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Volumn 3, Issue 2, 2008, Pages 205-221

Virulence factors in pneumococcal respiratory pathogenesis

Author keywords

Bacteriocins; Competence; Oxidative stress; Pili; Pneumolysin; Polysaccharide capsule; Proteases; Streptococcus pneumoniae

Indexed keywords

BACTERIAL POLYSACCHARIDE; BACTERIOCIN; CELL SURFACE PROTEIN; ENDONUCLEASE; ENDOPEPTIDASE CLP; HYALURONIDASE; MYOCILIN; MYOCILIN 4; PNEUMOLYSIN; PROTEINASE; PYRUVATE OXIDASE; VIRULENCE FACTOR;

EID: 47249148402     PISSN: 17460913     EISSN: None     Source Type: Journal    
DOI: 10.2217/17460913.3.2.205     Document Type: Review
Times cited : (21)

References (140)
  • 1
    • 0027372678 scopus 로고
    • A brief history of the pneumococcus in biomedical research: A panoply of scientific discovery
    • Watson DA, Musher DM, Jacobson JW, Verhoef J: A brief history of the pneumococcus in biomedical research: a panoply of scientific discovery. Clin. Infect. Dis. 17, 913-924 (1993).
    • (1993) Clin. Infect. Dis , vol.17 , pp. 913-924
    • Watson, D.A.1    Musher, D.M.2    Jacobson, J.W.3    Verhoef, J.4
  • 2
    • 1442299471 scopus 로고    scopus 로고
    • Streptoccus pneumoniae colonisation: The key to pneumococcal disease
    • Bogaert D, De Groot R, Hermans PW: Streptoccus pneumoniae colonisation: the key to pneumococcal disease. Lancet Infect. Dis. 4, 144-154 (2004).
    • (2004) Lancet Infect. Dis , vol.4 , pp. 144-154
    • Bogaert, D.1    De Groot, R.2    Hermans, P.W.3
  • 3
    • 30344475502 scopus 로고    scopus 로고
    • Streptococcus pneumoniae: Epidemiology, risk factors, and clinical features
    • Ortqvist A, Hedlund J, Kalin M: Streptococcus pneumoniae: epidemiology, risk factors, and clinical features. Semin. Respir. Crit. Care Med. 26, 563-574 (2005).
    • (2005) Semin. Respir. Crit. Care Med , vol.26 , pp. 563-574
    • Ortqvist, A.1    Hedlund, J.2    Kalin, M.3
  • 4
    • 4544275380 scopus 로고    scopus 로고
    • Streptococcus pneumoniae: Epidemiology and patterns of resistance
    • Jacobs MR: Streptococcus pneumoniae: epidemiology and patterns of resistance. Am. J. Med. 117(Suppl. 3A), 3S-15S (2004).
    • (2004) Am. J. Med , vol.117 , Issue.SUPPL. 3A
    • Jacobs, M.R.1
  • 5
    • 0242684416 scopus 로고    scopus 로고
    • Decline in invasive pneumococcal disease after the introduction of protein-polysaccharide conjugate vaccine
    • Whitney CG, Farley MM, Hadler J et al.: Decline in invasive pneumococcal disease after the introduction of protein-polysaccharide conjugate vaccine. N. Engl. J. Med. 348, 1737-1746 (2003).
    • (2003) N. Engl. J. Med , vol.348 , pp. 1737-1746
    • Whitney, C.G.1    Farley, M.M.2    Hadler, J.3
  • 6
    • 37349009553 scopus 로고    scopus 로고
    • Incidence of pneumococcal disease due to non-pneumococcal conjugate vaccine (PCV7) serotypes in the United States during the era of widespread PCV7 vaccination, 1998-2004
    • Hicks LA, Harrison LH, Flannery B et al.: Incidence of pneumococcal disease due to non-pneumococcal conjugate vaccine (PCV7) serotypes in the United States during the era of widespread PCV7 vaccination, 1998-2004. J. Infect. Dis. 196, 1346-1354 (2007).
    • (2007) J. Infect. Dis , vol.196 , pp. 1346-1354
    • Hicks, L.A.1    Harrison, L.H.2    Flannery, B.3
  • 7
    • 36849086796 scopus 로고    scopus 로고
    • Streptococcus pneumoniae: Proteomics of surface proteins for vaccine development
    • Morsczeck C, Prokohova T, Sigh J et al.: Streptococcus pneumoniae: proteomics of surface proteins for vaccine development. Clin. Microbiol. Infect. 14, 74-81 (2008).
    • (2008) Clin. Microbiol. Infect , vol.14 , pp. 74-81
    • Morsczeck, C.1    Prokohova, T.2    Sigh, J.3
  • 8
    • 0035919670 scopus 로고    scopus 로고
    • Complete genome sequence of a virulent isolate of Streptococcus pneumoniae
    • Tettelin H, Nelson KE, Paulsen IT et al.: Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science 293, 498-506 (2001).
    • (2001) Science , vol.293 , pp. 498-506
    • Tettelin, H.1    Nelson, K.E.2    Paulsen, I.T.3
  • 9
    • 84983711696 scopus 로고
    • Studies on the chemical nature of the substrate inducing transofrmation of pneumococcal types: Indcution of transformation by a desoxyribnucleic acid fraction isolated from the pneumococcus type III
    • Avery OT, MacLeod CM, McCarty M: Studies on the chemical nature of the substrate inducing transofrmation of pneumococcal types: indcution of transformation by a desoxyribnucleic acid fraction isolated from the pneumococcus type III. J. Exp. Med. 79, 137-158 (1944).
    • (1944) J. Exp. Med , vol.79 , pp. 137-158
    • Avery, O.T.1    MacLeod, C.M.2    McCarty, M.3
  • 10
    • 33745920513 scopus 로고    scopus 로고
    • Antibiotic stress induces genetic transformability in the human pathogen Streptococcus pneumoniae
    • Prudhomme M, Attaiech L, Sanchez G, Martin B, Claverys JP: Antibiotic stress induces genetic transformability in the human pathogen Streptococcus pneumoniae. Science 313, 89-92 (2006).
    • (2006) Science , vol.313 , pp. 89-92
    • Prudhomme, M.1    Attaiech, L.2    Sanchez, G.3    Martin, B.4    Claverys, J.P.5
  • 12
    • 36549020646 scopus 로고    scopus 로고
    • Comparative genomic analyses of seventeen Streptococcus pneumoniae strains: Insights into the pneumococcal supragenome
    • Hiller NL, Janto B, Hogg JS et al.: Comparative genomic analyses of seventeen Streptococcus pneumoniae strains: insights into the pneumococcal supragenome. J. Bacteriol. 189, 8186-8195 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 8186-8195
    • Hiller, N.L.1    Janto, B.2    Hogg, J.S.3
  • 13
    • 32044471320 scopus 로고    scopus 로고
    • Clonal and capsular types decide whether pneumococci will act as a primary or opportunistic pathogen
    • Sjostrom K, Spindler C, Ortovist A et al.: Clonal and capsular types decide whether pneumococci will act as a primary or opportunistic pathogen. Clin. Infect. Dis. 42, 451-459 (2006).
    • (2006) Clin. Infect. Dis , vol.42 , pp. 451-459
    • Sjostrom, K.1    Spindler, C.2    Ortovist, A.3
  • 14
    • 4644240495 scopus 로고    scopus 로고
    • Temporal and geographic stability of the serogroup-specific invasive disease potential of Streptococcus pneumoniae in children
    • Brueggemann AB, Peto TE, Crook DW, Butler JC, Kristinsson KG, Spratt BG: Temporal and geographic stability of the serogroup-specific invasive disease potential of Streptococcus pneumoniae in children. J. Infect. Dis. 190, 1203-1211 (2004).
    • (2004) J. Infect. Dis , vol.190 , pp. 1203-1211
    • Brueggemann, A.B.1    Peto, T.E.2    Crook, D.W.3    Butler, J.C.4    Kristinsson, K.G.5    Spratt, B.G.6
  • 15
    • 33746637557 scopus 로고    scopus 로고
    • Identification of a candidate Streptococcus pneumoniae core genome and regions of diversity correlated with invasive pneumococcal disease
    • Obert C, Sublett J, Kaushal D et al.: Identification of a candidate Streptococcus pneumoniae core genome and regions of diversity correlated with invasive pneumococcal disease. Infect. Immun. 74, 4766-4777 (2006).
    • (2006) Infect. Immun , vol.74 , pp. 4766-4777
    • Obert, C.1    Sublett, J.2    Kaushal, D.3
  • 16
    • 40749122598 scopus 로고    scopus 로고
    • Pattern of accessory genes predicts the same relatedness among strains of Streptococcus pneumoniae as sequencing house keeping genes: A novel approach in molecular epidemiology
    • DOI 10.1128/JCM.01438-07 , Epub ahead of print
    • Dagerhamn J, Blomberg C, Browall S, Sjostrom K, Morfeldt E, Henriques-Normark B: Pattern of accessory genes predicts the same relatedness among strains of Streptococcus pneumoniae as sequencing house keeping genes: a novel approach in molecular epidemiology. J. Clin. Microbiol. DOI 10.1128/JCM.01438-07 (2007) (Epub ahead of print).
