메뉴 건너뛰기




Volumn 98, Issue 3, 2007, Pages 488-496

Invasion mechanisms of Gram-positive pathogenic cocci

Author keywords

Internalisation; Invasion; Pathogenesis; Staphylococcus; Streptococcus

Indexed keywords

ADHESIN; ALPHA 2 ANTIPLASMIN; ALPHA 2 MACROGLOBULIN; ALPHA ENOLASE; ANTIBIOTIC AGENT; CAVEOLIN 1; ENZYME PRECURSOR; FIBRIN; FIBRONECTIN; FOCAL ADHESION KINASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; INTEGRIN; INVASIN; LAMININ; LIPOTEICHOIC ACID; M PROTEIN; PAXILLIN; PLASMIN; PLASMINOGEN; PROTEIN CDC42; PROTEIN KINASE FYN; PROTEIN KINASE YES; RAB7 PROTEIN; RAC PROTEIN; STAPHYLOKINASE; STREPTOKINASE; TEICHOIC ACID; THROMBOSPONDIN; UNINDEXED DRUG; VITRONECTIN;

EID: 34548663903     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH07-03-0179     Document Type: Article
Times cited : (57)

References (132)
  • 1
    • 84884464032 scopus 로고    scopus 로고
    • Extracellular matrix interaction with Gram-positive bacteria
    • Washington, D.C, ASM Press;
    • Chhatwal GS, Preissner KT. Extracellular matrix interaction with Gram-positive bacteria. In: Gram-positive pathognes. Washington, D.C.: ASM Press; 2006: 89-99.
    • (2006) Gram-positive pathognes , pp. 89-99
    • Chhatwal, G.S.1    Preissner, K.T.2
  • 2
    • 0036266507 scopus 로고    scopus 로고
    • Molecular mechanisms of adhesion, colonization, and invasion of group A streptococci
    • Courtney HS, Hasty DL, Dale JB. Molecular mechanisms of adhesion, colonization, and invasion of group A streptococci. Ann Med 2002; 34: 77-87.
    • (2002) Ann Med , vol.34 , pp. 77-87
    • Courtney, H.S.1    Hasty, D.L.2    Dale, J.B.3
  • 3
    • 31844452509 scopus 로고    scopus 로고
    • Sticky connections: Extracellular matrix protein recognition and integrin-mediated cellular invasion by Staphylococcus aureus
    • Hauck CR, Ohlsen K. Sticky connections: extracellular matrix protein recognition and integrin-mediated cellular invasion by Staphylococcus aureus. Curr Opin Microbiol 2006; 9: 5-11.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 5-11
    • Hauck, C.R.1    Ohlsen, K.2
  • 4
    • 23744478147 scopus 로고    scopus 로고
    • Mechanism and consequences of invasion of endothelial cells by Staphylococcus aureus
    • Sinha B, Herrmann M. Mechanism and consequences of invasion of endothelial cells by Staphylococcus aureus. Thromb Haemost 2005; 94: 266-277.
    • (2005) Thromb Haemost , vol.94 , pp. 266-277
    • Sinha, B.1    Herrmann, M.2
  • 5
    • 0030158265 scopus 로고    scopus 로고
    • Staphylococcus aureus invasion of bovine mammary epithelial cells
    • Almeida RA, Matthews KR, Cifrian E, et al. Staphylococcus aureus invasion of bovine mammary epithelial cells. J Dairy Sci 1996; 79: 1021-1026.
    • (1996) J Dairy Sci , vol.79 , pp. 1021-1026
    • Almeida, R.A.1    Matthews, K.R.2    Cifrian, E.3
  • 7
    • 0026723654 scopus 로고
    • Conspicuous ingestion of Staphylococcus aureus organisms by murine fibroblasts in vitro
    • Usui A, Murai M, Seki K, et al. Conspicuous ingestion of Staphylococcus aureus organisms by murine fibroblasts in vitro. Microbiol Immunol 1992; 36: 545-550.
    • (1992) Microbiol Immunol , vol.36 , pp. 545-550
    • Usui, A.1    Murai, M.2    Seki, K.3
  • 8
    • 0017228323 scopus 로고
    • Epithelial cell binding of group A streptococci by lipoteichoic acid on fimbriae denuded of M protein
    • Beachey EH, Ofek I. Epithelial cell binding of group A streptococci by lipoteichoic acid on fimbriae denuded of M protein. J Exp Med 1976; 143: 759-771.
    • (1976) J Exp Med , vol.143 , pp. 759-771
    • Beachey, E.H.1    Ofek, I.2
  • 9
    • 0025096419 scopus 로고
    • Streptococcus pyogenes clinical isolates and lipoteichoic acid
    • Leon O, Panes C. Streptococcus pyogenes clinical isolates and lipoteichoic acid. Infect Immun 1990; 58: 3779-3787.
    • (1990) Infect Immun , vol.58 , pp. 3779-3787
    • Leon, O.1    Panes, C.2
  • 10
    • 0026829655 scopus 로고
    • Lipoteichoic acid and M protein: Dual adhesins of group A streptococci
    • Courtney HS, von Hunolstein C, Dale JB, et al. Lipoteichoic acid and M protein: dual adhesins of group A streptococci. Microb Pathog 1992; 12: 199-208.
    • (1992) Microb Pathog , vol.12 , pp. 199-208
    • Courtney, H.S.1    von Hunolstein, C.2    Dale, J.B.3
  • 11
    • 0025728238 scopus 로고
    • Aggregation of group A streptococci by human saliva and effect of saliva on streptococcal adherence to host cells
    • Courtney HS, Hasty DL. Aggregation of group A streptococci by human saliva and effect of saliva on streptococcal adherence to host cells. Infect Immun 1991; 59: 1661-1666.
    • (1991) Infect Immun , vol.59 , pp. 1661-1666
    • Courtney, H.S.1    Hasty, D.L.2
  • 12
    • 2342639647 scopus 로고    scopus 로고
    • Role of teichoic acids in Staphylococcus aureus nasal colonization, a major risk factor in nosocomial infections
    • Weidenmaier C, Kokai-Kun JF, Kristian SA, et al. Role of teichoic acids in Staphylococcus aureus nasal colonization, a major risk factor in nosocomial infections. Nat Med 2004; 10: 243-245.
    • (2004) Nat Med , vol.10 , pp. 243-245
    • Weidenmaier, C.1    Kokai-Kun, J.F.2    Kristian, S.A.3
  • 13
    • 18544385333 scopus 로고    scopus 로고
    • Lack of wall teichoic acids in Staphylococcus aureus leads to reduced interactions with endothelial cells and to attenuated virulence in a rabbit model of endocarditis
    • Weidenmaier C, Peschel A, Xiong YQ, et al. Lack of wall teichoic acids in Staphylococcus aureus leads to reduced interactions with endothelial cells and to attenuated virulence in a rabbit model of endocarditis. J Infect Dis 2005; 191: 1771-1777.
    • (2005) J Infect Dis , vol.191 , pp. 1771-1777
    • Weidenmaier, C.1    Peschel, A.2    Xiong, Y.Q.3
  • 14
    • 0020700981 scopus 로고
    • Adherence of group A streptococci to fibronectin on oral epithelial cells
    • Simpson WA, Beachey EH. Adherence of group A streptococci to fibronectin on oral epithelial cells. Infect Immun 1983; 39: 275-279.
    • (1983) Infect Immun , vol.39 , pp. 275-279
    • Simpson, W.A.1    Beachey, E.H.2
  • 15
    • 0026696227 scopus 로고
    • Multiple adhesins of streptococci
    • Hasty DL, Ofek I, Courtney HS, et al. Multiple adhesins of streptococci. Infect Immun 1992; 60: 2147-2152.
