospholipase A2 action before and after phagocytosis by human neutrophils. J Immunol 176: 4987-4994.
    • (2006) J Immunol , vol.176 , pp. 4987-4994
    • Hunt, C.L.1    Nauseef, W.M.2    Weiss, J.P.3
  • 11
    • 0034282698 scopus 로고    scopus 로고
    • D-alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis
    • Hyyryläinen H-L, Vitikainen M, Thwaite J, Wu H, Sarvas M, et al. (2000) D-alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis. J Biol Chem 275: 26696-26703.
    • (2000) J Biol Chem , vol.275 , pp. 26696-26703
    • Hyyryläinen, H.-L.1    Vitikainen, M.2    Thwaite, J.3    Wu, H.4    Sarvas, M.5
  • 12
    • 33748670479 scopus 로고    scopus 로고
    • A functional dlt operon, encoding proteins required for incorporation of D-alanine in teichoic acids in gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus pneumoniae
    • Kovács M, Halfmann A, Fedtke I, Heintz M, Peschel A, et al. (2006) A functional dlt operon, encoding proteins required for incorporation of D-alanine in teichoic acids in gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus pneumoniae. J Bacteriol 188: 5797-5805.
    • (2006) J Bacteriol , vol.188 , pp. 5797-5805
    • Kovács, M.1    Halfmann, A.2    Fedtke, I.3    Heintz, M.4    Peschel, A.5
  • 13
    • 25144519572 scopus 로고    scopus 로고
    • D-alanylation of teichoic acids promotes group A Streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion
    • Kristian SA, Datta V, Weidenmaier C, Kansal R, Fedtke I, et al. (2005) D-alanylation of teichoic acids promotes group A Streptococcus antimicrobial peptide resistance, neutrophil survival, and epithelial cell invasion. J Bacteriol 187: 6719-6725.
    • (2005) J Bacteriol , vol.187 , pp. 6719-6725
    • Kristian, S.A.1    Datta, V.2    Weidenmaier, C.3    Kansal, R.4    Fedtke, I.5
  • 14
    • 1642312955 scopus 로고    scopus 로고
    • Influence of lipoteichoic adid D-alanylation on protein secretion in Lactococcus lactis as revealed by random mutagenesis
    • Nouaille S, Commissaire J, Gratadoux JJ, Ravn P, Bolotin A, et al. (2004) Influence of lipoteichoic adid D-alanylation on protein secretion in Lactococcus lactis as revealed by random mutagenesis. Appl Environ Microbiol 70: 1600-1607.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 1600-1607
    • Nouaille, S.1    Commissaire, J.2    Gratadoux, J.J.3    Ravn, P.4    Bolotin, A.5
  • 15
    • 33646574610 scopus 로고    scopus 로고
    • D-alanyl ester depletion of teichoic acids in Lactobacillus plantarum results in a major modification of lipoteichoic acid composition and cell wall perforations at the septum mediated by the Acm2 autolysin
    • Palumbo E, Deghorain M, Cocconcelli PS, Kleerebezem M, Geyer A, et al. (2006) D-alanyl ester depletion of teichoic acids in Lactobacillus plantarum results in a major modification of lipoteichoic acid composition and cell wall perforations at the septum mediated by the Acm2 autolysin. J Bacteriol 188: 3709-3715.
    • (2006) J Bacteriol , vol.188 , pp. 3709-3715
    • Palumbo, E.1    Deghorain, M.2    Cocconcelli, P.S.3    Kleerebezem, M.4    Geyer, A.5
  • 16
    • 0033806585 scopus 로고    scopus 로고
    • The D-alanine residues of Staphylococcus aureus teichoic acids alter the susceptibility to vancomycin and the activity of autolysins
    • Peschel A, Vuong C, Otto M, Götz F (2000) The D-alanine residues of Staphylococcus aureus teichoic acids alter the susceptibility to vancomycin and the activity of autolysins. Antimicrob Agents Chemother 44: 2845-2847.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 2845-2847
    • Peschel, A.1    Vuong, C.2    Otto, M.3    Götz, F.4
  • 17
    • 0001558367 scopus 로고
    • Differentiation of group A streptococci with a common R antigen into three serological types, with special reference to the bactericidal test
    • Lancefield RC (1957) Differentiation of group A streptococci with a common R antigen into three serological types, with special reference to the bactericidal test. J Exp Med 106: 525-544.