    • (2007) J. Clin. Microbiol
    • Dagerhamn, J.1    Blomberg, C.2    Browall, S.3    Sjostrom, K.4    Morfeldt, E.5    Henriques-Normark, B.6
  • 17
    • 33646947827 scopus 로고    scopus 로고
    • Genomic diversity between strains of the same serotype and multilocus sequence type among pneumococcal clinical isolates
    • Silva NA, McCluskey I, Jefferies JM et al.: Genomic diversity between strains of the same serotype and multilocus sequence type among pneumococcal clinical isolates. Infect. Immun. 74, 3513-3518 (2006).
    • (2006) Infect. Immun , vol.74 , pp. 3513-3518
    • Silva, N.A.1    McCluskey, I.2    Jefferies, J.M.3
  • 18
    • 34547924465 scopus 로고    scopus 로고
    • Clonal success of piliated penicillin nonsusceptible pneumococci
    • Sjostrom K, Blomberg C, Fernebro J et al.: Clonal success of piliated penicillin nonsusceptible pneumococci. Proc. Natl Acad Sci. USA 104, 12907-12912 (2007).
    • (2007) Proc. Natl Acad Sci. USA , vol.104 , pp. 12907-12912
    • Sjostrom, K.1    Blomberg, C.2    Fernebro, J.3
  • 19
    • 33644543756 scopus 로고    scopus 로고
    • Proteomic analysis of growth phase-dependent proteins of Streptococcus pneumoniae
    • Lee KJ, Bae SM, Lee MR, Yeon SM, Lee YH, Kim KS: Proteomic analysis of growth phase-dependent proteins of Streptococcus pneumoniae. Proteomics 6, 1274-1282 (2006),
    • (2006) Proteomics , vol.6 , pp. 1274-1282
    • Lee, K.J.1    Bae, S.M.2    Lee, M.R.3    Yeon, S.M.4    Lee, Y.H.5    Kim, K.S.6
  • 20
    • 33645744892 scopus 로고    scopus 로고
    • Comparative analysis of growth-phase-dependent gene expression in virulent and avirulent Streptococcus pneumoniae using a high-density DNA microarray
    • Ko KS, Park S, Oh WS et al.: Comparative analysis of growth-phase-dependent gene expression in virulent and avirulent Streptococcus pneumoniae using a high-density DNA microarray. Mol. Cells 21, 82-88 (2006).
    • (2006) Mol. Cells , vol.21 , pp. 82-88
    • Ko, K.S.1    Park, S.2    Oh, W.S.3
  • 21
    • 33845395519 scopus 로고    scopus 로고
    • The effect of protein expression of Streptococcus pneumoniae by blood
    • Bae SM, Yeon SM, Kim TS, Lee KJ: The effect of protein expression of Streptococcus pneumoniae by blood. J. Biochem. Mol. Biol. 39, 703-708 (2006).
    • (2006) J. Biochem. Mol. Biol , vol.39 , pp. 703-708
    • Bae, S.M.1    Yeon, S.M.2    Kim, T.S.3    Lee, K.J.4
  • 24
    • 33744793500 scopus 로고    scopus 로고
    • Attachment of capsular polysaccharide to the cell wall of Streptococcus pneumoniae type 2 is required for invasive disease
    • Morona JK, Morona R, Paton JC: Attachment of capsular polysaccharide to the cell wall of Streptococcus pneumoniae type 2 is required for invasive disease. Proc. Natl Acad. Sci. USA 103, 8505-8510 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8505-8510
    • Morona, J.K.1    Morona, R.2    Paton, J.C.3
  • 25
    • 0034020990 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of CpsD negatively regulates capsular polysaccharide biosynthesis in Streptococcus pneumoniae
    • Morona JK, Paton JC, Miller DC, Morona R: Tyrosine phosphorylation of CpsD negatively regulates capsular polysaccharide biosynthesis in Streptococcus pneumoniae. Mol. Microbiol. 35, 1431-1442 (2000).
    • (2000) Mol. Microbiol , vol.35 , pp. 1431-1442
    • Morona, J.K.1    Paton, J.C.2    Miller, D.C.3    Morona, R.4
  • 26
    • 0036134946 scopus 로고    scopus 로고
    • Streptococcus pneumoniae capsule biosynthesis protein CpsB is a novel manganese-dependent phosphotyrosine-protein phosphatase
    • Morona JK, Morona R, Miller DC, Paton JC: Streptococcus pneumoniae capsule biosynthesis protein CpsB is a novel manganese-dependent phosphotyrosine-protein phosphatase. J. Bacteriol. 184, 577-583 (2002).
    • (2002) J. Bacteriol , vol.184 , pp. 577-583
    • Morona, J.K.1    Morona, R.2    Miller, D.C.3    Paton, J.C.4
  • 27
    • 2442673903 scopus 로고    scopus 로고
    • The effect that mutations in the conserved capsular polysaccharide biosynthesis genes cpsA, cpsB, and cpsD have on virulence of Streptococcus pneumoniae
    • Morona JK, Miller DC, Morona R, Paton JC: The effect that mutations in the conserved capsular polysaccharide biosynthesis genes cpsA, cpsB, and cpsD have on virulence of Streptococcus pneumoniae. J. Infect. Dis. 189, 1905-1913 (2004).
    • (2004) J. Infect. Dis , vol.189 , pp. 1905-1913
    • Morona, J.K.1    Miller, D.C.2    Morona, R.3    Paton, J.C.4
  • 28
    • 0021814103 scopus 로고
    • Phagocytosis and killing of common bacterial pathogens of the lung by human alveolar macrophages
    • Jonsson S, Musher DM, Chapman A, Goree A, Lawrence EC: Phagocytosis and killing of common bacterial pathogens of the lung by human alveolar macrophages. J. Infect. Dis. 152, 4-13 (1985).
    • (1985) J. Infect. Dis , vol.152 , pp. 4-13
    • Jonsson, S.1    Musher, D.M.2    Chapman, A.3    Goree, A.4    Lawrence, E.C.5
  • 29
    • 0242333165 scopus 로고    scopus 로고
    • Streptococcus pneumoniae-associated human macrophage apoptosis after bacterial internalization via complement and Fcgamma receptors correlates with intracellular bacterial load
    • Ali F, Lee ME, Iannelli F et al.: Streptococcus pneumoniae-associated human macrophage apoptosis after bacterial internalization via complement and Fcgamma receptors correlates with intracellular bacterial load. J. Infect. Dis. 188, 1119-1131 (2003).
    • (2003) J. Infect. Dis , vol.188 , pp. 1119-1131
    • Ali, F.1    Lee, M.E.2    Iannelli, F.3
  • 31
    • 0028307194 scopus 로고
    • Phase variation in pneumococcal opacity: Relationship between colonial morphology and nasopharyngeal colonization
    • Weiser JN, Austrian R, Sreenivasan PK, Masure HR: Phase variation in pneumococcal opacity: relationship between colonial morphology and nasopharyngeal colonization. Infect. Immun. 62, 2582-2589 (1994).
    • (1994) Infect. Immun , vol.62 , pp. 2582-2589
    • Weiser, J.N.1    Austrian, R.2    Sreenivasan, P.K.3    Masure, H.R.4
  • 32
    • 0031906480 scopus 로고    scopus 로고
    • Association of intrastrain phase variation in quantity of capsular polysaccharide and teichoic acid with the virulence of Streptococcus pneumoniae
    • Kim JO, Weiser JN: Association of intrastrain phase variation in quantity of capsular polysaccharide and teichoic acid with the virulence of Streptococcus pneumoniae. J. Infect. Dis. 177, 368-377 (1998).
    • (1998) J. Infect. Dis , vol.177 , pp. 368-377
    • Kim, J.O.1    Weiser, J.N.2
  • 33
    • 33644526566 scopus 로고    scopus 로고
    • A pneumococcal pilus influences virulence and host inflammatory responses
    • Barocchi MA, Ries J, Zogaj X et al.: A pneumococcal pilus influences virulence and host inflammatory responses. Proc. Natl Acad. Sci. USA 103, 2857-2862 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 2857-2862
    • Barocchi, M.A.1    Ries, J.2    Zogaj, X.3
  • 34
    • 2442442058 scopus 로고    scopus 로고
    • The molecular basis of fibronectin-mediated bacterial adherence to host cells
    • Schwarz-Linek U, Hook M, Potts JR: The molecular basis of fibronectin-mediated bacterial adherence to host cells. Mol. Microbiol. 52, 631-641 (2004).
    • (2004) Mol. Microbiol , vol.52 , pp. 631-641
    • Schwarz-Linek, U.1    Hook, M.2    Potts, J.R.3
  • 35
    • 33846847480 scopus 로고    scopus 로고
    • Streptococcus pneumoniae pilus subunits protect mice against lethal challenge
    • Gianfaldoni C, Censini S, Hilleringmann M et al.: Streptococcus pneumoniae pilus subunits protect mice against lethal challenge. Infect. Immun. 75, 1059-1062 (2007).