    • (1992) Infect Immun , vol.60 , pp. 2147-2152
    • Hasty, D.L.1    Ofek, I.2    Courtney, H.S.3
  • 16
    • 0037381631 scopus 로고    scopus 로고
    • Molecular basis of group A streptococcal virulence
    • Bisno AL, Brito MO, Collins CM. Molecular basis of group A streptococcal virulence. Lancet Infect Dis 2003; 3: 191-200.
    • (2003) Lancet Infect Dis , vol.3 , pp. 191-200
    • Bisno, A.L.1    Brito, M.O.2    Collins, C.M.3
  • 17
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham MW. Pathogenesis of group A streptococcal infections. Clin Microbiol Rev 2000; 13: 470-511.
    • (2000) Clin Microbiol Rev , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 18
    • 0024412074 scopus 로고
    • Streptococcal M protein: Molecular design and biological behavior
    • Fischetti VA. Streptococcal M protein: molecular design and biological behavior. Clin Microbiol Rev 1989; 2: 285-314.
    • (1989) Clin Microbiol Rev , vol.2 , pp. 285-314
    • Fischetti, V.A.1
  • 19
    • 0001197006 scopus 로고
    • Current knowledge of type-specific M antigens of group A streptococci
    • Lancefield RC. Current knowledge of type-specific M antigens of group A streptococci. J Immunol 1962; 89: 307-313.
    • (1962) J Immunol , vol.89 , pp. 307-313
    • Lancefield, R.C.1
  • 20
    • 0015978213 scopus 로고
    • Parameters affecting the adherence and tissue tropisms of Streptococcus pyogenes
    • Ellen RP, Gibbons RJ. Parameters affecting the adherence and tissue tropisms of Streptococcus pyogenes. Infect Immun 1974; 9: 85-91.
    • (1974) Infect Immun , vol.9 , pp. 85-91
    • Ellen, R.P.1    Gibbons, R.J.2
  • 21
    • 0015334543 scopus 로고
    • M protein-associated adherence of Streptococcus pyogenes to epithelial surfaces: Prerequisite for virulence
    • Ellen RP, Gibbons RJ. M protein-associated adherence of Streptococcus pyogenes to epithelial surfaces: prerequisite for virulence. Infect Immun 1972; 5: 826-830.
    • (1972) Infect Immun , vol.5 , pp. 826-830
    • Ellen, R.P.1    Gibbons, R.J.2
  • 22
    • 34548703248 scopus 로고    scopus 로고
    • Nitsche-Schmitz DP, Rohde M, Chhatwal GS. Adhesion and Invasion of Streptococci in Eukaryotic Cells. Norwich, U. K. Horizon Bioscience; 2007.
    • Nitsche-Schmitz DP, Rohde M, Chhatwal GS. Adhesion and Invasion of Streptococci in Eukaryotic Cells. Norwich, U. K. Horizon Bioscience; 2007.
  • 23
    • 85047691958 scopus 로고    scopus 로고
    • Rheumatic fever-associated Streptococcus pyogenes isolates aggregate collagen
    • Dinkla K, Rohde M, Jansen WT, et al. Rheumatic fever-associated Streptococcus pyogenes isolates aggregate collagen. J Clin Invest 2003; 111: 1905-1912.
    • (2003) J Clin Invest , vol.111 , pp. 1905-1912
    • Dinkla, K.1    Rohde, M.2    Jansen, W.T.3
  • 24
    • 33644968057 scopus 로고    scopus 로고
    • Streptococcal protein FOG, a novel matrix adhesin interacting with collagen I in vivo
    • Nitsche DP, Johansson HM, Frick IM, et al. Streptococcal protein FOG, a novel matrix adhesin interacting with collagen I in vivo. J Biol Chem 2006; 281: 1670-1679.
    • (2006) J Biol Chem , vol.281 , pp. 1670-1679
    • Nitsche, D.P.1    Johansson, H.M.2    Frick, I.M.3
  • 25
    • 2942529092 scopus 로고    scopus 로고
    • Virulence potential of the staphylococcal adhesin CNA in experimental arthritis is determined by its affinity for collagen
    • Xu Y, Rivas JM, Brown EL, et al. Virulence potential of the staphylococcal adhesin CNA in experimental arthritis is determined by its affinity for collagen. J Infect Dis 2004; 189: 2323-2333.
    • (2004) J Infect Dis , vol.189 , pp. 2323-2333
    • Xu, Y.1    Rivas, J.M.2    Brown, E.L.3
  • 26
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti E, Pierschbacher MD. New perspectives in cell adhesion: RGD and integrins. Science 1987; 238: 491-497.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 27
    • 0033791977 scopus 로고    scopus 로고
    • Staphylococcal fibronectin binding protein interacts with heat shock protein 60 and integrins: Role in internalization by epithelial cells
    • Dziewanowska K, Carson AR, Patti JM, et al. Staphylococcal fibronectin binding protein interacts with heat shock protein 60 and integrins: role in internalization by epithelial cells. Infect Immun 2000; 68: 6321-6328.
    • (2000) Infect Immun , vol.68 , pp. 6321-6328
    • Dziewanowska, K.1    Carson, A.R.2    Patti, J.M.3
  • 28
    • 0034443264 scopus 로고    scopus 로고
    • Heterologously expressed Staphylococcus aureus fibronectin-binding proteins are sufficient for invasion of host cells
    • Sinha B, Francois P, Que YA, et al. Heterologously expressed Staphylococcus aureus fibronectin-binding proteins are sufficient for invasion of host cells. Infect Immun 2000; 68: 6871-6878.
    • (2000) Infect Immun , vol.68 , pp. 6871-6878
    • Sinha, B.1    Francois, P.2    Que, Y.A.3
  • 29
    • 0033643410 scopus 로고    scopus 로고
    • High frequency invasion of mammalian cells by beta hemolytic streptococci
    • Cleary PP, Cue D. High frequency invasion of mammalian cells by beta hemolytic streptococci. Sub-cell Biochem 2000; 33: 137-166.
    • (2000) Sub-cell Biochem , vol.33 , pp. 137-166
    • Cleary, P.P.1    Cue, D.2
  • 30
    • 0034646204 scopus 로고    scopus 로고
    • A nonpeptide integrin antagonist can inhibit epithelial cell ingestion of Streptococcus pyogenes by blocking formation of integrin alpha 5beta 1-fibronectin-M1 protein complexes
    • Cue D, Southern SO, Southern PJ, et al. A nonpeptide integrin antagonist can inhibit epithelial cell ingestion of Streptococcus pyogenes by blocking formation of integrin alpha 5beta 1-fibronectin-M1 protein complexes. Proc Natl Acad Sci USA 2000; 97: 2858-2863.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2858-2863
    • Cue, D.1    Southern, S.O.2    Southern, P.J.3
  • 31
    • 0033754023 scopus 로고    scopus 로고
    • Cellular invasion by Staphylococcus aureus involves a fibronectin bridge between the bacterial fibronectin-binding MSCRAMMs and host cell beta1 integrins
    • Fowler T, Wann ER, Joh D, et al. Cellular invasion by Staphylococcus aureus involves a fibronectin bridge between the bacterial fibronectin-binding MSCRAMMs and host cell beta1 integrins. Eur J Cell Biol 2000; 79: 672-679.
    • (2000) Eur J Cell Biol , vol.79 , pp. 672-679
    • Fowler, T.1    Wann, E.R.2    Joh, D.3
  • 32
    • 0030903802 scopus 로고    scopus 로고
    • The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells
    • Molinari G, Talay SR, Valentin-Weigand P, et al. The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells. Infect Immun 1997; 65: 1357-1363.