    • (1957) J Exp Med , vol.106 , pp. 525-544
    • Lancefield, R.C.1
  • 18
    • 0025077034 scopus 로고
    • Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci
    • Fischetti VA, Pancholi V, Schneewind O (1990) Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol Microbiol 4: 1603-1605.
    • (1990) Mol Microbiol , vol.4 , pp. 1603-1605
    • Fischetti, V.A.1    Pancholi, V.2    Schneewind, O.3
  • 19
    • 0023571164 scopus 로고
    • Identification of a gene that regulates expression of M protein, the major virulence determinant of group A streptococci
    • Caparon MG, Scott JR (1987) Identification of a gene that regulates expression of M protein, the major virulence determinant of group A streptococci. Proc Natl Acad Sci U S A 84: 8677-8681.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 8677-8681
    • Caparon, M.G.1    Scott, J.R.2
  • 20
    • 0026808610 scopus 로고
    • Environmental regulation of virulence in group A streptococci: Transcription of the gene encoding M protein is stimulated by carbon dioxide
    • Caparon MG, Geist RT, Perez-Casal J, Scott JR (1992) Environmental regulation of virulence in group A streptococci: transcription of the gene encoding M protein is stimulated by carbon dioxide. J Bacteriol 174: 5693-5701.
    • (1992) J Bacteriol , vol.174 , pp. 5693-5701
    • Caparon, M.G.1    Geist, R.T.2    Perez-Casal, J.3    Scott, J.R.4
  • 21
    • 0028867355 scopus 로고
    • Regulation of virulence by environmental signals in group A streptococci: Influence of osmolarity, temperature, gas exchange, and iron limitation on emm transcription
    • McIver KS, Heath AS, Scott JR (1995) Regulation of virulence by environmental signals in group A streptococci: influence of osmolarity, temperature, gas exchange, and iron limitation on emm transcription. Infect Immun 63: 4540-4542.
    • (1995) Infect Immun , vol.63 , pp. 4540-4542
    • McIver, K.S.1    Heath, A.S.2    Scott, J.R.3
  • 22
    • 0030753825 scopus 로고    scopus 로고
    • Role of mga in growth phase regulation of virulence genes of the group A streptococcus
    • McIver KS, Scott JR (1997) Role of mga in growth phase regulation of virulence genes of the group A streptococcus. J Bacteriol 179: 5178-5187.
    • (1997) J Bacteriol , vol.179 , pp. 5178-5187
    • McIver, K.S.1    Scott, J.R.2
  • 23
    • 0030976402 scopus 로고    scopus 로고
    • Conversion of M serotype 24 of Streptococcus pyogenes to M serotypes 5 and 18: Effect on resistance to phagocytosis and adhesion to host cells
    • Courtney HS, Liu S, Dale JB, Hasty DL (1997) Conversion of M serotype 24 of Streptococcus pyogenes to M serotypes 5 and 18: Effect on resistance to phagocytosis and adhesion to host cells. Infect Immun 65: 2472-2474.
    • (1997) Infect Immun , vol.65 , pp. 2472-2474
    • Courtney, H.S.1    Liu, S.2    Dale, J.B.3    Hasty, D.L.4
  • 24
    • 0343017792 scopus 로고
    • Antiphagocytic activity of streptococcal M protein: Selective binding of complement control protein factor H
    • Horstmann RD, Sievertsen HJ, Knobloch J, Fischetti VA (1988) Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H. Proc Natl Acad Sci U S A 85: 1657-1661.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 1657-1661
    • Horstmann, R.D.1    Sievertsen, H.J.2    Knobloch, J.3    Fischetti, V.A.4
  • 25
    • 0026472541 scopus 로고
    • Role of fibrinogen in complement inhibition by streptococcal M protein
    • Horstmann RD, Sievertsen HJ, Leippe M, Fischetti VA (1992) Role of fibrinogen in complement inhibition by streptococcal M protein. Infect Immun 60: 5036-5041.