    • (2007) Infect. Immun , vol.75 , pp. 1059-1062
    • Gianfaldoni, C.1    Censini, S.2    Hilleringmann, M.3
  • 37
    • 34250671127 scopus 로고    scopus 로고
    • Association of the pneumococcal pilus with certain capsular serotypes but not with increased virulence
    • Basset A, Trzcinski K, Hermos C et al.: Association of the pneumococcal pilus with certain capsular serotypes but not with increased virulence. J. Clin. Microbiol. 45, 1684-1689 (2007).
    • (2007) J. Clin. Microbiol , vol.45 , pp. 1684-1689
    • Basset, A.1    Trzcinski, K.2    Hermos, C.3
  • 38
    • 33747065797 scopus 로고    scopus 로고
    • Switch from planktonic to sessile life: A major event in pneumococcal pathogenesis
    • Oggioni MR, Trappetti C, Kadioglu A et al.: Switch from planktonic to sessile life: a major event in pneumococcal pathogenesis. Mol. Microbiol. 61, 1196-1210 (2006).
    • (2006) Mol. Microbiol , vol.61 , pp. 1196-1210
    • Oggioni, M.R.1    Trappetti, C.2    Kadioglu, A.3
  • 39
    • 0034971094 scopus 로고    scopus 로고
    • Pneumococcal virulence factors: Structure and function
    • Jedrzejas MJ: Pneumococcal virulence factors: structure and function. Microbiol. Mol. Biol. Rev. 65, 187-207 (2001).
    • (2001) Microbiol. Mol. Biol. Rev , vol.65 , pp. 187-207
    • Jedrzejas, M.J.1
  • 40
    • 33745585810 scopus 로고    scopus 로고
    • Pneumococcal neuraminidases A and B both have essential roles during infection of the respiratory tract and sepsis
    • Manco S, Hernon F, Yesilkaya H, Paton JC, Andrew PW, Kadioglu A: Pneumococcal neuraminidases A and B both have essential roles during infection of the respiratory tract and sepsis. Infect. Immun, 74, 4014-4020 (2006).
    • (2006) Infect. Immun , vol.74 , pp. 4014-4020
    • Manco, S.1    Hernon, F.2    Yesilkaya, H.3    Paton, J.C.4    Andrew, P.W.5    Kadioglu, A.6
  • 41
    • 33746692516 scopus 로고    scopus 로고
    • Bacterial neuraminidase facilitates mucosal infection by participating in biofilm production
    • Soong G, Muir A, Gomez MI et al.: Bacterial neuraminidase facilitates mucosal infection by participating in biofilm production. J. Clin. Invest. 116, 2297-2305 (2006).
    • (2006) J. Clin. Invest , vol.116 , pp. 2297-2305
    • Soong, G.1    Muir, A.2    Gomez, M.I.3
  • 42
    • 33745890309 scopus 로고    scopus 로고
    • Direct detection of bacterial biofilms on the middle-ear mucosa of children with chronic otitis media
    • Hall-Stoodley L, Hu FZ, Gieseke A et al.: Direct detection of bacterial biofilms on the middle-ear mucosa of children with chronic otitis media. JAMA 296, 202-211 (2006).
    • (2006) JAMA , vol.296 , pp. 202-211
    • Hall-Stoodley, L.1    Hu, F.Z.2    Gieseke, A.3
  • 43
    • 0037443951 scopus 로고    scopus 로고
    • Role of neuraminidase in lethal synergism between influenza virus and Streptococcus pneumoniae
    • McCullers JA, Bartmess KC: Role of neuraminidase in lethal synergism between influenza virus and Streptococcus pneumoniae. J Infect. Dis. 187, 1000-1009 (2003).
    • (2003) J Infect. Dis , vol.187 , pp. 1000-1009
    • McCullers, J.A.1    Bartmess, K.C.2
  • 44
    • 0036892227 scopus 로고    scopus 로고
    • Neuraminidase expressed by Streptococcus pneumoniae desialylates the lipopolysaccharide of Neisseria meningitidis and Haemophilus Influenzae: A paradigm for interbacterial competition among pathogens of the human respiratory tract
    • Shakhnovich EA, King SJ, Weiser JN: Neuraminidase expressed by Streptococcus pneumoniae desialylates the lipopolysaccharide of Neisseria meningitidis and Haemophilus Influenzae: a paradigm for interbacterial competition among pathogens of the human respiratory tract. Infect. Immun. 70, 7161-7164 (2002).
    • (2002) Infect. Immun , vol.70 , pp. 7161-7164
    • Shakhnovich, E.A.1    King, S.J.2    Weiser, J.N.3
  • 45
    • 0041823519 scopus 로고    scopus 로고
    • ZmpB, a novel virulence factor of Streptcoccus pneumoniae that induces tumor necrosis factor alpha production in the respiratory tract
    • Blue CE, Paterson GK, AR Kerr, Berge M, Claverys JP, Mitchell TJ: ZmpB, a novel virulence factor of Streptcoccus pneumoniae that induces tumor necrosis factor alpha production in the respiratory tract. Infect. Immun. 71, 4925-4935 (2003).
    • (2003) Infect. Immun , vol.71 , pp. 4925-4935
    • Blue, C.E.1    Paterson, G.K.2    Kerr, A.R.3    Berge, M.4    Claverys, J.P.5    Mitchell, T.J.6
  • 46
    • 0043166893 scopus 로고    scopus 로고
    • Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix metalloproteinase 9 and is a virulence factor in experimental pneumonia
    • Oggioni MR, Memmi G, Maggi T, Chiavolini D, Iannelli F, Pozzi G: Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix metalloproteinase 9 and is a virulence factor in experimental pneumonia. Mol Microbiol. 49, 795-805 (2003).
    • (2003) Mol Microbiol , vol.49 , pp. 795-805
    • Oggioni, M.R.1    Memmi, G.2    Maggi, T.3    Chiavolini, D.4    Iannelli, F.5    Pozzi, G.6
  • 47
    • 0018833761 scopus 로고
    • IgA1 proteases from Haemophilus influenzae, Streptococcus pneumoniae, Neisseria meningitidis, and Streptococcus sanguis. comparative immunochemical studies
    • Kilian M, Mestecky J, Kulhavy R, Tomana, M, Butler WT. IgA1 proteases from Haemophilus influenzae, Streptococcus pneumoniae, Neisseria meningitidis, and Streptococcus sanguis. comparative immunochemical studies. J. Immunol. 124, 2596-600 (1980).
    • (1980) J. Immunol , vol.124 , pp. 2596-2600
    • Kilian, M.1    Mestecky, J.2    Kulhavy, R.3    Tomana, M.4    Butler, W.T.5
  • 48
    • 0037386570 scopus 로고    scopus 로고
    • Weiser JN, Bae D, Fasching C, Scamurra RW, AJ Ratner, Janoff EN: Antibody-enhanced pneumococcal adherence requires IgA1 protease. Proc. Natl Acad. Sci. USA 100, 4215-4220 (2003).
    • Weiser JN, Bae D, Fasching C, Scamurra RW, AJ Ratner, Janoff EN: Antibody-enhanced pneumococcal adherence requires IgA1 protease. Proc. Natl Acad. Sci. USA 100, 4215-4220 (2003).
  • 49
    • 34147118014 scopus 로고    scopus 로고
    • Impact of the molecular form of immunoglobulin A on functional activity in defense against Streptococcus pneumoniae
    • Fasching CE, Grossman T, Corthesy B, Plaut AG, Weiser JN, Janoff EN: Impact of the molecular form of immunoglobulin A on functional activity in defense against Streptococcus pneumoniae. Infect. Immun. 75, 1801-1810 (2007).
    • (2007) Infect. Immun , vol.75 , pp. 1801-1810
    • Fasching, C.E.1    Grossman, T.2    Corthesy, B.3    Plaut, A.G.4    Weiser, J.N.5    Janoff, E.N.6
  • 50
    • 0032797913 scopus 로고    scopus 로고
    • Pneumococcal surface protein A inhibits complement activation by Streptococcus pneumoniae
    • Tu AH, Fulgham RL, McCrory MA, Briles DE, Szalai AJ: Pneumococcal surface protein A inhibits complement activation by Streptococcus pneumoniae. Infect. Immun. 67, 4720-4724 (1999).
    • (1999) Infect. Immun , vol.67 , pp. 4720-4724
    • Tu, A.H.1    Fulgham, R.L.2    McCrory, M.A.3    Briles, D.E.4    Szalai, A.J.5
  • 51
    • 22544455943 scopus 로고    scopus 로고
    • Additive inhibition of complement deposition by pneumolysin and PspA facilitates Streptococcus pneumoniae septicemia
    • Yuste J, Botto M, Paton JC, Holden DW, Brown JS: Additive inhibition of complement deposition by pneumolysin and PspA facilitates Streptococcus pneumoniae septicemia. J Immunol. 175, 1813-1819 (2005).