    • (1997) Infect Immun , vol.65 , pp. 1357-1363
    • Molinari, G.1    Talay, S.R.2    Valentin-Weigand, P.3
  • 33
    • 0034524338 scopus 로고    scopus 로고
    • Co-operative binding of human fibronectin to Sfb1 protein triggers streptococcal invasion into respiratory epithelial cells
    • Talay SR, Zock A, Rohde M, et al. Co-operative binding of human fibronectin to Sfb1 protein triggers streptococcal invasion into respiratory epithelial cells. Cell Microbiol 2000; 2: 521-535.
    • (2000) Cell Microbiol , vol.2 , pp. 521-535
    • Talay, S.R.1    Zock, A.2    Rohde, M.3
  • 34
    • 21244444520 scopus 로고    scopus 로고
    • Is plasminogen deployed as a Streptococcus pyogenes virulence factor?
    • Walker MJ, McArthur JD, McKay F, et al. Is plasminogen deployed as a Streptococcus pyogenes virulence factor? Trends Microbiol 2005; 13: 308-313.
    • (2005) Trends Microbiol , vol.13 , pp. 308-313
    • Walker, M.J.1    McArthur, J.D.2    McKay, F.3
  • 35
    • 0027451350 scopus 로고    scopus 로고
    • PAM, a novel plasminogen-binding protein from Streptococcus pyogenes
    • Berge A, Sjöbring U. PAM, a novel plasminogen-binding protein from Streptococcus pyogenes. J Biol Chem l993; 268: 25417-25424.
    • J Biol Chem l993 , vol.268 , pp. 25417-25424
    • Berge, A.1    Sjöbring, U.2
  • 36
    • 0032486286 scopus 로고    scopus 로고
    • alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi V, Fischetti VA. alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J Biol Chem 1998; 273: 14503-14515.
    • (1998) J Biol Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 37
    • 0027249488 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme
    • Pancholi V, Fischetti VA. Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme. Proc Natl Acad Sci USA 1993; 90: 8154-8158.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8154-8158
    • Pancholi, V.1    Fischetti, V.A.2
  • 38
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann S, Rohde M, Hammerschmidt S. Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein. Infect Immun 2004; 72: 2416-2419.
    • (2004) Infect Immun , vol.72 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 39
    • 0034931519 scopus 로고    scopus 로고
    • alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on die bacterial cell surface
    • Bergmann S, Rohde M, Chhatwal GS, et al. alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on die bacterial cell surface. Mol Microbiol 2001; 40: 1273-1287.
    • (2001) Mol Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3
  • 40
    • 23744464766 scopus 로고    scopus 로고
    • The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration
    • Bergmann S, Rohde M, Preissner KT, et al. The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration. Thromb Haemost 2005; 94: 304-311.
    • (2005) Thromb Haemost , vol.94 , pp. 304-311
    • Bergmann, S.1    Rohde, M.2    Preissner, K.T.3
  • 42
    • 0026501830 scopus 로고
    • Tissue-type plasminogen activator-mediated activation of plasminogen on the surface of group A, C, and G streptococci
    • Kuusela P, Ullberg M, Saksela O, et al. Tissue-type plasminogen activator-mediated activation of plasminogen on the surface of group A, C, and G streptococci. Infect Immun 1992; 60: 196-201.
    • (1992) Infect Immun , vol.60 , pp. 196-201
    • Kuusela, P.1    Ullberg, M.2    Saksela, O.3
  • 43
    • 0041440157 scopus 로고    scopus 로고
    • Plasminogen enhances virulence of group A streptococci by streptokinase-dependent and streptokinase-independent mechanisms
    • Khil J, Im M, Heath A, et al. Plasminogen enhances virulence of group A streptococci by streptokinase-dependent and streptokinase-independent mechanisms. J Infect Dis 2003; 188: 497-505.
    • (2003) J Infect Dis , vol.188 , pp. 497-505
    • Khil, J.1    Im, M.2    Heath, A.3
  • 44
    • 0033486130 scopus 로고    scopus 로고
    • Use of the plasminogen activation system by microorganisms
    • Coleman JL, Benach JL. Use of the plasminogen activation system by microorganisms. J Lab Clin Med 1999; 134: 567-576.
    • (1999) J Lab Clin Med , vol.134 , pp. 567-576
    • Coleman, J.L.1    Benach, J.L.2
  • 45
    • 0028089206 scopus 로고
    • Capturing host plasmin(ogen): A common mechanism for invasive pathogens?
    • Lottenberg R, Minning-Wenz D, Boyle MD. Capturing host plasmin(ogen): a common mechanism for invasive pathogens? Trends Microbiol 1994; 2: 20-24.
    • (1994) Trends Microbiol , vol.2 , pp. 20-24
    • Lottenberg, R.1    Minning-Wenz, D.2    Boyle, M.D.3
  • 46
    • 0345120581 scopus 로고    scopus 로고
    • Selective distribution of a high-affinity plasminogen-binding site among group A streptococci associated with impetigo
    • Svensson MD, Sjobring U, Bessen DE. Selective distribution of a high-affinity plasminogen-binding site among group A streptococci associated with impetigo. Infect Immun 1999; 67: 3915-3920.
    • (1999) Infect Immun , vol.67 , pp. 3915-3920
    • Svensson, M.D.1    Sjobring, U.2    Bessen, D.E.3
  • 47
    • 9144271096 scopus 로고    scopus 로고
    • Plasminogen binding by group A streptococcal isolates from a region of hyperendemicity for streptococcal skin infection and a high incidence of invasive infection
    • McKay FC, McArthur JD, Sanderson-Smith ML, et al. Plasminogen binding by group A streptococcal isolates from a region of hyperendemicity for streptococcal skin infection and a high incidence of invasive infection. Infect Immun 2004; 72: 364-370.
    • (2004) Infect Immun , vol.72 , pp. 364-370
    • McKay, F.C.1    McArthur, J.D.2    Sanderson-Smith, M.L.3
  • 48
    • 0031042682 scopus 로고    scopus 로고
    • Plasminogen activation by invasive human pathogens
    • Boyle MD, Lottenberg R. Plasminogen activation by invasive human pathogens. Thromb Haemost 1997; 77: 1-10.
    • (1997) Thromb Haemost , vol.77 , pp. 1-10
    • Boyle, M.D.1    Lottenberg, R.2
  • 50
    • 4344601240 scopus 로고    scopus 로고
    • Plasminogen is a critical host pathogenicity factor for group A streptococcal infection
    • Sun H, Ringdahl U, Homeister JW, et al. Plasminogen is a critical host pathogenicity factor for group A streptococcal infection. Science 2004; 305: 1283-1286.
    • (2004) Science , vol.305 , pp. 1283-1286
    • Sun, H.1    Ringdahl, U.2    Homeister, J.W.3
  • 51
    • 0029116995 scopus 로고
    • Invasion of cultured human cells by Streptococcus pyogenes
    • Greco R, De Martino L, Donnarumma G, et al. Invasion of cultured human cells by Streptococcus pyogenes. Res Microbiol 1995; 146: 551-560.
    • (1995) Res Microbiol , vol.146 , pp. 551-560
    • Greco, R.1    De Martino, L.2    Donnarumma, G.3
  • 52
    • 0028046519 scopus 로고
    • Group A streptococci efficiently invade human respiratory epithelial cells
    • LaPenta D, Rubens C, Chi E, et al. Group A streptococci efficiently invade human respiratory epithelial cells. Proc Natl Acad Sci USA 1994; 91: 12115-1219.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12115-11219
    • LaPenta, D.1    Rubens, C.2    Chi, E.3
  • 53
    • 0030667715 scopus 로고    scopus 로고
    • An intracellular sanctuary for Streptococcus pyogenes in human tonsillar epithelium - studies of asymptomatic carriers and in vitro cultured biopsies
    • Österlund A, Engstrand L. An intracellular sanctuary for Streptococcus pyogenes in human tonsillar epithelium - studies of asymptomatic carriers and in vitro cultured biopsies. Acta Otolaryngol 1997b; 117: 883-888.