    • (1992) Infect Immun , vol.60 , pp. 5036-5041
    • Horstmann, R.D.1    Sievertsen, H.J.2    Leippe, M.3    Fischetti, V.A.4
  • 26
    • 0020052104 scopus 로고
    • Antiopsonic activity of fibrinogen bound to M protein on the surface of group A streptococci
    • Whitnack E, Beachey EH (1982) Antiopsonic activity of fibrinogen bound to M protein on the surface of group A streptococci. J Clin Invest 69: 1042.
    • (1982) J Clin Invest , vol.69 , pp. 1042
    • Whitnack, E.1    Beachey, E.H.2
  • 27
    • 33745625880 scopus 로고    scopus 로고
    • Alanine esters of enterococcal lipoteichoic acid play a role in biofilm formation and resistance to antimicrobial peptides
    • Fabretti F, Theilacker C, Baldassarri L, Kaczynski Z, Kropec A, et al. (2006) Alanine esters of enterococcal lipoteichoic acid play a role in biofilm formation and resistance to antimicrobial peptides. Infect Immun 74: 4164-4171.
    • (2006) Infect Immun , vol.74 , pp. 4164-4171
    • Fabretti, F.1    Theilacker, C.2    Baldassarri, L.3    Kaczynski, Z.4    Kropec, A.5
  • 28
    • 0034033679 scopus 로고    scopus 로고
    • Genetic relatedness and superantigen expression of M type 1 group A streptococcal isolates from severe and nonsevere invasive disease
    • Chatellier S, Ihendyane N, Kansal RG, Khambaty F, Basma H, et al. (2000) Genetic relatedness and superantigen expression of M type 1 group A streptococcal isolates from severe and nonsevere invasive disease. Infect Immun 68: 3523-3534.
    • (2000) Infect Immun , vol.68 , pp. 3523-3534
    • Chatellier, S.1    Ihendyane, N.2    Kansal, R.G.3    Khambaty, F.4    Basma, H.5
  • 29
    • 0037315055 scopus 로고    scopus 로고
    • Molecular genetic analysis of a group A Streptococcus operon encoding serum opacity factor and a novel fibronectin-binding protein, SfbX
    • Jeng A, Sakota V, Li Z, Datta V, Beall B, et al. (2003) Molecular genetic analysis of a group A Streptococcus operon encoding serum opacity factor and a novel fibronectin-binding protein, SfbX. J Bacteriol 185: 1208-1217.
    • (2003) J Bacteriol , vol.185 , pp. 1208-1217
    • Jeng, A.1    Sakota, V.2    Li, Z.3    Datta, V.4    Beall, B.5
  • 30
    • 33645975827 scopus 로고    scopus 로고
    • Monocyte and macrophage activation by lipoteichoic acid is independent of alanine and is potentiated by hemoglobin
    • Hasty DL, Meron-Sudai S, Cox KH, Nagorna T, Ruiz-Bustos E, et al. (2006) Monocyte and macrophage activation by lipoteichoic acid is independent of alanine and is potentiated by hemoglobin. J Immunol 176: 5567-5576.
    • (2006) J Immunol , vol.176 , pp. 5567-5576
    • Hasty, D.L.1    Meron-Sudai, S.2    Cox, K.H.3    Nagorna, T.4    Ruiz-Bustos, E.5
  • 31
    • 0030027865 scopus 로고    scopus 로고
    • Efficient insertional mutagenesis in lactococci and other Gram-positive bacteria
    • Maguin E, Prévost H, Ehrlich SD, Gruss A (1996) Efficient insertional mutagenesis in lactococci and other Gram-positive bacteria. J Bacteriol 178: 931-935.
    • (1996) J Bacteriol , vol.178 , pp. 931-935
    • Maguin, E.1    Prévost, H.2    Ehrlich, S.D.3    Gruss, A.4
  • 32
    • 0023271951 scopus 로고
    • Sequence and type-specific immunogenicity of the amino-terminal region of type 1 streptococcal M protein
    • Kraus W, Haanes-Fritz E, Cleary PP, Seyer JM, Dale JB, et al. (1987) Sequence and type-specific immunogenicity of the amino-terminal region of type 1 streptococcal M protein. J Immunol 139: 3084-3090.
