메뉴 건너뛰기




Volumn 189, Issue 12, 2007, Pages 4539-4543

pH-dependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHLORAMPHENICOL; ENOLASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LIPOTEICHOIC ACID; MEMBRANE PROTEIN; PLASMINOGEN;

EID: 34250333853     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00378-07     Document Type: Article
Times cited : (115)

References (23)
  • 1
    • 0038460041 scopus 로고    scopus 로고
    • Surface localized glyceraldehyde-3-phosphate dehydrogenase of Mycoplasma genitalium binds mucin
    • Alvarez, R. A., M. W. Blaylock, and J. B. Baseman. 2003. Surface localized glyceraldehyde-3-phosphate dehydrogenase of Mycoplasma genitalium binds mucin. Mol. Microbiol. 48:1417-1425.
    • (2003) Mol. Microbiol , vol.48 , pp. 1417-1425
    • Alvarez, R.A.1    Blaylock, M.W.2    Baseman, J.B.3
  • 2
    • 0036430117 scopus 로고    scopus 로고
    • Domains in the S-layer protein CbsA of Lactobacillus crispatus involved in adherence to collagens, laminin and lipoteichoic acids and in self-assembly
    • Antikainen, J., L. Anton, J. Sillanpaii, and T. K. Korhonen. 2002. Domains in the S-layer protein CbsA of Lactobacillus crispatus involved in adherence to collagens, laminin and lipoteichoic acids and in self-assembly. Mol. Microbiol. 46:381-394.
    • (2002) Mol. Microbiol , vol.46 , pp. 381-394
    • Antikainen, J.1    Anton, L.2    Sillanpaii, J.3    Korhonen, T.K.4
  • 3
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann, S., M. Rohde, and S. Hammerschmidt. 2004. Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein. Infect. Immun. 72:2416-2419.
    • (2004) Infect. Immun , vol.72 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 4
    • 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., M. Rohde, K. T. Preissner, and S. Hammerschmidt. 2005. 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. Haemostasis 94:304-311.
    • (2005) Thromb. Haemostasis , vol.94 , pp. 304-311
    • Bergmann, S.1    Rohde, M.2    Preissner, K.T.3    Hammerschmidt, S.4
  • 5
    • 0034931519 scopus 로고    scopus 로고
    • α-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann, S., M. Rohde, G. S. Chhatwal, and S. Hammerschmidt. 2001. α-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol. Microbiol. 40:1273-1287.
    • (2001) Mol. Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 6
    • 25444529704 scopus 로고    scopus 로고
    • Inhibition of cell surface export of group A streptococcal anchorless surface dehydrogenase affects bacterial adherence and antiphagocytic properties
    • Boël, G., H. Jin, and V. Pancholi. 2005. Inhibition of cell surface export of group A streptococcal anchorless surface dehydrogenase affects bacterial adherence and antiphagocytic properties. Infect. Immun. 73:6237-6248.
    • (2005) Infect. Immun , vol.73 , pp. 6237-6248
    • Boël, G.1    Jin, H.2    Pancholi, V.3
  • 10
    • 7044230038 scopus 로고    scopus 로고
    • Streptococcus mutans surface alpha-enolase binds salivary mucin MG2 and human plasminogen
    • Ge, J., D. M. Catt, and R. L. Gregory. 2004. Streptococcus mutans surface alpha-enolase binds salivary mucin MG2 and human plasminogen. Infect. Immun. 72:6748-6752.
    • (2004) Infect. Immun , vol.72 , pp. 6748-6752
    • Ge, J.1    Catt, D.M.2    Gregory, R.L.3
  • 14
    • 0033404562 scopus 로고    scopus 로고
    • Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: A novel mechanism of protein association at the surface of gram-positive bacteria
    • Jonquieres, R., H. Bierne, F. Fiedler, P. Gounon, and P. Cossart. 1999. Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: a novel mechanism of protein association at the surface of gram-positive bacteria. Mol. Microbiol. 34:902-914.
    • (1999) Mol. Microbiol , vol.34 , pp. 902-914
    • Jonquieres, R.1    Bierne, H.2    Fiedler, F.3    Gounon, P.4    Cossart, P.5
  • 15
    • 0026673916 scopus 로고
    • Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor
    • Lottenberg, R., C. C. Broder, M. D. Boyle, S. J. Kain, B. L. Schroeder, and R. Curtiss III. 1992. Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor. J. Bacteriol. 174:5204-5210.
    • (1992) J. Bacteriol , vol.174 , pp. 5204-5210
    • Lottenberg, R.1    Broder, C.C.2    Boyle, M.D.3    Kain, S.J.4    Schroeder, B.L.5    Curtiss III, R.6
  • 16
    • 0034986066 scopus 로고    scopus 로고
    • pH-regulated secretion of a glyceraldehyde-3-phosphate dehydrogenase from Streptococcus gordonii FSS2: Purification, characterization, and cloning of the gene encoding this enzyme
    • Nelson, D., J. M. Goldstein, K. Boatright, D. W. Harty, S. L. Cook, P. J. Hickman, J. Potempa, J. Travis, and J. A. Mayo. 2001. pH-regulated secretion of a glyceraldehyde-3-phosphate dehydrogenase from Streptococcus gordonii FSS2: purification, characterization, and cloning of the gene encoding this enzyme. J. Dent. Res. 80:371-377.
    • (2001) J. Dent. Res , vol.80 , pp. 371-377
    • Nelson, D.1    Goldstein, J.M.2    Boatright, K.3    Harty, D.W.4    Cook, S.L.5    Hickman, P.J.6    Potempa, J.7    Travis, J.8    Mayo, J.A.9
  • 17
    • 0032486286 scopus 로고    scopus 로고
    • α-Enolase, a novel strong plasmin( ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi, V., and V. A. Fischetti. 1998. α-Enolase, a novel strong plasmin( ogen) binding protein on the surface of pathogenic streptococci. J. Biol. Chem. 273:14503-14515.
    • (1998) J. Biol. Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 18
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi, V., and V. A. Fischetti. 1992. 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) J. Exp. Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 20
    • 0141834741 scopus 로고    scopus 로고
    • Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: Surface localization, enzymatic activity, and protein-protein interactions
    • Seifert, K. N., W. P. McArthur, A. S. Bleiweis, and L. J. Brady. 2003. Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: surface localization, enzymatic activity, and protein-protein interactions. Can. J. Microbiol. 49:350-356.
    • (2003) Can. J. Microbiol , vol.49 , pp. 350-356
    • Seifert, K.N.1    McArthur, W.P.2    Bleiweis, A.S.3    Brady, L.J.4
  • 21
    • 33744901493 scopus 로고    scopus 로고
    • Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils
    • Terao, Y., M. Yamaguchi, S. Hamada, and S. Kawabata. 2006. Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils. J. Biol. Chem. 281:14215-14223.
    • (2006) J. Biol. Chem , vol.281 , pp. 14215-14223
    • Terao, Y.1    Yamaguchi, M.2    Hamada, S.3    Kawabata, S.4
  • 23
    • 0025857363 scopus 로고
    • Fluorescent microparticlcs as a rapid tool in bacterial adherence studies
    • Westerlund, B. 1991. Fluorescent microparticlcs as a rapid tool in bacterial adherence studies. J. Microbiol. Methods 13:135-143.
    • (1991) J. Microbiol. Methods , vol.13 , pp. 135-143
    • Westerlund, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.