    • (1997) Acta Otolaryngol , vol.117 , pp. 883-888
    • Österlund, A.1    Engstrand, L.2
  • 54
    • 0030950679 scopus 로고    scopus 로고
    • Intracellular reservoir of Streptococcus pyogenes in vivo: A possible explanation for recurrent pharyngotonsillitis
    • Österlund A, Popa R, Nikkila T, et al. Intracellular reservoir of Streptococcus pyogenes in vivo: a possible explanation for recurrent pharyngotonsillitis. Laryngoscope 1997; 107: 640-647.
    • (1997) Laryngoscope , vol.107 , pp. 640-647
    • Österlund, A.1    Popa, R.2    Nikkila, T.3
  • 55
    • 0026460955 scopus 로고
    • Respiratory epithelial cell invasion by group B streptococci
    • Rubens CE, Smith S, Hulse M, et al. Respiratory epithelial cell invasion by group B streptococci. Infect Immun 1992; 60: 5157-5163.
    • (1992) Infect Immun , vol.60 , pp. 5157-5163
    • Rubens, C.E.1    Smith, S.2    Hulse, M.3
  • 56
    • 0034734629 scopus 로고    scopus 로고
    • Pharyngeal carriage of group C and group G streptococci and acute rheumatic fever in an Aboriginal population
    • Haidan A, Talay SR, Rohde M, et al. Pharyngeal carriage of group C and group G streptococci and acute rheumatic fever in an Aboriginal population. Lancet 2000; 356: 1167-1169.
    • (2000) Lancet , vol.356 , pp. 1167-1169
    • Haidan, A.1    Talay, S.R.2    Rohde, M.3
  • 57
    • 0037407486 scopus 로고    scopus 로고
    • Invasion and killing of human endothelial cells by viridans group streptococci
    • Stinson MW, Alder S, Kumar S. Invasion and killing of human endothelial cells by viridans group streptococci. Infect Immun 2003; 71: 2365-2372.
    • (2003) Infect Immun , vol.71 , pp. 2365-2372
    • Stinson, M.W.1    Alder, S.2    Kumar, S.3
  • 58
    • 0032883924 scopus 로고    scopus 로고
    • Epithelial invasion and cell lysis by virulent strains of Streptococcus suis is enhanced by the presence of suilysin
    • Norton PM, Rolph C, Ward PN, et al. Epithelial invasion and cell lysis by virulent strains of Streptococcus suis is enhanced by the presence of suilysin. FEMS Immunol Med Microbiol 1999; 26: 25-35.
    • (1999) FEMS Immunol Med Microbiol , vol.26 , pp. 25-35
    • Norton, P.M.1    Rolph, C.2    Ward, P.N.3
  • 59
    • 0029756760 scopus 로고    scopus 로고
    • Uptake of Streptococcus pneumoniae by respiratory epithelial cells
    • Talbot UM, Paton AW, Paton JC. Uptake of Streptococcus pneumoniae by respiratory epithelial cells. Infect Immun 1996; 64: 3772-3777.
    • (1996) Infect Immun , vol.64 , pp. 3772-3777
    • Talbot, U.M.1    Paton, A.W.2    Paton, J.C.3
  • 60
    • 33845406952 scopus 로고    scopus 로고
    • Adherence and internalization of Streptococcus gordonii by epithelial cells involves beta1 integrin recognition by SspA and SspB (antigen I/II family) polypeptides
    • Nobbs AH, Shearer BH, Drobni M, et al. Adherence and internalization of Streptococcus gordonii by epithelial cells involves beta1 integrin recognition by SspA and SspB (antigen I/II family) polypeptides. Cell Microbiol 2007; 9: 65-83.
    • (2007) Cell Microbiol , vol.9 , pp. 65-83
    • Nobbs, A.H.1    Shearer, B.H.2    Drobni, M.3
  • 61
    • 1842430006 scopus 로고    scopus 로고
    • Bacterial invasion: The paradigms of enteroinvasive pathogens
    • Cossart P, Sansonetti PJ. Bacterial invasion: the paradigms of enteroinvasive pathogens. Science 2004; 304: 242-248.
    • (2004) Science , vol.304 , pp. 242-248
    • Cossart, P.1    Sansonetti, P.J.2
  • 62
    • 0031686023 scopus 로고    scopus 로고
    • Streptococcus pyogenes serotype M1 encodes multiple pathways for entry into human epithelial cells
    • Cue D, Dombek PE, Lam H, et al. Streptococcus pyogenes serotype M1 encodes multiple pathways for entry into human epithelial cells. Infect Immun 1998; 66: 4593-4601.
    • (1998) Infect Immun , vol.66 , pp. 4593-4601
    • Cue, D.1    Dombek, P.E.2    Lam, H.3
  • 63
    • 0034041061 scopus 로고    scopus 로고
    • Two distinct pathways for the invasion of Streptococcus pyogenes in non-phagocytic cells
    • Molinari G, Rohde M, Guzman CA, et al. Two distinct pathways for the invasion of Streptococcus pyogenes in non-phagocytic cells. Cell Microbiol 2000; 2: 145-154.
    • (2000) Cell Microbiol , vol.2 , pp. 145-154
    • Molinari, G.1    Rohde, M.2    Guzman, C.A.3
  • 64
    • 4444347083 scopus 로고    scopus 로고
    • Non-encapsulated strains reveal novel insights in invasion and survival of Streptococcus suis in epithelial cells
    • Benga L, Goethe R, Rohde M, et al. Non-encapsulated strains reveal novel insights in invasion and survival of Streptococcus suis in epithelial cells. Cell Microbiol 2004; 6: 867-881.
    • (2004) Cell Microbiol , vol.6 , pp. 867-881
    • Benga, L.1    Goethe, R.2    Rohde, M.3
  • 65
    • 21044436925 scopus 로고    scopus 로고
    • Cellular invasion by Staphylococcus aureus reveals a functional link between focal adhesion kinase and cortactin in integrin-mediated internalisation
    • Agerer F, Lux S, Michel A, et al. Cellular invasion by Staphylococcus aureus reveals a functional link between focal adhesion kinase and cortactin in integrin-mediated internalisation. J Cell Sci 2005; 118: 2189-2200.
    • (2005) J Cell Sci , vol.118 , pp. 2189-2200
    • Agerer, F.1    Lux, S.2    Michel, A.3
  • 66
    • 0031741285 scopus 로고    scopus 로고
    • Internalization of Staphylococcus aureus by endothelial cells induces apoptosis
    • Menzies BE, Kourteva I. Internalization of Staphylococcus aureus by endothelial cells induces apoptosis. Infect Immun 1998; 66: 5994-5998.
    • (1998) Infect Immun , vol.66 , pp. 5994-5998
    • Menzies, B.E.1    Kourteva, I.2
  • 67
    • 0036062323 scopus 로고    scopus 로고
    • Invasion of human keratinocytes by Staphylococcus aureus and intracellular bacterial persistence represent haemolysin-independent virulence mechanisms that are followed by features of necrotic and apoptotic keratinocyte cell death
    • Mempel M, Schnopp C, Hojka M, et al. Invasion of human keratinocytes by Staphylococcus aureus and intracellular bacterial persistence represent haemolysin-independent virulence mechanisms that are followed by features of necrotic and apoptotic keratinocyte cell death. Br J Dermatol 2002; 146: 943-951.
    • (2002) Br J Dermatol , vol.146 , pp. 943-951
    • Mempel, M.1    Schnopp, C.2    Hojka, M.3
  • 68
    • 21144433633 scopus 로고    scopus 로고
    • Fibrinogen and fibronectin binding cooperate for valve infection and invasion in Staphylococcus aureus experimental endocarditis
    • Que YA, Haefliger JA, Piroth L, et al. Fibrinogen and fibronectin binding cooperate for valve infection and invasion in Staphylococcus aureus experimental endocarditis. J Exp Med 2005; 201: 1627-1635.