    • (1987) J Immunol , vol.139 , pp. 3084-3090
    • Kraus, W.1    Haanes-Fritz, E.2    Cleary, P.P.3    Seyer, J.M.4    Dale, J.B.5
  • 33
    • 85025390197 scopus 로고
    • The antigenic complex of Streptococcus haemolyticus. I. Demonstration of a type-specific substance in extracts of Streptococcus haemolyticus
    • Lancefield RC (1928) The antigenic complex of Streptococcus haemolyticus. I. Demonstration of a type-specific substance in extracts of Streptococcus haemolyticus. J Exp Med 47: 91-103.
    • (1928) J Exp Med , vol.47 , pp. 91-103
    • Lancefield, R.C.1
  • 34
    • 0034778929 scopus 로고    scopus 로고
    • Generation and surface localization of intact M protein in Streptococcus pyogenes are dependent on sagA
    • Biswas I, Germon P, McDade K, Scott JR (2001) Generation and surface localization of intact M protein in Streptococcus pyogenes are dependent on sagA. Infect Immun 69: 7029-7038.
    • (2001) Infect Immun , vol.69 , pp. 7029-7038
    • Biswas, I.1    Germon, P.2    McDade, K.3    Scott, J.R.4
  • 35
    • 0034926023 scopus 로고    scopus 로고
    • Reciprocal, temporal expression of SpeA and SpeB by invasive isolates of group A streptococcal isolates in vivo
    • Kazmi SU, Kansal R, Aziz RK, Hooshdaran M, Norrby-Teglund A, et al. (2001) Reciprocal, temporal expression of SpeA and SpeB by invasive isolates of group A streptococcal isolates in vivo. Infect Immun 69: 4988-4995.
    • (2001) Infect Immun , vol.69 , pp. 4988-4995
    • Kazmi, S.U.1    Kansal, R.2    Aziz, R.K.3    Hooshdaran, M.4    Norrby-Teglund, A.5
  • 36
    • 33645776051 scopus 로고    scopus 로고
    • Genomewide analysis of group A streptococci reveals a mutation that modulates global phenotype and disease specificity
    • Sumby P, Whitney AR, Graviss EA, DeLeo FR, Musser JM (2006) Genomewide analysis of group A streptococci reveals a mutation that modulates global phenotype and disease specificity. PLoS Pathogens 2: 41-49.
    • (2006) PLoS Pathogens , vol.2 , pp. 41-49
    • Sumby, P.1    Whitney, A.R.2    Graviss, E.A.3    DeLeo, F.R.4    Musser, J.M.5
  • 37
    • 34547693093 scopus 로고    scopus 로고
    • DNase Sda1 provides selection pressure for a switch to invasive group A streptococcal infection
    • Walker MJ, Hollands A, Sanderson-Smith ML, Cole JN, Kirk K, et al. (2007) DNase Sda1 provides selection pressure for a switch to invasive group A streptococcal infection. Nat Med 13: 981-985.
    • (2007) Nat Med , vol.13 , pp. 981-985
    • Walker, M.J.1    Hollands, A.2    Sanderson-Smith, M.L.3    Cole, J.N.4    Kirk, K.5
  • 38
    • 0032932438 scopus 로고    scopus 로고
    • Insertional inactivation of genes responsible for the D-alanylation of lipoteichoic acid in Streptococcus gordonii DL1 (Challis) affects intrageneric coaggregations
    • Clemans DL, Kolenbrander PE, Debabov DV, Zhang Q, Lunsford RD, et al. (1999) Insertional inactivation of genes responsible for the D-alanylation of lipoteichoic acid in Streptococcus gordonii DL1 (Challis) affects intrageneric coaggregations. Infect Immun 67: 2464-2474.
    • (1999) Infect Immun , vol.67 , pp. 2464-2474
    • Clemans, D.L.1    Kolenbrander, P.E.2    Debabov, D.V.3    Zhang, Q.4    Lunsford, R.D.5
  • 40
    • 0036135303 scopus 로고    scopus 로고
    • Optimization of the cell wall microenvironment allows increased production of recombinant Bacillus anthracis protective antigen from B. subtilis
    • Thwaite JE, Baillie LW, Carter NM, Stephenson K, Rees M, et al. (2002) Optimization of the cell wall microenvironment allows increased production of recombinant Bacillus anthracis protective antigen from B. subtilis. Appl Environ Microbiol 68: 227-234.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 227-234
    • Thwaite, J.E.1    Baillie, L.W.2    Carter, N.M.3    Stephenson, K.4    Rees, M.5
  • 41
    • 0030067110 scopus 로고    scopus 로고
    • Protein SIC, a novel extracellular protein of Streptococcus pyogenes interfering with complement function
    • Akesson P, Sjöholm AG, Björck L (1996) Protein SIC, a novel extracellular protein of Streptococcus pyogenes interfering with complement function. J Biol Chem 271: 1081-1088.
