메뉴 건너뛰기




Volumn 7, Issue , 2016, Pages

Erratum: Group A Streptococcus exploits human plasminogen for bacterial translocation across epithelial barrier via tricellular tight junctions (Scientific Reports (2016) 6 (20069) DOI: 10.1038/srep20069);Group A Streptococcus exploits human plasminogen for bacterial translocation across epithelial barrier via tricellular tight junctions

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; ENOLASE; PLASMINOGEN; STREPTOCOCCAL SURFACE ENOLASE; TRICELLULIN;

EID: 84956684639     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep46388     Document Type: Erratum
Times cited : (38)

References (47)
  • 2
    • 34347334334 scopus 로고    scopus 로고
    • New understanding of the group A Streptococcus pathogenesis cycle
    • Tart, A. H., Walker, M. J., Musser, J. M. New understanding of the group A Streptococcus pathogenesis cycle. Trends Microbiol. 15, 318-325 (2007).
    • (2007) Trends Microbiol. , vol.15 , pp. 318-325
    • Tart, A.H.1    Walker, M.J.2    Musser, J.M.3
  • 5
    • 0015846194 scopus 로고
    • Further observations on the fine structure of freeze-cleaved tight junctions
    • Staehelin, L. A. Further observations on the fine structure of freeze-cleaved tight junctions. J. Cell Sci. 13, 763-786 (1973).
    • (1973) J. Cell Sci. , vol.13 , pp. 763-786
    • Staehelin, L.A.1
  • 6
    • 0015994540 scopus 로고
    • The structure of the zonula occludens. A single fibril model based on freeze-fracture
    • Wade, J. B., Karnovsky, M. J. The structure of the zonula occludens. A single fibril model based on freeze-fracture. J. Cell Biol. 60, 168-180 (1974).
    • (1974) J. Cell Biol. , vol.60 , pp. 168-180
    • Wade, J.B.1    Karnovsky, M.J.2
  • 7
    • 0021881877 scopus 로고
    • A re-assessment of the tricellular region of epithelial cell tight junctions in trachea of Guinea pig
    • Walker, D. C., MacKenzie, A., Hulbert, W. C., Hogg, J. C. A re-assessment of the tricellular region of epithelial cell tight junctions in trachea of guinea pig. Acta Anat. 122, 35-38 (1985).
    • (1985) Acta Anat. , vol.122 , pp. 35-38
    • Walker, D.C.1    MacKenzie, A.2    Hulbert, W.C.3    Hogg, J.C.4
  • 8
    • 29144533473 scopus 로고    scopus 로고
    • Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells
    • Ikenouchi, J. et al. Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J. Cell Biol. 171, 939-945 (2005).
    • (2005) J. Cell Biol. , vol.171 , pp. 939-945
    • Ikenouchi, J.1
  • 9
    • 84859938186 scopus 로고    scopus 로고
    • Shigella targets epithelial tricellular junctions and uses a noncanonical clathrin-dependent endocytic pathway to spread between cells
    • Fukumatsu, M. et al. Shigella targets epithelial tricellular junctions and uses a noncanonical clathrin-dependent endocytic pathway to spread between cells. Cell Host Microbe 11, 325-336 (2012).
    • (2012) Cell Host Microbe , vol.11 , pp. 325-336
    • Fukumatsu, M.1
  • 10
    • 78951469708 scopus 로고    scopus 로고
    • Streptolysin S contributes to group A streptococcal translocation across an epithelial barrier
    • Sumitomo, T. et al. Streptolysin S contributes to group A streptococcal translocation across an epithelial barrier. J. Biol. Chem. 286, 2750-2761 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 2750-2761
    • Sumitomo, T.1
  • 12
    • 21244444520 scopus 로고    scopus 로고
    • Is plasminogen deployed as a Streptococcus pyogenes virulence factor?
    • Walker, M. J., McArthur, J. D., McKay, F., Ranson, M. Is plasminogen deployed as a Streptococcus pyogenes virulence factor? Trends Microbiol. 13, 308-313 (2005).
    • (2005) Trends Microbiol. , vol.13 , pp. 308-313
    • Walker, M.J.1    McArthur, J.D.2    McKay, F.3    Ranson, M.4
  • 13
    • 0242321265 scopus 로고    scopus 로고
    • Plasminogen-mediated group A streptococcal adherence and pericellular invasion of human pharyngeal cells
    • Pancholi, V., Fontan, P., Jin, H. Plasminogen-mediated group A streptococcal adherence and pericellular invasion of human pharyngeal cells. Microb. Pathog. 35, 293-303 (2003).