    • (2005) J Exp Med , vol.201 , pp. 1627-1635
    • Que, Y.A.1    Haefliger, J.A.2    Piroth, L.3
  • 69
    • 9444241592 scopus 로고    scopus 로고
    • Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1
    • Sinha B, Francois PP, Nusse O, et al. Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1. Cell Microbiol 1999; 1: 101-117.
    • (1999) Cell Microbiol , vol.1 , pp. 101-117
    • Sinha, B.1    Francois, P.P.2    Nusse, O.3
  • 70
    • 0033982879 scopus 로고    scopus 로고
    • Distribution and antigenicity of fibronectin binding proteins (SfbI and SfbII) of Streptococcus pyogenes clinical isolates from the northern territory, Australia
    • Goodfellow AM, Hibble M, Talay SR, et al. Distribution and antigenicity of fibronectin binding proteins (SfbI and SfbII) of Streptococcus pyogenes clinical isolates from the northern territory, Australia. J Clin Microbiol 2000; 38: 389-392.
    • (2000) J Clin Microbiol , vol.38 , pp. 389-392
    • Goodfellow, A.M.1    Hibble, M.2    Talay, S.R.3
  • 71
    • 0029130366 scopus 로고
    • Characterization of a novel fibronectin-binding surface protein in group A streptococci
    • Kreikemeyer B, Talay SR, Chhatwal GS. Characterization of a novel fibronectin-binding surface protein in group A streptococci. Mol Microbiol 1995; 17: 137-145.
    • (1995) Mol Microbiol , vol.17 , pp. 137-145
    • Kreikemeyer, B.1    Talay, S.R.2    Chhatwal, G.S.3
  • 72
    • 0028955430 scopus 로고
    • Distribution of fibronectin-binding proteins among group A streptococci of different M types
    • Natanson S, Sela S, Moses AE, et al. Distribution of fibronectin-binding proteins among group A streptococci of different M types. J Infect Dis 1995; 171: 871-878.
    • (1995) J Infect Dis , vol.171 , pp. 871-878
    • Natanson, S.1    Sela, S.2    Moses, A.E.3
  • 73
    • 0348110222 scopus 로고    scopus 로고
    • Evolution of sfbI encoding streptococcal fibronectin-binding protein I: Horizontal genetic transfer and gene mosaic structure
    • Towers RJ, Fagan PK, Talay SR, et al. Evolution of sfbI encoding streptococcal fibronectin-binding protein I: horizontal genetic transfer and gene mosaic structure. J Clin Microbiol 2003; 41: 5398-5406.
    • (2003) J Clin Microbiol , vol.41 , pp. 5398-5406
    • Towers, R.J.1    Fagan, P.K.2    Talay, S.R.3
  • 74
    • 4644293801 scopus 로고    scopus 로고
    • High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules
    • Schwarz-Linek U, Pilka ES, Pickford AR, et al. High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules. J Biol Chem 2004; 279: 39017-39025.
    • (2004) J Biol Chem , vol.279 , pp. 39017-39025
    • Schwarz-Linek, U.1    Pilka, E.S.2    Pickford, A.R.3
  • 75
    • 0026706763 scopus 로고
    • Fibronectin-binding protein of Streptococcus pyogenes: Sequence of the binding domain involved in adherence of streptococci to epithelial cells
    • Talay SR, Valentin-Weigand P, Jerlstrom PG, et al. Fibronectin-binding protein of Streptococcus pyogenes: sequence of the binding domain involved in adherence of streptococci to epithelial cells. Infect Immun 1992; 60: 3837-3844.
    • (1992) Infect Immun , vol.60 , pp. 3837-3844
    • Talay, S.R.1    Valentin-Weigand, P.2    Jerlstrom, P.G.3
  • 76
    • 0028023460 scopus 로고
    • M protein and protein F act as important determinants of cell-specific tropism of Streptococcus pyogenes in skin tissue
    • Okada N, Pentland AP, Falk P, et al. M protein and protein F act as important determinants of cell-specific tropism of Streptococcus pyogenes in skin tissue. J Clin Invest 1994; 94: 965-977.
    • (1994) J Clin Invest , vol.94 , pp. 965-977
    • Okada, N.1    Pentland, A.P.2    Falk, P.3
  • 77
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher MD, Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984; 309: 30-33.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 78
    • 0031871348 scopus 로고    scopus 로고
    • Protein F1 is required for efficient entry of Streptococcus pyogenes into epithelial cells
    • Jadoun J, Ozeri V, Burstein E, et al. Protein F1 is required for efficient entry of Streptococcus pyogenes into epithelial cells. J Infect Dis 1998; 178: 147-158.
    • (1998) J Infect Dis , vol.178 , pp. 147-158
    • Jadoun, J.1    Ozeri, V.2    Burstein, E.3
  • 79
    • 0031789927 scopus 로고    scopus 로고
    • Roles of integrins and fibronectin in the entry of Streptococcus pyogenes into cells via protein F1
    • Ozeri V, Rosenshine I, Mosher DF, et al. Roles of integrins and fibronectin in the entry of Streptococcus pyogenes into cells via protein F1. Mol Microbiol 1998; 30: 625-637.
    • (1998) Mol Microbiol , vol.30 , pp. 625-637
    • Ozeri, V.1    Rosenshine, I.2    Mosher, D.F.3
  • 80
    • 0034883769 scopus 로고    scopus 로고
    • De novo formation of focal complex-like structures in host cells by invading Streptococci
    • Ozeri V, Rosenshine I, Ben-Ze'Ev A, et al. De novo formation of focal complex-like structures in host cells by invading Streptococci. Mol Microbiol 2001; 41: 561-573.
    • (2001) Mol Microbiol , vol.41 , pp. 561-573
    • Ozeri, V.1    Rosenshine, I.2    Ben-Ze'Ev, A.3
  • 81
    • 0031871416 scopus 로고    scopus 로고
    • Entry of OpaA+ gonococci into HEp-2 cells requires concerted action of glycosaminoglycans, fibronectin and integrin receptors
    • van Putten JP, Duensing TD, Cole RL. Entry of OpaA+ gonococci into HEp-2 cells requires concerted action of glycosaminoglycans, fibronectin and integrin receptors. Mol Microbiol 1998; 29: 369-379.
    • (1998) Mol Microbiol , vol.29 , pp. 369-379
    • van Putten, J.P.1    Duensing, T.D.2    Cole, R.L.3
  • 82
    • 0035147433 scopus 로고    scopus 로고
    • Subversion of integrins by enteropathogenic Yersinia
    • Isberg RR, Barnes P. Subversion of integrins by enteropathogenic Yersinia. J Cell Sci 2001; 114: 21-28.
    • (2001) J Cell Sci , vol.114 , pp. 21-28
    • Isberg, R.R.1    Barnes, P.2
  • 83
  • 84
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • Schoenwaelder SM, Burridge K. Bidirectional signaling between the cytoskeleton and integrins. Curr Opin Cell Biol 1999; 11: 274-286.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 274-286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 85
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas SM, Brugge JS. Cellular functions regulated by Src family kinases. Annu Rev Cell Dev Biol 1997; 13: 513-609.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 86
    • 0142180077 scopus 로고    scopus 로고
    • Integrin-mediated invasion of Staphylococcus aureus into human cells requires Src family protein-tyrosine kinases
    • Agerer F, Michel A, Ohlsen K, et al. Integrin-mediated invasion of Staphylococcus aureus into human cells requires Src family protein-tyrosine kinases. J Biol Chem 2003; 278: 42524-42531.