    • (1996) J Biol Chem , vol.271 , pp. 1081-1088
    • Akesson, P.1    Sjöholm, A.G.2    Björck, L.3
  • 42
    • 0033043749 scopus 로고    scopus 로고
    • Streptococcus pyogenes strains containing emm12 and emm55 possess a novel gene coding for distantly related SIC protein
    • Hartas J, Sriprakash KS (1999) Streptococcus pyogenes strains containing emm12 and emm55 possess a novel gene coding for distantly related SIC protein. Microb Pathog 26: 25-33.
    • (1999) Microb Pathog , vol.26 , pp. 25-33
    • Hartas, J.1    Sriprakash, K.S.2
  • 43
    • 36148948693 scopus 로고    scopus 로고
    • The catabolite control protein CcpA binds to Pmga and influences expression of the virulence regulator Mga in the group A streptococcus
    • Almengor AC, Kinkel TL, Day SJ, McIver KS (2007) The catabolite control protein CcpA binds to Pmga and influences expression of the virulence regulator Mga in the group A streptococcus. J Bacteriol 189: 8405-8416.
    • (2007) J Bacteriol , vol.189 , pp. 8405-8416
    • Almengor, A.C.1    Kinkel, T.L.2    Day, S.J.3    McIver, K.S.4
  • 44
    • 0037674820 scopus 로고    scopus 로고
    • Virulence factor regulation and regulatory networks in Streptococcus pyogenes and their impact on pathogen-host interactions
    • Kreikemeyer B, McIver KS, Podbielski A (2003) Virulence factor regulation and regulatory networks in Streptococcus pyogenes and their impact on pathogen-host interactions. Trends Microbiol 11: 3857-3865.
    • (2003) Trends Microbiol , vol.11 , pp. 3857-3865
    • Kreikemeyer, B.1    McIver, K.S.2    Podbielski, A.3
  • 45
    • 0033041979 scopus 로고    scopus 로고
    • The rgg gene of Streptococcus pyogenes NZ131 positively influences extracellular SPE B production
    • Chaussee MS, Ajdic D, Ferretti JJ (1999) The rgg gene of Streptococcus pyogenes NZ131 positively influences extracellular SPE B production. Infect Immun 67: 1715-1722.
    • (1999) Infect Immun , vol.67 , pp. 1715-1722
    • Chaussee, M.S.1    Ajdic, D.2    Ferretti, J.J.3
  • 46
    • 33646558556 scopus 로고    scopus 로고
    • Cation-induced transcriptional regulation of the dlt operon of Staphylococcus aureus
    • Koprivnjak T, Mlakar V, Swanson L, Fournier B, Peschel A, et al. (2006) Cation-induced transcriptional regulation of the dlt operon of Staphylococcus aureus. J Bacteriol 188: 3622-3630.
    • (2006) J Bacteriol , vol.188 , pp. 3622-3630
    • Koprivnjak, T.1    Mlakar, V.2    Swanson, L.3    Fournier, B.4    Peschel, A.5
  • 48
    • 11144322172 scopus 로고    scopus 로고
    • Autolysis of Lactococcus lactis is increased upon D-alanine depletion of peptidoglycan and lipoteichoic acids
    • Steen A, Palumbo E, Deghorain M, Cocconcelli PS, Delcour J, et al. (2005) Autolysis of Lactococcus lactis is increased upon D-alanine depletion of peptidoglycan and lipoteichoic acids. J Bacteriol 187: 114-124.
    • (2005) J Bacteriol , vol.187 , pp. 114-124
    • Steen, A.1    Palumbo, E.2    Deghorain, M.3    Cocconcelli, P.S.4    Delcour, J.5
  • 49
    • 21344450057 scopus 로고    scopus 로고
    • Inhibition of the D-alanine:D-alanyl carrier protein ligase from Bacillus subtilis increases the bacterium's susceptibility to antibiotics that target the cell wall
    • May JJ, Finking R, Wiegeshoff F, Weber TT, Bandur N, et al. (2005) Inhibition of the D-alanine:D-alanyl carrier protein ligase from Bacillus subtilis increases the bacterium's susceptibility to antibiotics that target the cell wall. FEBS J 272: 2993-3003.