    • (2005) J Immunol , vol.175 , pp. 1813-1819
    • Yuste, J.1    Botto, M.2    Paton, J.C.3    Holden, D.W.4    Brown, J.S.5
  • 52
    • 33845488909 scopus 로고    scopus 로고
    • Differential role of CbpA and PspA in modulation of in vitro CXC chemokine responses of respiratory epithelial cells to infection with Streptococcus pneumoniae
    • Graham RM, Paton JC: Differential role of CbpA and PspA in modulation of in vitro CXC chemokine responses of respiratory epithelial cells to infection with Streptococcus pneumoniae. Infect. Immun. 74, 6739-6749 (2006).
    • (2006) Infect. Immun , vol.74 , pp. 6739-6749
    • Graham, R.M.1    Paton, J.C.2
  • 53
    • 0034664821 scopus 로고    scopus 로고
    • The polymeric immunoglobulin receptor translocates pneumococci across human nasopharyngeal epithelial cells
    • Zhang JR, Mostov KE, Lamm ME et al.: The polymeric immunoglobulin receptor translocates pneumococci across human nasopharyngeal epithelial cells. Cell 102, 827-837 (2000).
    • (2000) Cell , vol.102 , pp. 827-837
    • Zhang, J.R.1    Mostov, K.E.2    Lamm, M.E.3
  • 54
    • 1342304130 scopus 로고    scopus 로고
    • Ectodomains 3 and 4 of human polymeric Immunoglobulin receptor (hpIgR) mediate invasion of Streptococcus pneumoniae into the epithelium
    • Elm C, Braathen R, Bergmann S et al.: Ectodomains 3 and 4 of human polymeric Immunoglobulin receptor (hpIgR) mediate invasion of Streptococcus pneumoniae into the epithelium. J. Biol. Chem. 279, 6296-6304 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 6296-6304
    • Elm, C.1    Braathen, R.2    Bergmann, S.3
  • 55
    • 4644242435 scopus 로고    scopus 로고
    • An important role for polymeric Ig receptor-mediated transport of IgA in protection against Streptococcus pneumoniae nasopharyngeal carriage
    • Sun K, Johansen FE, Eckmann L, Metzger DW: An important role for polymeric Ig receptor-mediated transport of IgA in protection against Streptococcus pneumoniae nasopharyngeal carriage. J. Immunol. 173, 4576-4581 (2004).
    • (2004) J. Immunol , vol.173 , pp. 4576-4581
    • Sun, K.1    Johansen, F.E.2    Eckmann, L.3    Metzger, D.W.4
  • 56
    • 0029165459 scopus 로고
    • Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor
    • Cundell DR, Gerard NP, Gerard C, Idapaan-Heikkila I, Tuomanen EI: Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor. Nature 377, 435-438 (1995).
    • (1995) Nature , vol.377 , pp. 435-438
    • Cundell, D.R.1    Gerard, N.P.2    Gerard, C.3    Idapaan-Heikkila, I.4    Tuomanen, E.I.5
  • 57
    • 0030968621 scopus 로고    scopus 로고
    • SpsA, a novel pneumococcal surface protein with specific binding to secretory immunoglobulin A and secretory component
    • Hammerschmidt S, Talay SR, Brandtzaeg P, Chhatwal GS: SpsA, a novel pneumococcal surface protein with specific binding to secretory immunoglobulin A and secretory component. Mol. Microbiol. 25, 1113-1124 (1997).
    • (1997) Mol. Microbiol , vol.25 , pp. 1113-1124
    • Hammerschmidt, S.1    Talay, S.R.2    Brandtzaeg, P.3    Chhatwal, G.S.4
  • 58
    • 0037083508 scopus 로고    scopus 로고
    • Streptococcus pneumoniae evades complement attack and opsonophagocytosis by expressing the pspC locus-encoded Hic protein that binds to short consensus repeats 8-11 of factor H
    • Jarva H, Janulczyk R, Hellwage J, Zipfel PF, Bjorck L, Meri S: Streptococcus pneumoniae evades complement attack and opsonophagocytosis by expressing the pspC locus-encoded Hic protein that binds to short consensus repeats 8-11 of factor H. J. Immunol. 168, 1886-1894 (2002).
    • (2002) J. Immunol , vol.168 , pp. 1886-1894
    • Jarva, H.1    Janulczyk, R.2    Hellwage, J.3    Zipfel, P.F.4    Bjorck, L.5    Meri, S.6
  • 59
    • 33744957535 scopus 로고    scopus 로고
    • Streptococcus pneumoniae recruits complement factor H through the amino terminus of CbpA
    • Lu L, Ma Y, Zhang JR: Streptococcus pneumoniae recruits complement factor H through the amino terminus of CbpA. J. Biol. Chem. 281, 15464-15474 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 15464-15474
    • Lu, L.1    Ma, Y.2    Zhang, J.R.3
  • 60
    • 33748051087 scopus 로고    scopus 로고
    • The contribution of PspC to pneumococcal virulence varies between strains and is accomplished by both complement evasion and complement-independent mechanisms
    • Kerr AR, Paterson GK, McCluskey J et al.: The contribution of PspC to pneumococcal virulence varies between strains and is accomplished by both complement evasion and complement-independent mechanisms. Infect. Immun. 74, 5319-5324 (2006).
    • (2006) Infect. Immun , vol.74 , pp. 5319-5324
    • Kerr, A.R.1    Paterson, G.K.2    McCluskey, J.3
  • 61
    • 34147146425 scopus 로고    scopus 로고
    • Contributions of pneumolysin, pneumococcal surface protein A (PspA), and PspC to pathogenicity of Streptococcus pneumoniae D39 in a mouse model
    • Ogunniyi AD, LeMessurier KS, Graham RM et al.: Contributions of pneumolysin, pneumococcal surface protein A (PspA), and PspC to pathogenicity of Streptococcus pneumoniae D39 in a mouse model. Infect. Immun. 75, 1843-1851 (2007).
    • (2007) Infect. Immun , vol.75 , pp. 1843-1851
    • Ogunniyi, A.D.1    LeMessurier, K.S.2    Graham, R.M.3
  • 62
    • 2142646463 scopus 로고    scopus 로고
    • Pneumococcal surface protein C contributes to sepsis caused by Streptococcus pneumoniae in mice
    • Iannelli F, Chiavolini D, Ricci S, Oggioni MR, Pozzi G: Pneumococcal surface protein C contributes to sepsis caused by Streptococcus pneumoniae in mice. Infect. Immun. 72, 3077-3080 (2004).
    • (2004) Infect. Immun , vol.72 , pp. 3077-3080
    • Iannelli, F.1    Chiavolini, D.2    Ricci, S.3    Oggioni, M.R.4    Pozzi, G.5
  • 63
    • 6944224035 scopus 로고    scopus 로고
    • Tissue-specific contributions of pneumococcal virulence factors to pathogenesis
    • Orihuela CJ, Gao G, Francis KP Yu J, Tuomanen EI: Tissue-specific contributions of pneumococcal virulence factors to pathogenesis. Infect. Dis. 190, 1661-1669 (2004).
    • (2004) Infect. Dis , vol.190 , pp. 1661-1669
    • Orihuela, C.J.1    Gao, G.2    Francis, K.P.3    Yu, J.4    Tuomanen, E.I.5
  • 64
    • 0036118026 scopus 로고    scopus 로고
    • Role of pneumococcal surface protein C in nasopharyngeal carriage and pneumonia and its ability to elicit protection against carriage of Streptococcus pneumoniae
    • Balachandran P, Brooks-Walter A, Virolainen-Julkunen A, Hollingshead SK, Briles DE: Role of pneumococcal surface protein C in nasopharyngeal carriage and pneumonia and its ability to elicit protection against carriage of Streptococcus pneumoniae. Infect. Immun. 70, 2526-2534 (2002).
    • (2002) Infect. Immun , vol.70 , pp. 2526-2534
    • Balachandran, P.1    Brooks-Walter, A.2    Virolainen-Julkunen, A.3    Hollingshead, S.K.4    Briles, D.E.5
  • 65
    • 0033981143 scopus 로고    scopus 로고
    • Additive attenuation of virulence of Streptococcus pneumoniae by mutation of the genes encoding pneumolysin and other putative pneumococcal virulence proteins
    • Berry AM, Paton JC: Additive attenuation of virulence of Streptococcus pneumoniae by mutation of the genes encoding pneumolysin and other putative pneumococcal virulence proteins. Infect. Immun. 68, 133-140 (2000).
    • (2000) Infect. Immun , vol.68 , pp. 133-140
    • Berry, A.M.1    Paton, J.C.2
  • 66
    • 31844451911 scopus 로고    scopus 로고
    • Multifunctional role of choline binding protein G in pneumococcal pathogenesis
    • Mann B, Orihuela C, Antikainen J et al.: Multifunctional role of choline binding protein G in pneumococcal pathogenesis. Infect. Immun. 74, 821-829 (2006).
    • (2006) Infect. Immun , vol.74 , pp. 821-829
    • Mann, B.1    Orihuela, C.2    Antikainen, J.3
  • 67
    • 0034786512 scopus 로고    scopus 로고
    • The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence
    • Holmes AR, McNab R, Minsap KW et al.: The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence. Mol. Microbiol. 41, 1395-1408 (2001).