    • (2003) J Biol Chem , vol.278 , pp. 42524-42531
    • Agerer, F.1    Michel, A.2    Ohlsen, K.3
  • 87
    • 0032948146 scopus 로고    scopus 로고
    • Mechanisms of internalization of Staphylococcus aureus by cultured human osteoblasts
    • Jevon M, Guo C, Ma B, et al. Mechanisms of internalization of Staphylococcus aureus by cultured human osteoblasts. Infect Immun 1999; 67: 2677-2681.
    • (1999) Infect Immun , vol.67 , pp. 2677-2681
    • Jevon, M.1    Guo, C.2    Ma, B.3
  • 88
    • 4644372118 scopus 로고    scopus 로고
    • Internalization of Staphylococcus aureus by human keratinocytes
    • Kintarak S, Whawell SA, Speight PM, et al. Internalization of Staphylococcus aureus by human keratinocytes. Infect Immun 2004; 72: 5668-5675.
    • (2004) Infect Immun , vol.72 , pp. 5668-5675
    • Kintarak, S.1    Whawell, S.A.2    Speight, P.M.3
  • 89
    • 0035213652 scopus 로고    scopus 로고
    • Fibronectin-binding protein A of Staphylococcus aureus has multiple, substituting, binding regions that mediate adherence to fibronectin and invasion of endothelial cells
    • Massey RC, Kantzanou MN, Fowler T, et al. Fibronectin-binding protein A of Staphylococcus aureus has multiple, substituting, binding regions that mediate adherence to fibronectin and invasion of endothelial cells. Cell Microbiol 2001; 3: 839-851.
    • (2001) Cell Microbiol , vol.3 , pp. 839-851
    • Massey, R.C.1    Kantzanou, M.N.2    Fowler, T.3
  • 90
    • 0028859357 scopus 로고
    • Adhesion properties of mutants of Staphylococcus aureus defective in fibronectin-binding proteins and studies on the expression of fnb genes
    • Greene C, McDevitt D, Francois P, et al. Adhesion properties of mutants of Staphylococcus aureus defective in fibronectin-binding proteins and studies on the expression of fnb genes. Mol Microbiol 1995; 17: 1143-1152.
    • (1995) Mol Microbiol , vol.17 , pp. 1143-1152
    • Greene, C.1    McDevitt, D.2    Francois, P.3
  • 91
    • 0041386346 scopus 로고    scopus 로고
    • In vivo and in vitro demonstration that Staphylococcus aureus is an intracellular pathogen in the presence or absence of fibronectin-binding proteins
    • Brouillette E, Grondin G, Shkreta L, et al. In vivo and in vitro demonstration that Staphylococcus aureus is an intracellular pathogen in the presence or absence of fibronectin-binding proteins. Microb Pathog 2003; 35: 159-169.
    • (2003) Microb Pathog , vol.35 , pp. 159-169
    • Brouillette, E.1    Grondin, G.2    Shkreta, L.3
  • 92
    • 0038001468 scopus 로고    scopus 로고
    • Src kinase has a central role in in vitro cellular internalization of Staphylococcus aureus
    • Fowler T, Johansson S, Wary KK, et al. Src kinase has a central role in in vitro cellular internalization of Staphylococcus aureus. Cell Microbiol 2003; 5: 417-426.
    • (2003) Cell Microbiol , vol.5 , pp. 417-426
    • Fowler, T.1    Johansson, S.2    Wary, K.K.3
  • 93
    • 0032813475 scopus 로고    scopus 로고
    • Fibronectin binding protein and host cell tyrosine kinase are required for internalization of Staphylococcus aureus by epithelial cells
    • Dziewanowska K, Patti JM, Deobald CF, et al. Fibronectin binding protein and host cell tyrosine kinase are required for internalization of Staphylococcus aureus by epithelial cells. Infect Immun 1999; 67: 4673-4678.
    • (1999) Infect Immun , vol.67 , pp. 4673-4678
    • Dziewanowska, K.1    Patti, J.M.2    Deobald, C.F.3
  • 94
    • 2442505474 scopus 로고    scopus 로고
    • Reduced adherence and host cell invasion by methicillin-resistant Staphylococcus aureus expressing the surface protein Pis
    • Juuti KM, Sinha B, Werbick C, et al. Reduced adherence and host cell invasion by methicillin-resistant Staphylococcus aureus expressing the surface protein Pis. J Infect Dis 2004; 189: 1574-1584.
    • (2004) J Infect Dis , vol.189 , pp. 1574-1584
    • Juuti, K.M.1    Sinha, B.2    Werbick, C.3
  • 95
    • 0042978789 scopus 로고    scopus 로고
    • Host cell caveolae act as an entry-port for group A streptococci
    • Rohde M, Muller E, Chhatwal GS, et al. Host cell caveolae act as an entry-port for group A streptococci. Cell Microbiol 2003; 5: 323-342.
    • (2003) Cell Microbiol , vol.5 , pp. 323-342
    • Rohde, M.1    Muller, E.2    Chhatwal, G.S.3
  • 96
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans L, Kartenbeck J, Helenius A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat Cell Biol 2001; 3: 473-483.
    • (2001) Nat Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 97
    • 0031899956 scopus 로고    scopus 로고
    • High-frequency intracellular infection and erythrogenic toxin A expression undergo phase variation in M1 group A streptococci
    • Cleary PP, McLandsborough L, Ikeda L, et al. High-frequency intracellular infection and erythrogenic toxin A expression undergo phase variation in M1 group A streptococci. Mol Microbiol 1998; 28: 157-167.
    • (1998) Mol Microbiol , vol.28 , pp. 157-167
    • Cleary, P.P.1    McLandsborough, L.2    Ikeda, L.3
  • 98
    • 33144467086 scopus 로고    scopus 로고
    • Streptococcal modulation of cellular invasion via TGF-beta1 signaling
    • Wang B, Li S, Southern PJ, et al. Streptococcal modulation of cellular invasion via TGF-beta1 signaling. Proc Natl Acad Sci USA 2006; 103: 2380-2385.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2380-2385
    • Wang, B.1    Li, S.2    Southern, P.J.3
  • 99
    • 0032904116 scopus 로고    scopus 로고
    • High-frequency intracellular invasion of epithelial cells by sero-type M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements
    • Dombek PE, Cue D, Sedgewick J, et al. High-frequency intracellular invasion of epithelial cells by sero-type M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements. Mol Microbiol 1999; 31: 859-870.
    • (1999) Mol Microbiol , vol.31 , pp. 859-870
    • Dombek, P.E.1    Cue, D.2    Sedgewick, J.3
  • 100
    • 0033002358 scopus 로고    scopus 로고
    • Comparison of adherence to and penetration of a human laryngeal epithelial cell line by group A streptococci of various M protein types
    • Hagman MM, Dale JB, Stevens DL. Comparison of adherence to and penetration of a human laryngeal epithelial cell line by group A streptococci of various M protein types. FEMS Immunol Med Microbiol 1999; 23: 195-204.
    • (1999) FEMS Immunol Med Microbiol , vol.23 , pp. 195-204
    • Hagman, M.M.1    Dale, J.B.2    Stevens, D.L.3
  • 101
    • 0042825310 scopus 로고    scopus 로고
    • Intracellular survival of Streptococcus pyogenes in polymorphonuclear cells results in increased bacterial virulence
    • Medina E, Rohde M, Chhatwal GS. Intracellular survival of Streptococcus pyogenes in polymorphonuclear cells results in increased bacterial virulence. Infect Immum 2003; 71: 5376-5380.
    • (2003) Infect Immum , vol.71 , pp. 5376-5380
    • Medina, E.1    Rohde, M.2    Chhatwal, G.S.3
  • 102
    • 0035818973 scopus 로고    scopus 로고
    • Cywes C, Wessels MR. Group A Streptococcus tissue invasion by CD44-mediated cell signalling. Nature 2001; 414: 648-652.