    • (2003) Microb. Pathog. , vol.35 , pp. 293-303
    • Pancholi, V.1    Fontan, P.2    Jin, H.3
  • 14
    • 0033838876 scopus 로고    scopus 로고
    • Molecular studies of the intestinal mucosal barrier physiopathology using cocultures of epithelial and immune cells: A technical update
    • Kerneis, S. et al. Molecular studies of the intestinal mucosal barrier physiopathology using cocultures of epithelial and immune cells: a technical update. Microbes Infect. 2, 1119-1124 (2000).
    • (2000) Microbes Infect. , vol.2 , pp. 1119-1124
    • Kerneis, S.1
  • 15
    • 0037329956 scopus 로고    scopus 로고
    • The use of transepithelial models to examine host-pathogen interactions
    • McCormick, B. A. The use of transepithelial models to examine host-pathogen interactions. Curr. Opin. Microbiol. 6, 77-81 (2003).
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 77-81
    • McCormick, B.A.1
  • 17
    • 84877694434 scopus 로고    scopus 로고
    • Group A streptococcal cysteine protease cleaves epithelial junctions and contributes to bacterial translocation
    • Sumitomo, T., Nakata, M., Higashino, M., Terao, Y., Kawabata, S. Group A streptococcal cysteine protease cleaves epithelial junctions and contributes to bacterial translocation. J. Biol. Chem. 288, 13317-13324 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 13317-13324
    • Sumitomo, T.1    Nakata, M.2    Higashino, M.3    Terao, Y.4    Kawabata, S.5
  • 18
    • 84861117698 scopus 로고    scopus 로고
    • The X-ray crystal structure of full-length human plasminogen
    • Law, R. H. et al. The X-ray crystal structure of full-length human plasminogen. Cell Rep. 1, 185-190 (2012).
    • (2012) Cell Rep. , vol.1 , pp. 185-190
    • Law, R.H.1
  • 19
    • 0032486286 scopus 로고    scopus 로고
    • Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi, V., Fischetti, V. A. Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J. Biol. Chem. 273, 14503-14515 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 20
    • 0346881417 scopus 로고    scopus 로고
    • Role of the C-terminal lysine residues of streptococcal surface enolase in Glu-and Lys-plasminogen-binding activities of group A streptococci
    • Derbise, A., Song, Y. P., Parikh, S., Fischetti, V. A., Pancholi, V. Role of the C-terminal lysine residues of streptococcal surface enolase in Glu-and Lys-plasminogen-binding activities of group A streptococci. Infect. Immun. 72, 94-105 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 94-105
    • Derbise, A.1    Song, Y.P.2    Parikh, S.3    Fischetti, V.A.4    Pancholi, V.5
  • 21
    • 23944510259 scopus 로고    scopus 로고
    • Genome sequence of a serotype M28 strain of Group A Streptococcus: Potential new insights into puerperal sepsis and bacterial disease specificity
    • Green, N. M. et al. Genome sequence of a serotype M28 strain of Group A Streptococcus: potential new insights into puerperal sepsis and bacterial disease specificity. J. Infect. Dis. 192, 760-770 (2005).
    • (2005) J. Infect. Dis. , vol.192 , pp. 760-770
    • Green, N.M.1
  • 22
    • 67650529851 scopus 로고    scopus 로고
    • Defining the structural basis of human plasminogen binding by streptococcal surface enolase
    • Cork, A. J. et al. Defining the structural basis of human plasminogen binding by streptococcal surface enolase. J. Biol. Chem. 284, 17129-17137 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 17129-17137
    • Cork, A.J.1
  • 24
    • 0017855840 scopus 로고
    • Morphological factors influencing transepithelial permeability: A model for the resistance of the zonulaoccludens
    • Claude, P. Morphological factors influencing transepithelial permeability: a model for the resistance of the zonulaoccludens. J. Membr. Biol. 39, 219-232 (1978).
    • (1978) J. Membr. Biol. , vol.39 , pp. 219-232
    • Claude, P.1
  • 25
    • 24644435107 scopus 로고    scopus 로고
    • Microbial strategies to target, cross or disrupt epithelia
    • Sousa, S., Lecuit, M., Cossart, P. Microbial strategies to target, cross or disrupt epithelia. Curr. Opin. Cell Biol. 17, 489-498 (2005).
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 489-498
    • Sousa, S.1    Lecuit, M.2    Cossart, P.3
  • 26
    • 63249098521 scopus 로고    scopus 로고
    • Tight junctions as targets of infectious agents
    • Guttman, J. A., Finlay, B. B. Tight junctions as targets of infectious agents. Biochim. Biophys. Acta 1788, 832-841 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 832-841
    • Guttman, J.A.1    Finlay, B.B.2
  • 27
    • 0020315806 scopus 로고
    • Plasminogen in human saliva
    • Moody, G. H. Plasminogen in human saliva. Int. J. Oral Surg. 11, 110-114 (1982).