    • (2001) Mol. Microbiol , vol.41 , pp. 1395-1408
    • Holmes, A.R.1    McNab, R.2    Minsap, K.W.3
  • 68
    • 20244373759 scopus 로고    scopus 로고
    • PavA of Streptococcus pneumoniae modulates adherence, invasion, and meningeal inflammation
    • Pracht D, Elm C, Gerber J et al.: PavA of Streptococcus pneumoniae modulates adherence, invasion, and meningeal inflammation. Infect Immun. 73, 2680-2689 (2005).
    • (2005) Infect Immun , vol.73 , pp. 2680-2689
    • Pracht, D.1    Elm, C.2    Gerber, J.3
  • 69
    • 0025640782 scopus 로고
    • Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O and contains a single cysteine
    • Geoffroy C, Mengaud J, Alouf JE, Cossart P: Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O and contains a single cysteine. J. Bacteriol. 172, 7301-7305 (1990).
    • (1990) J. Bacteriol , vol.172 , pp. 7301-7305
    • Geoffroy, C.1    Mengaud, J.2    Alouf, J.E.3    Cossart, P.4
  • 70
    • 0018917907 scopus 로고
    • Binding of cholesterol by sulfhydryl-activated cytolysins
    • Johnson MK, Geoffroy C, Alouf JE: Binding of cholesterol by sulfhydryl-activated cytolysins. Infect. Immun. 27, 97-101 (1980).
    • (1980) Infect. Immun , vol.27 , pp. 97-101
    • Johnson, M.K.1    Geoffroy, C.2    Alouf, J.E.3
  • 71
    • 0023251174 scopus 로고
    • Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumaniae
    • Walker JA, Allen RL, Falmagne P, Johnson MK, Boulnois GJ: Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumaniae. Infect. Immun. 55, 1184-1189 (1987).
    • (1987) Infect. Immun , vol.55 , pp. 1184-1189
    • Walker, J.A.1    Allen, R.L.2    Falmagne, P.3    Johnson, M.K.4    Boulnois, G.J.5
  • 72
    • 0014941489 scopus 로고
    • Multiple antibiotic resistance in a bacterium with suppressed autolytic system
    • Tomasz A, Albino A, Zanati E: Multiple antibiotic resistance in a bacterium with suppressed autolytic system. Nature 227, 138-140 (1970).
    • (1970) Nature , vol.227 , pp. 138-140
    • Tomasz, A.1    Albino, A.2    Zanati, E.3
  • 73
    • 0014961281 scopus 로고
    • Choline-containing teichoic acid as a structural component of pneumococcal cell wall and its role in sensitivity to lysis by an autolytic enzyme
    • Mosser JL, Tomasz A: Choline-containing teichoic acid as a structural component of pneumococcal cell wall and its role in sensitivity to lysis by an autolytic enzyme. J Biol. Chem. 245, 287-298 (1970).
    • (1970) J Biol. Chem , vol.245 , pp. 287-298
    • Mosser, J.L.1    Tomasz, A.2
  • 75
    • 0035035231 scopus 로고    scopus 로고
    • The autolytic enzyme LytA of Streptococcus pneumoniae is not responsible for releasing pneumolysin
    • Balachandran P, Honingshead SK, Paton JC, Briles DE: The autolytic enzyme LytA of Streptococcus pneumoniae is not responsible for releasing pneumolysin. J. Bacteriol. 183, 3108-3116 (2001).
    • (2001) J. Bacteriol , vol.183 , pp. 3108-3116
    • Balachandran, P.1    Honingshead, S.K.2    Paton, J.C.3    Briles, D.E.4
  • 76
    • 20844444771 scopus 로고    scopus 로고
    • Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: Genetic requirements
    • Guiral S, Mitchell TJ, Martin B, Claverys JP: Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: genetic requirements. Proc. Natl Acad. Sci. USA 102, 8710-8715 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 8710-8715
    • Guiral, S.1    Mitchell, T.J.2    Martin, B.3    Claverys, J.P.4
  • 77
    • 12844281219 scopus 로고    scopus 로고
    • Contribution of the ATP-dependent protease C1pCP to the autolysis and virulence of Streptococcus pneumaniae
    • Ibrahim YM, Kerr AR, Silva NA, Mitchell TJ: Contribution of the ATP-dependent protease C1pCP to the autolysis and virulence of Streptococcus pneumaniae. Infect. Immun. 73, 730-740 (2005).
    • (2005) Infect. Immun , vol.73 , pp. 730-740
    • Ibrahim, Y.M.1    Kerr, A.R.2    Silva, N.A.3    Mitchell, T.J.4
  • 78
    • 0344837301 scopus 로고    scopus 로고
    • Pneumolysin-dependent and -independent gene expression identified by cDNA microarray analysis of THP-1 human mononuclear cells stimulated by Streptococcus pneumoniae
    • Rogers PD, Thornton J, Barker KS et al.: Pneumolysin-dependent and -independent gene expression identified by cDNA microarray analysis of THP-1 human mononuclear cells stimulated by Streptococcus pneumoniae. Infect. Immun. 71, 2087-2094 (2003).
    • (2003) Infect. Immun , vol.71 , pp. 2087-2094
    • Rogers, P.D.1    Thornton, J.2    Barker, K.S.3
  • 79
    • 34548080058 scopus 로고    scopus 로고
    • Histone modifications induced by a family of bacterial toxins
    • Hamon MA, Batsche E, Regnault B et al.: Histone modifications induced by a family of bacterial toxins. Proc. Natl Acad. Sci. USA 104, 13467-13472 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 13467-13472
    • Hamon, M.A.1    Batsche, E.2    Regnault, B.3
  • 80
    • 0029986122 scopus 로고    scopus 로고
    • Distinct roles for pneumolysin's cytotoxic and complement activities in the pathogenesis of pneumococcal pneumonia
    • Rubins JB, Charboneau D, Fasching C et al.: Distinct roles for pneumolysin's cytotoxic and complement activities in the pathogenesis of pneumococcal pneumonia. Am. J. Res. Respir. Crit. Care Med. 153, 1339-1346 (1996).
    • (1996) Am. J. Res. Respir. Crit. Care Med , vol.153 , pp. 1339-1346
    • Rubins, J.B.1    Charboneau, D.2    Fasching, C.3
  • 81
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • Tilley SJ, Orlova EV, Gilbert RJ, Andrew PW, Saibil HR: Structural basis of pore formation by the bacterial toxin pneumolysin. Cell 121, 247-56 (2005).
    • (2005) Cell , vol.121 , pp. 247-256
    • Tilley, S.J.1    Orlova, E.V.2    Gilbert, R.J.3    Andrew, P.W.4    Saibil, H.R.5
  • 82
    • 3142754927 scopus 로고    scopus 로고
    • Pneumolysin-induced lung injury is independent of leukocyte trafficking into the alveolar space
    • Maus UA, Srivastava M, Paton JC et al.: Pneumolysin-induced lung injury is independent of leukocyte trafficking into the alveolar space. J. Immunol. 173, 1307-1312 (2004).
    • (2004) J. Immunol , vol.173 , pp. 1307-1312
    • Maus, U.A.1    Srivastava, M.2    Paton, J.C.3
  • 83
    • 34548038609 scopus 로고    scopus 로고
    • Lim JH, Stirling B, Derry J et al.: Tumor suppressor CYLD regulates acute lung injury in lethal Streptococcus pneumaniae infections. Immunity 27, 349-360 (2007).
    • Lim JH, Stirling B, Derry J et al.: Tumor suppressor CYLD regulates acute lung injury in lethal Streptococcus pneumaniae infections. Immunity 27, 349-360 (2007).
  • 84
    • 4043145865 scopus 로고    scopus 로고
    • Pneumolysin potentiates oxidative inactivation of alpha-1-proteinase inhibitor by activated human neutrophils
    • Cockeran R, Theron AJ, Feldman C, Mitchel TJ, Anderson R: Pneumolysin potentiates oxidative inactivation of alpha-1-proteinase inhibitor by activated human neutrophils. Respir. Med. 98, 865-871 (2004).
    • (2004) Respir. Med , vol.98 , pp. 865-871
    • Cockeran, R.1    Theron, A.J.2    Feldman, C.3    Mitchel, T.J.4    Anderson, R.5
  • 85
    • 0036138321 scopus 로고    scopus 로고
    • Roles of interleukin-6 and macrophage inflammatory protein-2 in pneumolysin-induced lung inflammation in mice
    • Rijneveld AW, van den Dobbelsteen GP, Florquin S et al.: Roles of interleukin-6 and macrophage inflammatory protein-2 in pneumolysin-induced lung inflammation in mice. J. Infect. Dis. 185, 123-126 (2002).
    • (2002) J. Infect. Dis , vol.185 , pp. 123-126
    • Rijneveld, A.W.1    van den Dobbelsteen, G.P.2    Florquin, S.3
  • 86
    • 34247607711 scopus 로고    scopus 로고
    • Importance of phosphoinositide 3-kinase gamma in the host defense against pneumococcal infection
    • Maus UA, Backi M, Winter C et al.: Importance of phosphoinositide 3-kinase gamma in the host defense against pneumococcal infection. Am. J. Respir. Crit. Care Med. 175, 958-966 (2007).