    • Cywes C, Wessels MR. Group A Streptococcus tissue invasion by CD44-mediated cell signalling. Nature 2001; 414: 648-652.
  • 103
    • 0032523209 scopus 로고    scopus 로고
    • Hyaluronic acid capsule modulates M protein-mediated adherence and acts as a ligand for attachment of group A Streptococcus to CD44 on human keratinocytes
    • Schrager HM, Alberti S, Cywes C, et al. Hyaluronic acid capsule modulates M protein-mediated adherence and acts as a ligand for attachment of group A Streptococcus to CD44 on human keratinocytes. J Clin Invest 1998; 101: 1708-1716.
    • (1998) J Clin Invest , vol.101 , pp. 1708-1716
    • Schrager, H.M.1    Alberti, S.2    Cywes, C.3
  • 104
    • 0033787963 scopus 로고    scopus 로고
    • CD44 as a receptor for colonization of the pharynx by group A Streptococcus
    • Cywes C, Stamenkovic I, Wessels MR. CD44 as a receptor for colonization of the pharynx by group A Streptococcus. J Clin Invest 2000; 106: 995-1002.
    • (2000) J Clin Invest , vol.106 , pp. 995-1002
    • Cywes, C.1    Stamenkovic, I.2    Wessels, M.R.3
  • 105
    • 2942614702 scopus 로고    scopus 로고
    • Interactions with fibronectin attenuate the virulence of Streptococcus pyogenes
    • Nyberg P, Sakai T, Cho KH, et al. Interactions with fibronectin attenuate the virulence of Streptococcus pyogenes. Embo J 2004; 23: 2166-2174.
    • (2004) Embo J , vol.23 , pp. 2166-2174
    • Nyberg, P.1    Sakai, T.2    Cho, K.H.3
  • 106
    • 0029443502 scopus 로고
    • Regulation of host cell recognition in Streptococcus pyogenes
    • Gibson C, Fogg G, Okada N, et al. Regulation of host cell recognition in Streptococcus pyogenes. Dev Biol Stand 1995; 85: 137-144.
    • (1995) Dev Biol Stand , vol.85 , pp. 137-144
    • Gibson, C.1    Fogg, G.2    Okada, N.3
  • 107
    • 2942618331 scopus 로고    scopus 로고
    • SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1
    • Nyberg P, Rasmussen M, Von Pawel-Rammingen U, et al. SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1. Microbiology 2004; 150: 1559-1569.
    • (2004) Microbiology , vol.150 , pp. 1559-1569
    • Nyberg, P.1    Rasmussen, M.2    Von Pawel-Rammingen, U.3
  • 108
    • 1842372721 scopus 로고    scopus 로고
    • Invasion of brain microvascular endothelial cells by group B streptococci
    • Nizet V, Kim KS, Stins M, et al. Invasion of brain microvascular endothelial cells by group B streptococci. Infect Immun 1997; 65: 5074-5081.
    • (1997) Infect Immun , vol.65 , pp. 5074-5081
    • Nizet, V.1    Kim, K.S.2    Stins, M.3
  • 109
    • 24644446476 scopus 로고    scopus 로고
    • Blood-brain barrier invasion by group B Streptococcus depends upon proper cell-surface anchoring of lipoteichoic acid
    • Doran KS, Engelson EJ, Khosravi A, et al. Blood-brain barrier invasion by group B Streptococcus depends upon proper cell-surface anchoring of lipoteichoic acid. J Clin Invest 2005; 115: 2499-2507.
    • (2005) J Clin Invest , vol.115 , pp. 2499-2507
    • Doran, K.S.1    Engelson, E.J.2    Khosravi, A.3
  • 110
    • 30944446387 scopus 로고    scopus 로고
    • Group B Streptococcus crosses human epithelial cells by a paracellular route
    • Soriani M, Santi I, Taddei A, et al. Group B Streptococcus crosses human epithelial cells by a paracellular route. J Infect Dis 2006; 193: 241-250.
    • (2006) J Infect Dis , vol.193 , pp. 241-250
    • Soriani, M.1    Santi, I.2    Taddei, A.3
  • 111
    • 0037443060 scopus 로고    scopus 로고
    • Survival of Streptococcus pyogenes within host phagocytic cells: A pathogenic mechanism for persistence and systemic invasion
    • Medina E, Goldmann O, Toppel AW, et al. Survival of Streptococcus pyogenes within host phagocytic cells: a pathogenic mechanism for persistence and systemic invasion. J Infect Dis 2003; 187: 597-603.
    • (2003) J Infect Dis , vol.187 , pp. 597-603
    • Medina, E.1    Goldmann, O.2    Toppel, A.W.3
  • 112
    • 0037397627 scopus 로고    scopus 로고
    • Streptococcus pyogenes expressing M and M-like surface proteins are phagocytosed but survive inside human neutrophils
    • Staali L, Morgelin M, Bjorck L, et al. Streptococcus pyogenes expressing M and M-like surface proteins are phagocytosed but survive inside human neutrophils. Cell Microbiol 2003; 5: 253-265.
    • (2003) Cell Microbiol , vol.5 , pp. 253-265
    • Staali, L.1    Morgelin, M.2    Bjorck, L.3
  • 113
    • 33644870686 scopus 로고    scopus 로고
    • Streptococcus pyogenes bacteria modulate membrane traffic in human neutrophils and selectively inhibit azurophilic granule fusion with phagosomes
    • Staali L, Bauer S, Morgelin M, et al. Streptococcus pyogenes bacteria modulate membrane traffic in human neutrophils and selectively inhibit azurophilic granule fusion with phagosomes. Cell Microbiol 2006; 8: 690-703.
    • (2006) Cell Microbiol , vol.8 , pp. 690-703
    • Staali, L.1    Bauer, S.2    Morgelin, M.3
  • 114
    • 0037452582 scopus 로고    scopus 로고
    • Genome-wide protective response used by group A Streptococcus to evade destruction by human polymorphonuclear leukocytes
    • Voyich JM, Sturdevant DE, Braughton KR, et al. Genome-wide protective response used by group A Streptococcus to evade destruction by human polymorphonuclear leukocytes. Proc Natl Acad Sci USA 2003; 100: 1996-2001.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1996-2001
    • Voyich, J.M.1    Sturdevant, D.E.2    Braughton, K.R.3
  • 115
    • 0141814639 scopus 로고    scopus 로고
    • Bacterial pathogens modulate an apoptosis differentiation program in human neutrophils
    • Kobayashi SD, Braughton KR, Whitney AR, et al. Bacterial pathogens modulate an apoptosis differentiation program in human neutrophils. Proc Natl Acad Sci USA 2003; 100: 10948-10953.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10948-10953
    • Kobayashi, S.D.1    Braughton, K.R.2    Whitney, A.R.3
  • 116
    • 2142768811 scopus 로고    scopus 로고
    • Role of macrophages in host resistance to group A streptococci
    • Goldmann O, Rohde M, Chhatwal GS, et al. Role of macrophages in host resistance to group A streptococci. Infect Immun 2004; 72: 2956-2963.
    • (2004) Infect Immun , vol.72 , pp. 2956-2963
    • Goldmann, O.1    Rohde, M.2    Chhatwal, G.S.3
  • 117
    • 33645370250 scopus 로고    scopus 로고
    • Viable group A streptococci in macrophages during acute soft tissue infection
    • Thulin P, Johansson L, Low DE, et al. Viable group A streptococci in macrophages during acute soft tissue infection. PLoS Med 2006; 3: e53.