    • (1982) Int. J. Oral Surg. , vol.11 , pp. 110-114
    • Moody, G.H.1
  • 28
    • 0025439344 scopus 로고
    • The possible role of oral epithelial cells in tissue-type plasminogen activator-related fibrinolysis in human saliva
    • Sindet-Pedersen, S., Gram, J., Jespersen, J. The possible role of oral epithelial cells in tissue-type plasminogen activator-related fibrinolysis in human saliva. J. Dent. Res. 69, 1283-1286 (1990).
    • (1990) J. Dent. Res. , vol.69 , pp. 1283-1286
    • Sindet-Pedersen, S.1    Gram, J.2    Jespersen, J.3
  • 29
    • 51349138787 scopus 로고    scopus 로고
    • Allelic variants of streptokinase from Streptococcus pyogenes display functional differences in plasminogen activation
    • McArthur, J. D. et al. Allelic variants of streptokinase from Streptococcus pyogenes display functional differences in plasminogen activation. FASEB J. 22, 3146-3153 (2008).
    • (2008) FASEB J. , vol.22 , pp. 3146-3153
    • McArthur, J.D.1
  • 30
    • 0025757268 scopus 로고
    • Isolation of a prokaryotic plasmin receptor. Relationship to a plasminogen activator produced by the same micro-organism
    • Broder, C. C., Lottenberg, R., von Mering, G. O., Johnston, K. H., Boyle, M. D. Isolation of a prokaryotic plasmin receptor. Relationship to a plasminogen activator produced by the same micro-organism. J. Biol. Chem. 266, 4922-4928 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 4922-4928
    • Broder, C.C.1    Lottenberg, R.2    Von Mering, G.O.3    Johnston, K.H.4    Boyle, M.D.5
  • 31
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi, V., Fischetti, V. A. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J. Exp. Med. 176, 415-426 (1992).
    • (1992) J. Exp. Med. , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 32
    • 0027451350 scopus 로고
    • PAM a novel plasminogen-binding protein from Streptococcus pyogenes
    • Berge, A., Sjobring, U. PAM, a novel plasminogen-binding protein from Streptococcus pyogenes. J. Biol. Chem. 268, 25417-25424 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 25417-25424
    • Berge, A.1    Sjobring, U.2
  • 33
    • 33846929584 scopus 로고    scopus 로고
    • The plasminogen-binding group A streptococcal M proteinrelated protein Prp binds plasminogen via arginine and histidine residues
    • Sanderson-Smith, M. L., Dowton, M., Ranson, M., Walker, M. J. The plasminogen-binding group A streptococcal M proteinrelated protein Prp binds plasminogen via arginine and histidine residues. J. Bacteriol. 189, 1435-1440 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 1435-1440
    • Sanderson-Smith, M.L.1    Dowton, M.2    Ranson, M.3    Walker, M.J.4
  • 34
    • 36749052845 scopus 로고    scopus 로고
    • The Streptococcus pyogenes serotype M49 Nra-Ralp3 transcriptional regulatory network and its control of virulence factor expression from the novel eno ralp3 epf sagA pathogenicity region
    • Kreikemeyer, B. et al. The Streptococcus pyogenes serotype M49 Nra-Ralp3 transcriptional regulatory network and its control of virulence factor expression from the novel eno ralp3 epf sagA pathogenicity region. Infect. Immun. 75, 5698-5710 (2007).
    • (2007) Infect. Immun. , vol.75 , pp. 5698-5710
    • Kreikemeyer, B.1
  • 35
    • 0345120581 scopus 로고    scopus 로고
    • Selective distribution of a high-affinity plasminogen-binding site among group A streptococci associated with impetigo
    • Svensson, M. D., Sjobring, U., Bessen, D. E. Selective distribution of a high-affinity plasminogen-binding site among group A streptococci associated with impetigo. Infect. Immun. 67, 3915-3920 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 3915-3920
    • Svensson, M.D.1    Sjobring, U.2    Bessen, D.E.3
  • 36
    • 5144224570 scopus 로고    scopus 로고
    • Plasmin(ogen)-binding ?-enolase from Streptococcus pneumoniae: Crystal structure and evaluation of plasmin(ogen)-binding sites
    • Ehinger, S., Schubert, W. D., Bergmann, S., Hammerschmidt, S., Heinz, D. W. Plasmin(ogen)-binding ?-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites. J. Mol. Biol. 343, 997-1005 (2004).