    • (2005) FEBS J , vol.272 , pp. 2993-3003
    • May, J.J.1    Finking, R.2    Wiegeshoff, F.3    Weber, T.T.4    Bandur, N.5
  • 50
    • 0035478714 scopus 로고    scopus 로고
    • Isolated hypervariable regions derived from streptococcal M proteins specifically bind human C4b-binding protein: Implications for antigenic variation
    • Morfeldt E, Berggard K, Persson J, Drakenberg T, Johnsson E, et al. (2001) Isolated hypervariable regions derived from streptococcal M proteins specifically bind human C4b-binding protein: implications for antigenic variation. J Immunol 167: 3870-3877.
    • (2001) J Immunol , vol.167 , pp. 3870-3877
    • Morfeldt, E.1    Berggard, K.2    Persson, J.3    Drakenberg, T.4    Johnsson, E.5
  • 51
    • 0036841294 scopus 로고    scopus 로고
    • Acquisition of regulators of complement activation by Streptococcus pyogenes serotype M1
    • Pandiripally V, Gregory E, Cue D (2002) Acquisition of regulators of complement activation by Streptococcus pyogenes serotype M1. Infect Immun 70: 6206-6214.
    • (2002) Infect Immun , vol.70 , pp. 6206-6214
    • Pandiripally, V.1    Gregory, E.2    Cue, D.3
  • 52
    • 0342265104 scopus 로고    scopus 로고
    • Assessment of the interaction of human complement regulatory proteins with group A streptococcus. Identification of a high-affinity group A streptococcus binding site in FHL-1
    • Pérez-Caballero D, Alberti S, Vivanco F, Sánchez-Corral P, Rodriguez de Córdoba S (2000) Assessment of the interaction of human complement regulatory proteins with group A streptococcus. Identification of a high-affinity group A streptococcus binding site in FHL-1. Eur J Immunol 30: 1243-1253.
    • (2000) Eur J Immunol , vol.30 , pp. 1243-1253
    • Pérez-Caballero, D.1    Alberti, S.2    Vivanco, F.3    Sánchez-Corral, P.4    Rodriguez de Córdoba, S.5
  • 53
    • 0022295839 scopus 로고
    • Inhibition of complement-mediated opsonization and phagocytosis of Streptococcus pyogenes by D fragments of fibrinogen and fibrin bound to cell surface M protein
    • Whitnack E, Beachey EH (1985) Inhibition of complement-mediated opsonization and phagocytosis of Streptococcus pyogenes by D fragments of fibrinogen and fibrin bound to cell surface M protein. J Exp Med 162: 1983-1997.
    • (1985) J Exp Med , vol.162 , pp. 1983-1997
    • Whitnack, E.1    Beachey, E.H.2
  • 54
    • 0020075242 scopus 로고
    • Restricted deposition of C3 on M+ group A streptococci: Correlation with resistance to phagocytosis
    • Jacks-Weis J, Kim Y, Cleary PP (1982) Restricted deposition of C3 on M+ group A streptococci: correlation with resistance to phagocytosis. J Immunol 128: 1897-1902.
    • (1982) J Immunol , vol.128 , pp. 1897-1902
    • Jacks-Weis, J.1    Kim, Y.2    Cleary, P.P.3
  • 56
    • 1842684177 scopus 로고    scopus 로고
    • The interaction of streptococcal inhibitor of complement (SIC) and its proteolytic fragments with the human beta defensins
    • Fernie-King BA, Seilly DJ, Davies A, Lachmann PJ (2004) The interaction of streptococcal inhibitor of complement (SIC) and its proteolytic fragments with the human beta defensins. Immunol 111: 444-452.
    • (2004) Immunol , vol.111 , pp. 444-452
    • Fernie-King, B.A.1    Seilly, D.J.2    Davies, A.3    Lachmann, P.J.4
  • 57
    • 0037930850 scopus 로고    scopus 로고
    • SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides
    • Frick IM, Akesson P, Rasmussen M, Schmidtchen A, Björck L (2003) SIC, a secreted protein of Streptococcus pyogenes that inactivates antibacterial peptides. J Biol Chem 278: 16561-16566.