    • (2007) Am. J. Respir. Crit. Care Med , vol.175 , pp. 958-966
    • Maus, U.A.1    Backi, M.2    Winter, C.3
  • 87
    • 25444476969 scopus 로고    scopus 로고
    • THP-1 monocytes up-regulate intercellular adhesion molecule 1 in response to pneumolysin from Streptococcus pnuemoniae
    • Thornton J, McDaniel LS: THP-1 monocytes up-regulate intercellular adhesion molecule 1 in response to pneumolysin from Streptococcus pnuemoniae. Infect. Immun. 73, 6493-6498 (2005).
    • (2005) Infect. Immun , vol.73 , pp. 6493-6498
    • Thornton, J.1    McDaniel, L.S.2
  • 88
    • 0041929522 scopus 로고    scopus 로고
    • Two distinct mechanisms for induction of dendritic cell apoptosis in response to intact Streptococcus pneumoniae
    • Colino J, Snapper CM: Two distinct mechanisms for induction of dendritic cell apoptosis in response to intact Streptococcus pneumoniae. J. Immunol. 174, 2354-2365 (2003).
    • (2003) J. Immunol , vol.174 , pp. 2354-2365
    • Colino, J.1    Snapper, C.M.2
  • 90
    • 14744272986 scopus 로고    scopus 로고
    • Synergistic proinflammatory responses induced by polymicrobial colonization of epithelial surfaces
    • Ratner AJ, Lysenko ES, Paul MN, Weiser JN: Synergistic proinflammatory responses induced by polymicrobial colonization of epithelial surfaces. Proc. Natl Acad. Sci. USA 102, 3429-3434 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 3429-3434
    • Ratner, A.J.1    Lysenko, E.S.2    Paul, M.N.3    Weiser, J.N.4
  • 92
    • 0037103529 scopus 로고    scopus 로고
    • Pneumolysin activates the synthesis and release of interleukin-8 by human neutrophils in vitro
    • Cockeran R, Durandt C, Feldman C, Mitchell TJ, Anderson R: Pneumolysin activates the synthesis and release of interleukin-8 by human neutrophils in vitro. J. Infect. Dis. 186, 562-565 (2002).
    • (2002) J. Infect. Dis , vol.186 , pp. 562-565
    • Cockeran, R.1    Durandt, C.2    Feldman, C.3    Mitchell, T.J.4    Anderson, R.5
  • 93
    • 34548497122 scopus 로고    scopus 로고
    • Presence of nonhemolytic pneumolysin in serotypes of Streptococcus pneumoniae associated with disease outbreaks
    • Jefferies JM, Johnston CH, Kirkham LA et al.: Presence of nonhemolytic pneumolysin in serotypes of Streptococcus pneumoniae associated with disease outbreaks. J. Infect. Dis. 196, 936-944 (2007).
    • (2007) J. Infect. Dis , vol.196 , pp. 936-944
    • Jefferies, J.M.1    Johnston, C.H.2    Kirkham, L.A.3
  • 94
    • 0037378079 scopus 로고    scopus 로고
    • Pneumococcal behavior and host responses during bronchopneumonia are affected differently by the cytolytic and complement-activating activities of pneumolysin
    • Jounblat R, Kadioglu A, Mitchell TJ, Andrew PW: Pneumococcal behavior and host responses during bronchopneumonia are affected differently by the cytolytic and complement-activating activities of pneumolysin. Infect. Immun. 71, 1813-1819 (2003).
    • (2003) Infect. Immun , vol.71 , pp. 1813-1819
    • Jounblat, R.1    Kadioglu, A.2    Mitchell, T.J.3    Andrew, P.W.4
  • 95
    • 0037452778 scopus 로고    scopus 로고
    • Recognition of pneumolysin by Toll-like receptor 4 confers resistance to pneumococcal infection
    • Malley R, Henneke P, Morse SC et al.: Recognition of pneumolysin by Toll-like receptor 4 confers resistance to pneumococcal infection. Proc. Natl Acad. Sci. USA 100, 1966-1971 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1966-1971
    • Malley, R.1    Henneke, P.2    Morse, S.C.3
  • 96
    • 2142763016 scopus 로고    scopus 로고
    • CD4-T-lymphocyte interactions with pneumolysin and pneumococci suggest a crucial protective role in the host response to pneumococcal infection
    • Kadioglu A, Coward W, Colston MJ, Hewitt CR, Andrew PW: CD4-T-lymphocyte interactions with pneumolysin and pneumococci suggest a crucial protective role in the host response to pneumococcal infection. Infect. Immun. 72, 2689-2697 (2004).
    • (2004) Infect. Immun , vol.72 , pp. 2689-2697
    • Kadioglu, A.1    Coward, W.2    Colston, M.J.3    Hewitt, C.R.4    Andrew, P.W.5
  • 97
    • 0036139243 scopus 로고    scopus 로고
    • Induction of gamma interferon and nitric oxide by truncated pneumolysin that lacks pore-forming activity
    • Baba H, Kawamura I, Kohda C et al.: Induction of gamma interferon and nitric oxide by truncated pneumolysin that lacks pore-forming activity. Infect. Immun. 70, 107-113 (2002).
    • (2002) Infect. Immun , vol.70 , pp. 107-113
    • Baba, H.1    Kawamura, I.2    Kohda, C.3
  • 98
    • 25444523483 scopus 로고    scopus 로고
    • The apoptotic response to pneumolysin is Toll-like receptor 4 dependent and protects against pneumococcal disease
    • Srivastava A, Henneke P, Visintin A et al.: The apoptotic response to pneumolysin is Toll-like receptor 4 dependent and protects against pneumococcal disease. Infect. Immun. 73, 6479-6487 (2005).
    • (2005) Infect. Immun , vol.73 , pp. 6479-6487
    • Srivastava, A.1    Henneke, P.2    Visintin, A.3
  • 99
    • 33846518459 scopus 로고    scopus 로고
    • A novel role for IκB kinase WN a and IKKβ in ERK-dependent up-regulation of MUC5AC mucin transcription by Streptococcus pneumoniae
    • Ha U, Lim JH, Jono H et al. A novel role for IκB kinase WN a and IKKβ in ERK-dependent up-regulation of MUC5AC mucin transcription by Streptococcus pneumoniae. J. Immunol. 178, 1736-1747 (2007).
    • (2007) J. Immunol , vol.178 , pp. 1736-1747
    • Ha, U.1    Lim, J.H.2    Jono, H.3
  • 100
    • 0013955508 scopus 로고
    • Bacteriocins of Diplococcus pneumoniae. I. Antagonistic relationships and genetic transformations
    • Mindich L: Bacteriocins of Diplococcus pneumoniae. I. Antagonistic relationships and genetic transformations. J. Bacteriol. 92, 1090-1098 (1966).
    • (1966) J. Bacteriol , vol.92 , pp. 1090-1098
    • Mindich, L.1
  • 101
    • 35648954612 scopus 로고    scopus 로고
    • Diversity of bacteriocins and activity spectrum in Streptococcus pneumoniae
    • Lux T, Nuhn M, Hakenbeck R, Reichmann P: Diversity of bacteriocins and activity spectrum in Streptococcus pneumoniae. J. Bacteriol. 189, 7741-7751 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 7741-7751
    • Lux, T.1    Nuhn, M.2    Hakenbeck, R.3    Reichmann, P.4
  • 102
    • 33846031140 scopus 로고    scopus 로고
    • The blp bacteriocins of Streptococcus pneumoniae mediate intraspecies competition both in vitro and in vivo
    • Dawid S, Roche AM, Weiser JN: The blp bacteriocins of Streptococcus pneumoniae mediate intraspecies competition both in vitro and in vivo. Infect. Immun. 75, 443-451 (2007).
    • (2007) Infect. Immun , vol.75 , pp. 443-451
    • Dawid, S.1    Roche, A.M.2    Weiser, J.N.3
  • 103
    • 0033888896 scopus 로고    scopus 로고
    • Microarray-based identification of a novel Streptococcus pneumoniae regulon controlled by an autoinduced peptide
    • de Saizieu A, Gardes C, Flint N et al.: Microarray-based identification of a novel Streptococcus pneumoniae regulon controlled by an autoinduced peptide. J. Bacteriol. 182, 4696-4703 (2000).
    • (2000) J. Bacteriol , vol.182 , pp. 4696-4703
    • de Saizieu, A.1    Gardes, C.2    Flint, N.3
  • 104
    • 16544367143 scopus 로고    scopus 로고
    • Extracellular-peptide control of competence for genetic transformation in Streptococcus pneumoniae
    • Claverys JP, Havarstein LS: Extracellular-peptide control of competence for genetic transformation in Streptococcus pneumoniae. Front Biosci. 7, D1798-D1814 (2002).