    • (2004) J. Mol. Biol. , vol.343 , pp. 997-1005
    • Ehinger, S.1    Schubert, W.D.2    Bergmann, S.3    Hammerschmidt, S.4    Heinz, D.W.5
  • 37
    • 84926429595 scopus 로고    scopus 로고
    • Stability of the octameric structure affects plasminogen-binding capacity of streptococcal enolase
    • Cork, A. J. et al. Stability of the octameric structure affects plasminogen-binding capacity of streptococcal enolase. PLoS One 10, e0121764 (2015).
    • (2015) PLoS One , vol.10 , pp. e0121764
    • Cork, A.J.1
  • 38
    • 0038501069 scopus 로고    scopus 로고
    • Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae
    • Bergmann, S. et al. Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Mol. Microbiol. 49, 411-423 (2003).
    • (2003) Mol. Microbiol. , vol.49 , pp. 411-423
    • Bergmann, S.1
  • 40
    • 1242318719 scopus 로고    scopus 로고
    • Mouse skin passage of Streptococcus pyogenes results in increased streptokinase expression and activity
    • Rezcallah, M. S., Boyle, M. D., Sledjeski, D. D. Mouse skin passage of Streptococcus pyogenes results in increased streptokinase expression and activity. Microbiology 150, 365-371 (2004).
    • (2004) Microbiology , vol.150 , pp. 365-371
    • Rezcallah, M.S.1    Boyle, M.D.2    Sledjeski, D.D.3
  • 41
    • 0035818973 scopus 로고    scopus 로고
    • Group A Streptococcus tissue invasion by CD44-mediated cell signaling
    • Cywes, C., Wessels, M. R. Group A Streptococcus tissue invasion by CD44-mediated cell signaling. Nature 414, 648-652 (2001).
    • (2001) Nature , vol.414 , pp. 648-652
    • Cywes, C.1    Wessels, M.R.2
  • 42
    • 4344601240 scopus 로고    scopus 로고
    • Plasminogen is a critical host pathogenicity factor for group A streptococcal infection
    • Sun, H. et al. Plasminogen is a critical host pathogenicity factor for group A streptococcal infection. Science 305, 1283-1286 (2004).
    • (2004) Science , vol.305 , pp. 1283-1286
    • Sun, H.1
  • 43
    • 0025861975 scopus 로고
    • Shuttle vectors containing a multiple cloning site and a lacZ' gene for conjugal transfer of DNA from Escherichia coli to gram-positive bacteria
    • Trieu-Cuot, P., Carlier, C., Poyart-Salmeron, C., Courvalin, P. Shuttle vectors containing a multiple cloning site and a lacZ? gene for conjugal transfer of DNA from Escherichia coli to gram-positive bacteria. Gene 102, 99-104 (1991).
    • (1991) Gene , vol.102 , pp. 99-104
    • Trieu-Cuot, P.1    Carlier, C.2    Poyart-Salmeron, C.3    Courvalin, P.4
  • 44
    • 0034781075 scopus 로고    scopus 로고
    • Thermosensitive suicide vectors for gene replacement in Streptococcus suis
    • Takamatsu, D., Osaki, M., Sekizaki, T. Thermosensitive suicide vectors for gene replacement in Streptococcus suis. Plasmid 46, 140-148 (2001).
    • (2001) Plasmid , vol.46 , pp. 140-148
    • Takamatsu, D.1    Osaki, M.2    Sekizaki, T.3
  • 45
    • 80054827495 scopus 로고    scopus 로고
    • Assembly mechanism of FCT region type 1 pili in serotype M6 Streptococcus pyogenes
    • Nakata, M. et al. Assembly mechanism of FCT region type 1 pili in serotype M6 Streptococcus pyogenes. J. Biol. Chem. 286, 37566-37577 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 37566-37577
    • Nakata, M.1
  • 46
    • 58449108647 scopus 로고    scopus 로고
    • Mode of expression and functional characterization of FCT-3 pilus region-encoded proteins in Streptococcus pyogenes serotype M49
    • Nakata, M. et al. Mode of expression and functional characterization of FCT-3 pilus region-encoded proteins in Streptococcus pyogenes serotype M49. Infect. Immun. 77, 32-44 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 32-44
    • Nakata, M.1
  • 47
    • 61349132103 scopus 로고    scopus 로고
    • PfbA a novel plasmin-and fibronectin-binding protein of Streptococcus pneumoniae, contributes to fibronectin-dependent adhesion and antiphagocytosis
    • Yamaguchi, M., Terao, Y., Mori, Y., Hamada, S., Kawabata, S. PfbA, a novel plasmin-and fibronectin-binding protein of Streptococcus pneumoniae, contributes to fibronectin-dependent adhesion and antiphagocytosis. J. Biol. Chem. 283, 36272-36279 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 36272-36279
    • Yamaguchi, M.1    Terao, Y.2    Mori, Y.3    Hamada, S.4    Kawabata, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.