    • (2003) J Biol Chem , vol.278 , pp. 16561-16566
    • Frick, I.M.1    Akesson, P.2    Rasmussen, M.3    Schmidtchen, A.4    Björck, L.5
  • 58
    • 0037188512 scopus 로고    scopus 로고
    • Insight into the molecular basis of pathogen abundance: Group A streptococcus inhibitor of complement inhibits bacterial adherence and internalization into human cells
    • Hoe NP, Ireland RM, DeLeo FR, Gowen BB, Dorward DW, et al. (2002) Insight into the molecular basis of pathogen abundance: Group A streptococcus inhibitor of complement inhibits bacterial adherence and internalization into human cells. Proc Natl Acad Sci U S A 99: 7646-7651.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 7646-7651
    • Hoe, N.P.1    Ireland, R.M.2    DeLeo, F.R.3    Gowen, B.B.4    Dorward, D.W.5
  • 59
    • 0031669931 scopus 로고    scopus 로고
    • Identification of csrR/csrS, a genetic locus that regulates hyaluronic acid capsule synthesis in group A streptococcus
    • Levin JC, Wessels MR (1998) Identification of csrR/csrS, a genetic locus that regulates hyaluronic acid capsule synthesis in group A streptococcus. Mol Microbiol 30: 209-219.
    • (1998) Mol Microbiol , vol.30 , pp. 209-219
    • Levin, J.C.1    Wessels, M.R.2
  • 60
    • 0033053646 scopus 로고    scopus 로고
    • A response regulator that represses transcription of several virulence operons in the group A streptococcus
    • Federle MJ, McIver KS, Scott JR (1999) A response regulator that represses transcription of several virulence operons in the group A streptococcus. J Bacteriol 181: 3649-3657.
    • (1999) J Bacteriol , vol.181 , pp. 3649-3657
    • Federle, M.J.1    McIver, K.S.2    Scott, J.R.3
  • 61
    • 0041387460 scopus 로고    scopus 로고
    • Role of RopB in growth phase expression of the SpeB cysteine protease of Streptococcus pyogenes
    • Neely MN, Lyon WR, Runft DL, Caparon M (2003) Role of RopB in growth phase expression of the SpeB cysteine protease of Streptococcus pyogenes. J Bacteriol 185: 5166-5174.
    • (2003) J Bacteriol , vol.185 , pp. 5166-5174
    • Neely, M.N.1    Lyon, W.R.2    Runft, D.L.3    Caparon, M.4
  • 62
    • 0036153610 scopus 로고    scopus 로고
    • Rgg influences the expression of multiple regulatory loci to coregulate virulence factor expression in Streptococcus pyogenes
    • Chaussee MS, Sylva GL, Sturdevant DE, Smoot LM, Graham MR, et al. (2002) Rgg influences the expression of multiple regulatory loci to coregulate virulence factor expression in Streptococcus pyogenes. Infect Immun 70: 762-770.
    • (2002) Infect Immun , vol.70 , pp. 762-770
    • Chaussee, M.S.1    Sylva, G.L.2    Sturdevant, D.E.3    Smoot, L.M.4    Graham, M.R.5
  • 63
    • 0141960369 scopus 로고    scopus 로고
    • Rgg coordinates virulence factor synthesis and metabolism in Streptococcus pyogenes
    • Chaussee MS, Somerville GA, Reitzer L, Musser JM (2003) Rgg coordinates virulence factor synthesis and metabolism in Streptococcus pyogenes. J Bacteriol 185: 6016-6024.
    • (2003) J Bacteriol , vol.185 , pp. 6016-6024
    • Chaussee, M.S.1    Somerville, G.A.2    Reitzer, L.3    Musser, J.M.4
  • 65
    • 0016724704 scopus 로고
    • Influence of alanyl ester residues on the binding of magnesium ions to teichoic acids
    • Lambert PA, Hancock IC, Baddily J (1975) Influence of alanyl ester residues on the binding of magnesium ions to teichoic acids. Biochem J 151: 671-676.
    • (1975) Biochem J , vol.151 , pp. 671-676
    • Lambert, P.A.1    Hancock, I.C.2    Baddily, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.