    • (2002) Front Biosci , vol.7
    • Claverys, J.P.1    Havarstein, L.S.2
  • 105
    • 0028845364 scopus 로고
    • An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae
    • Havarstein LS, Coomaraswamy G, Morrison DA: An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae. Proc. Natl Acad. Sci. USA 92, 11140-11144 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11140-11144
    • Havarstein, L.S.1    Coomaraswamy, G.2    Morrison, D.A.3
  • 106
    • 33645081479 scopus 로고    scopus 로고
    • New insights into the pneumococcal fratricide: Relationship to clumping and identification of a novel immunity factor
    • Havarstein LS, Martin B, Johnsborg O, Granadel C, Claverys JP: New insights into the pneumococcal fratricide: relationship to clumping and identification of a novel immunity factor. Mol. Microbiol. 59, 1297-1307 (2006).
    • (2006) Mol. Microbiol , vol.59 , pp. 1297-1307
    • Havarstein, L.S.1    Martin, B.2    Johnsborg, O.3    Granadel, C.4    Claverys, J.P.5
  • 107
    • 22144435935 scopus 로고    scopus 로고
    • Co-ordinated bacteriocin production and competence development: A possible mechanism for taking up DNA from neighbouring species
    • Kreth J, Merritt J, Shi W, Qi F: Co-ordinated bacteriocin production and competence development: a possible mechanism for taking up DNA from neighbouring species. Mol. Microbiol. 57, 392-404 (2005).
    • (2005) Mol. Microbiol , vol.57 , pp. 392-404
    • Kreth, J.1    Merritt, J.2    Shi, W.3    Qi, F.4
  • 108
    • 7644243116 scopus 로고    scopus 로고
    • Release of DNA into the medium by competent Streptococcus pneumoniae: Kinetics, mechanism and stability of the liberated DNA
    • Moscoso M, Claverys JP: Release of DNA into the medium by competent Streptococcus pneumoniae: kinetics, mechanism and stability of the liberated DNA. Mol. Microbiol. 54, 783-794 (2004).
    • (2004) Mol. Microbiol , vol.54 , pp. 783-794
    • Moscoso, M.1    Claverys, J.P.2
  • 109
    • 21144431739 scopus 로고    scopus 로고
    • Choline-binding protein D (CbpD) in Streptococcus pneumoniae is essential for competence-induced cell lysis
    • Kausmally L, Johnsborg O, Lunde M, Knutsen E, Havarstein LS: Choline-binding protein D (CbpD) in Streptococcus pneumoniae is essential for competence-induced cell lysis. J. Bacteriol. 187, 4338-4435 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 4338-4435
    • Kausmally, L.1    Johnsborg, O.2    Lunde, M.3    Knutsen, E.4    Havarstein, L.S.5
  • 110
    • 0037188501 scopus 로고    scopus 로고
    • Induction of natural competence in Streptococcus pneumoniae triggers lysis and DNA release from a subfraction of the cell population
    • Steinmoen H, Knutsen E, Havarstein LS: Induction of natural competence in Streptococcus pneumoniae triggers lysis and DNA release from a subfraction of the cell population. Proc. Natl Acad. Sci. USA 99, 7681-7686 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7681-7686
    • Steinmoen, H.1    Knutsen, E.2    Havarstein, L.S.3
  • 111
    • 35948931348 scopus 로고    scopus 로고
    • Pneumococcal LytA autolysin, a potent therapeutic agent in experimental peritonitis-sepsis caused by highly betalactam-resistant Streptococcus pneumoniae
    • Rodriguez-Cerrato V, Garcia P, Huelves L et al.: Pneumococcal LytA autolysin, a potent therapeutic agent in experimental peritonitis-sepsis caused by highly betalactam-resistant Streptococcus pneumoniae. Antimicrob. Agents Chemother. 51, 3371-3373 (2007).
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 3371-3373
    • Rodriguez-Cerrato, V.1    Garcia, P.2    Huelves, L.3
  • 112
    • 33751119902 scopus 로고    scopus 로고
    • Biofilm formation by Streptococcus pneumoniae: Role of choline, extracellular DNA, and capsular polysaccharide In microbial accretion
    • Moscoso M, Garcia E, Lopez R: Biofilm formation by Streptococcus pneumoniae: role of choline, extracellular DNA, and capsular polysaccharide In microbial accretion. J. Bacteriol. 188, 7785-7795 (2006).
    • (2006) J. Bacteriol , vol.188 , pp. 7785-7795
    • Moscoso, M.1    Garcia, E.2    Lopez, R.3
  • 113
    • 8744303083 scopus 로고    scopus 로고
    • Is autoinducer-2 a universal signal for interspecies communication: A comparative genomic and phylogenetic analysis of the synthesis and signal transduction pathways
    • Sun J, Daniel R, Wagner-Dobler I, Zeng AP: Is autoinducer-2 a universal signal for interspecies communication: a comparative genomic and phylogenetic analysis of the synthesis and signal transduction pathways. BMC Evol. Biol. 4, 36 (2004).
    • (2004) BMC Evol. Biol , vol.4 , pp. 36
    • Sun, J.1    Daniel, R.2    Wagner-Dobler, I.3    Zeng, A.P.4
  • 114
    • 0038104847 scopus 로고    scopus 로고
    • Mutation of luxS of Streptococcus pneumoniae affects virulence in a mouse model
    • Stroeher UH, Paton AW, Ogunniyi AD, Paton JC: Mutation of luxS of Streptococcus pneumoniae affects virulence in a mouse model. Infect. Immun. 71, 3206-3212 (2003).
    • (2003) Infect. Immun , vol.71 , pp. 3206-3212
    • Stroeher, U.H.1    Paton, A.W.2    Ogunniyi, A.D.3    Paton, J.C.4
  • 115
    • 32244442842 scopus 로고    scopus 로고
    • LuxS impacts on LytA- dependent autolysis and on competence in Streprococcus pneumoniae
    • Romao S, Memmi G, Oggioni MR, Trombe MC: LuxS impacts on LytA- dependent autolysis and on competence in Streprococcus pneumoniae. Microbiology 152, 333-341 (2006).
    • (2006) Microbiology , vol.152 , pp. 333-341
    • Romao, S.1    Memmi, G.2    Oggioni, M.R.3    Trombe, M.C.4
  • 116
    • 2142649224 scopus 로고    scopus 로고
    • LuxS is required for persistent pneumococcal carriage and expression of virulence and biosynthesis genes
    • Joyce EA, Kawale A, Censini, S, Kim CC, Covacci A, Falkow S: LuxS is required for persistent pneumococcal carriage and expression of virulence and biosynthesis genes. Infect. Immun. 72, 2964-2975 (2004).
    • (2004) Infect. Immun , vol.72 , pp. 2964-2975
    • Joyce, E.A.1    Kawale, A.2    Censini, S.3    Kim, C.C.4    Covacci, A.5    Falkow, S.6
  • 117
    • 33846898975 scopus 로고    scopus 로고
    • Toll-like receptor 9 acts at an early stage in host defence against pneumococcal infection
    • Albiger B, Dahlberg S, Sandgren A et al.: Toll-like receptor 9 acts at an early stage in host defence against pneumococcal infection. Cell Microbiol. 9, 633-644 (2007).
    • (2007) Cell Microbiol , vol.9 , pp. 633-644
    • Albiger, B.1    Dahlberg, S.2    Sandgren, A.3
  • 118
    • 1542287347 scopus 로고    scopus 로고
    • Neutrophil extracellular traps kill bacteria
    • Brinkmann V, Reichard U, Goosmann C et al.: Neutrophil extracellular traps kill bacteria. Science 303, 1532-1535 (2004).
    • (2004) Science , vol.303 , pp. 1532-1535
    • Brinkmann, V.1    Reichard, U.2    Goosmann, C.3
  • 119
    • 34047259058 scopus 로고    scopus 로고
    • Capsule and D-alanylated lipoteichoic acids protect Streptococcus pneumoniae against neutrophil extracellular traps
    • Wartha F, Beiter K, Albiger B et al.: Capsule and D-alanylated lipoteichoic acids protect Streptococcus pneumoniae against neutrophil extracellular traps. Cell Microbiol. 9, 1162-1171 (2007).
    • (2007) Cell Microbiol , vol.9 , pp. 1162-1171
    • Wartha, F.1    Beiter, K.2    Albiger, B.3
  • 120
  • 121
    • 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
    • Kovacs M, Halfmann A, Fedtke I et al.: 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).
    • (2006) J. Bacteriol , vol.188 , pp. 5797-5805
    • Kovacs, M.1    Halfmann, A.2    Fedtke, I.3
  • 122
    • 0033945724 scopus 로고    scopus 로고
    • Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract
    • Pericone CD, Overweg K, Hermans PW, Weiser JN: Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract. Infect. Immun. 68, 3990-3997 (2000).
    • (2000) Infect. Immun , vol.68 , pp. 3990-3997
    • Pericone, C.D.1    Overweg, K.2    Hermans, P.W.3    Weiser, J.N.4
  • 123
    • 0027377225 scopus 로고
    • Identification of hydrogen peroxide as a Streptococcus pneumoniae toxin for rat alveolar epithelial cells
    • Duane PG, Rubins A Weisel HR, Janoff EN: Identification of hydrogen peroxide as a Streptococcus pneumoniae toxin for rat alveolar epithelial cells. Infect. Immun. 61, 4392-4397 (1993).