    • (2006) PLoS Med , vol.3
    • Thulin, P.1    Johansson, L.2    Low, D.E.3
  • 118
    • 0035724292 scopus 로고    scopus 로고
    • Fba, a novel fibronectin-binding protein from Streptococcus pyogenes, promotes bacterial entry into epithelial cells, and the fba gene is positively transcribed under the Mga regulator
    • Terao Y, Kawabata S, Kunitomo E, et al. Fba, a novel fibronectin-binding protein from Streptococcus pyogenes, promotes bacterial entry into epithelial cells, and the fba gene is positively transcribed under the Mga regulator. Mol Microbiol 2001; 42: 75-86.
    • (2001) Mol Microbiol , vol.42 , pp. 75-86
    • Terao, Y.1    Kawabata, S.2    Kunitomo, E.3
  • 119
    • 0037033063 scopus 로고    scopus 로고
    • Molecular characterization of a novel fibronectin-binding protein of Streptococcus pyogenes strains isolated from toxic shock-like syndrome patients
    • Terao Y, Kawabata S, Nakata M, et al. Molecular characterization of a novel fibronectin-binding protein of Streptococcus pyogenes strains isolated from toxic shock-like syndrome patients. J Biol Chem 2002; 277: 47428-47435.
    • (2002) J Biol Chem , vol.277 , pp. 47428-47435
    • Terao, Y.1    Kawabata, S.2    Nakata, M.3
  • 120
    • 0029945894 scopus 로고    scopus 로고
    • Differential effects of the streptococcal fibronectin-binding protein, FBP54, on adhesion of group A streptococci to human buccal cells and HEp-2 tissue culture cells
    • Courtney HS, Dale JB, Hasty DI. Differential effects of the streptococcal fibronectin-binding protein, FBP54, on adhesion of group A streptococci to human buccal cells and HEp-2 tissue culture cells. Infect Immun 1996; 64: 2415-2419.
    • (1996) Infect Immun , vol.64 , pp. 2415-2419
    • Courtney, H.S.1    Dale, J.B.2    Hasty, D.I.3
  • 121
    • 0017763869 scopus 로고
    • Adherence pharyngeal and skin strains of group A streptococci to human skin and oral epithelial cells
    • Alkan M, Ofek I, Beachey EH. Adherence pharyngeal and skin strains of group A streptococci to human skin and oral epithelial cells. Infect Immun 1977; 18: 555-557.
    • (1977) Infect Immun , vol.18 , pp. 555-557
    • Alkan, M.1    Ofek, I.2    Beachey, E.H.3
  • 122
    • 0028089775 scopus 로고
    • Analysis of the role of M24 protein in group A streptococcal adhesion and colonization by use of omega-interposon mutagenesis
    • Courtney HS, Bronze MS, Dale JB, et al. Analysis of the role of M24 protein in group A streptococcal adhesion and colonization by use of omega-interposon mutagenesis. Infect Immun 1994; 62: 4868-4873.
    • (1994) Infect Immun , vol.62 , pp. 4868-4873
    • Courtney, H.S.1    Bronze, M.S.2    Dale, J.B.3
  • 123
    • 0028008787 scopus 로고
    • M protein mediates streptococcal adhesion to HEp-2 cells
    • Wang JR, Stinson MW. M protein mediates streptococcal adhesion to HEp-2 cells. Infect Immun 1994; 62: 442-448.
    • (1994) Infect Immun , vol.62 , pp. 442-448
    • Wang, J.R.1    Stinson, M.W.2
  • 124
    • 0032910564 scopus 로고    scopus 로고
    • Serum opacity factor is a major fibronectin-binding protein and a virulence determinant of M type 2 Streptococcus pyogenes
    • Courtney HS, Hasty DL, Li Y, et al. Serum opacity factor is a major fibronectin-binding protein and a virulence determinant of M type 2 Streptococcus pyogenes. Mol Microbiol 1999; 32: 89-98.
    • (1999) Mol Microbiol , vol.32 , pp. 89-98
    • Courtney, H.S.1    Hasty, D.L.2    Li, Y.3
  • 125
    • 0028928762 scopus 로고
    • DNA sequence of the serum opacity factor of group A streptococci: Identification of a fibronectin-binding repeat domain
    • Rakonjac JV, Robbins JC, Fischetti VA. DNA sequence of the serum opacity factor of group A streptococci: identification of a fibronectin-binding repeat domain. Infect Immun 1995; 63: 622-631.
    • (1995) Infect Immun , vol.63 , pp. 622-631
    • Rakonjac, J.V.1    Robbins, J.C.2    Fischetti, V.A.3
  • 126
    • 0029934980 scopus 로고    scopus 로고
    • Identification of a fibronectin-binding protein (GfbA) in pathogenic group G streptococci
    • Kline JB, Xu S, Bisno AL, et al. Identification of a fibronectin-binding protein (GfbA) in pathogenic group G streptococci. Infect Immun 1996; 64: 2122-2129.
    • (1996) Infect Immun , vol.64 , pp. 2122-2129
    • Kline, J.B.1    Xu, S.2    Bisno, A.L.3
  • 127
    • 7044247620 scopus 로고    scopus 로고
    • The fibrinogen receptor FbsA promotes adherence of Streptococcus agalactiae to human epithelial cells
    • Schubert A, Zakikhany K, Pietrocola G, et al. The fibrinogen receptor FbsA promotes adherence of Streptococcus agalactiae to human epithelial cells. Infect Immun 2004; 72: 6197-6205.
    • (2004) Infect Immun , vol.72 , pp. 6197-6205
    • Schubert, A.1    Zakikhany, K.2    Pietrocola, G.3
  • 128
    • 21544480286 scopus 로고    scopus 로고
    • Adherence to and invasion of human brain microvascular endothelial cells are promoted by fibrinogen-binding protein FbsA of Streptococcus agalactiae
    • Tenenbaum T, Bloier C, Adam R, et al. Adherence to and invasion of human brain microvascular endothelial cells are promoted by fibrinogen-binding protein FbsA of Streptococcus agalactiae. Infect Immun 2005; 73: 4404-4409.
    • (2005) Infect Immun , vol.73 , pp. 4404-4409
    • Tenenbaum, T.1    Bloier, C.2    Adam, R.3
  • 129
    • 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, Millsap KW, et al. The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence. Mol Microbiol 2001; 41: 1395-1408.
    • (2001) Mol Microbiol , vol.41 , pp. 1395-1408
    • Holmes, A.R.1    McNab, R.2    Millsap, K.W.3
  • 130
    • 0034607985 scopus 로고    scopus 로고
    • The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen
    • Wann ER, Gurusiddappa S, Hook M. The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen. J Biol Chem 2000; 275: 13863-13871.
    • (2000) J Biol Chem , vol.275 , pp. 13863-13871
    • Wann, E.R.1    Gurusiddappa, S.2    Hook, M.3
  • 131
    • 0032899735 scopus 로고    scopus 로고
    • Adherence of Staphylococcus aureus is enhanced by an endogenous secreted protein with broad binding activity
    • Palma M, Haggar A, Flock JI. Adherence of Staphylococcus aureus is enhanced by an endogenous secreted protein with broad binding activity. J Bacteriol 1999; 181: 2840-2845.
    • (1999) J Bacteriol , vol.181 , pp. 2840-2845
    • Palma, M.1    Haggar, A.2    Flock, J.I.3
  • 132
    • 0035164511 scopus 로고    scopus 로고
    • Identification and characterization of a novel 38.5-kilodalton cell surface protein of Staphylococcus aureus with extended-spectrum binding activity for extracellular matrix and plasma proteins
    • Hussain M, Becker K, von Eiff C, et al. Identification and characterization of a novel 38.5-kilodalton cell surface protein of Staphylococcus aureus with extended-spectrum binding activity for extracellular matrix and plasma proteins. J Bacteriol 2001; 183: 6778-6786.
    • (2001) J Bacteriol , vol.183 , pp. 6778-6786
    • Hussain, M.1    Becker, K.2    von Eiff, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.