    • (1993) Infect. Immun , vol.61 , pp. 4392-4397
    • Duane, P.G.1    Rubins, A.2    Weisel, H.R.3    Janoff, E.N.4
  • 124
    • 0034098917 scopus 로고    scopus 로고
    • Role of manganese-containing superoxide dismutase in oxidative stress and virulence of Streptococcus pneumoniae
    • Yesilkaya H, Kadioglu A, Gingles N, Alexander JE, Mitchell TJ, Andrew PW: Role of manganese-containing superoxide dismutase in oxidative stress and virulence of Streptococcus pneumoniae. Infect. Immun. 68, 2819-2826 (2000).
    • (2000) Infect. Immun , vol.68 , pp. 2819-2826
    • Yesilkaya, H.1    Kadioglu, A.2    Gingles, N.3    Alexander, J.E.4    Mitchell, T.J.5    Andrew, P.W.6
  • 125
    • 0036178058 scopus 로고    scopus 로고
    • Virulence of Streptococcus pneumoniae: PsaA mutants are hypersensitive to oxidative stress
    • Tseng HJ, McEwan AG, Paton JC, Jennings MP: Virulence of Streptococcus pneumoniae: PsaA mutants are hypersensitive to oxidative stress. Infect. Immun. 70, 1635-1639 (2002).
    • (2002) Infect. Immun , vol.70 , pp. 1635-1639
    • Tseng, H.J.1    McEwan, A.G.2    Paton, J.C.3    Jennings, M.P.4
  • 126
    • 0345687929 scopus 로고    scopus 로고
    • Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the fenton reaction
    • Pericone CD, Park S, Imlay A Weiser JN: Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the fenton reaction. J. Bacteriol. 185, 6815-6825 (2003).
    • (2003) J. Bacteriol , vol.185 , pp. 6815-6825
    • Pericone, C.D.1    Park, S.2    Imlay, A.3    Weiser, J.N.4
  • 127
    • 34548583324 scopus 로고    scopus 로고
    • SpxB is a suicide gene of Steptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model
    • Regev-Yochay G, Trzcinski K, Thompson CM, Lipsitch M, Malley R: SpxB is a suicide gene of Steptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model. J. Bacteriol. 189, 6532-6539 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 6532-6539
    • Regev-Yochay, G.1    Trzcinski, K.2    Thompson, C.M.3    Lipsitch, M.4    Malley, R.5
  • 128
    • 33745460121 scopus 로고    scopus 로고
    • Interference between Streptococcus pneumoniae and Staphylococcus aureus: In vitro hydrogen peroxide-mediated killing by Streptococcus pneumoniae
    • Regev-Yochay G, Trzcinski K, Thompson CM, Malley R, Lipsitch M: Interference between Streptococcus pneumoniae and Staphylococcus aureus: In vitro hydrogen peroxide-mediated killing by Streptococcus pneumoniae. J Bacteriol. 188, 4996-5001 (2006).
    • (2006) J Bacteriol , vol.188 , pp. 4996-5001
    • Regev-Yochay, G.1    Trzcinski, K.2    Thompson, C.M.3    Malley, R.4    Lipsitch, M.5
  • 129
    • 33645300106 scopus 로고    scopus 로고
    • An operun in Streptococcus pneumoniae containing a putative alkylhydroperoxidase D homologue contributes to virulence and the response to oxidative stress
    • Paterson GK, Blue CE, Mitchell TJ: An operun in Streptococcus pneumoniae containing a putative alkylhydroperoxidase D homologue contributes to virulence and the response to oxidative stress. Microb. Pathog. 40, 152-160 (2006).
    • (2006) Microb. Pathog , vol.40 , pp. 152-160
    • Paterson, G.K.1    Blue, C.E.2    Mitchell, T.J.3
  • 130
    • 0038649846 scopus 로고    scopus 로고
    • Effect of heat shock and mutations in C1pL and C1pP on virulence gene expression in Streptococcus pneumoniae
    • Kwon HY, Kim SW, Choi MH et al.: Effect of heat shock and mutations in C1pL and C1pP on virulence gene expression in Streptococcus pneumoniae. Infect. Immun. 71, 3757-3765 (2003).
    • (2003) Infect. Immun , vol.71 , pp. 3757-3765
    • Kwon, H.Y.1    Kim, S.W.2    Choi, M.H.3
  • 131
    • 4644372119 scopus 로고    scopus 로고
    • The C1pP protease of Streptococcus pneumoniae modulates virulence gene expression and protects against fatal pneumococcal challenge
    • Kwon HY, Ogunniyi AD, Choi MH, Pyo SN, Rhee DK, Paton JC: The C1pP protease of Streptococcus pneumoniae modulates virulence gene expression and protects against fatal pneumococcal challenge. Infect. Immun. 72, 5646-5653 (2004).
    • (2004) Infect. Immun , vol.72 , pp. 5646-5653
    • Kwon, H.Y.1    Ogunniyi, A.D.2    Choi, M.H.3    Pyo, S.N.4    Rhee, D.K.5    Paton, J.C.6
  • 132
    • 0036279922 scopus 로고    scopus 로고
    • Global transcriptional analysis of c1pP mutations of type 2 Streptococcus pneumoniae and their effects on physiology and virulence
    • Robertson GT, Ng WL, Foley J, Gilmour R, Winkler ME: Global transcriptional analysis of c1pP mutations of type 2 Streptococcus pneumoniae and their effects on physiology and virulence. J Bacteriol. 184, 3508-3520 (2002).
    • (2002) J Bacteriol , vol.184 , pp. 3508-3520
    • Robertson, G.T.1    Ng, W.L.2    Foley, J.3    Gilmour, R.4    Winkler, M.E.5
  • 133
    • 34249893901 scopus 로고    scopus 로고
    • Modulation of adherence, invasion, and tumor necrosis factor alpha secretion during the early stages of infection by Streptococcus pneumoniae C1pL
    • Tu le N, Jeong HY, Kwon HY et al.: Modulation of adherence, invasion, and tumor necrosis factor alpha secretion during the early stages of infection by Streptococcus pneumoniae C1pL. Infect. Immun. 75, 2996-3005 (2007).
    • (2007) Infect. Immun , vol.75 , pp. 2996-3005
    • Tu le, N.1    Jeong, H.Y.2    Kwon, H.Y.3
  • 134
    • 0034674165 scopus 로고    scopus 로고
    • Mechanism of hyaluronan binding and degradation: Structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 A resolution
    • Ponnuraj K, Jedrzejas MJ: Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 A resolution. J. Mol. Biol. 299, 885-895 (2000).
    • (2000) J. Mol. Biol , vol.299 , pp. 885-895
    • Ponnuraj, K.1    Jedrzejas, M.J.2
  • 135
    • 38549174180 scopus 로고    scopus 로고
    • Unveiling molecular mechanisms of bacterial surface proteins: Streatacoccus pneumoniae as a model organism for structural studies
    • Jedrzejas MJ: Unveiling molecular mechanisms of bacterial surface proteins: Streatacoccus pneumoniae as a model organism for structural studies. Cell Mol. Life Sci. 64(21), 2799-2822 (2007).
    • (2007) Cell Mol. Life Sci , vol.64 , Issue.21 , pp. 2799-2822
    • Jedrzejas, M.J.1
  • 137
    • 0036047758 scopus 로고    scopus 로고
    • Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors
    • Hava DL, Camilli A: Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors. Mol. Microbiol. 45, 1389-1406 (2002).
    • (2002) Mol. Microbiol , vol.45 , pp. 1389-1406
    • Hava, D.L.1    Camilli, A.2
  • 138
    • 33645087140 scopus 로고    scopus 로고
    • Deglycosylation of human glycoconjugates by the sequential activities of exoglycosidases expressed by Streptococcus pneumoniae
    • King SJ, Hippe KR, Weiser JN: Deglycosylation of human glycoconjugates by the sequential activities of exoglycosidases expressed by Streptococcus pneumoniae. Mol. Microbiol. 59, 961-974 (2006).
    • (2006) Mol. Microbiol , vol.59 , pp. 961-974
    • King, S.J.1    Hippe, K.R.2    Weiser, J.N.3
  • 139
    • 0034442654 scopus 로고    scopus 로고
    • Antigenicity, expression, and molecular characterization of surface-located pullulanase of Streptococcus pneumoniae
    • Bongaerts RJ, Heinz HE Hadding U, Zysk G: Antigenicity, expression, and molecular characterization of surface-located pullulanase of Streptococcus pneumoniae. Infect. Immun. 68, 7141-7143 (2000).
    • (2000) Infect. Immun , vol.68 , pp. 7141-7143
    • Bongaerts, R.J.1    Heinz, H.E.2    Hadding, U.3    Zysk, G.4
  • 140
    • 33846096051 scopus 로고    scopus 로고
    • Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors
    • van Bueren AL, Higgins M, Wang D, Burke RD, Boraston AB: Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors. Nat. Struct. Mol. Biol. 14, 76-84 (2007).
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 76-84
    • van Bueren, A.L.1    Higgins, M.2    Wang, D.3    Burke, R.D.4    Boraston, A.B.5


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