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Volumn 320, Issue 2, 2004, Pages 347-353

Identification and characterization of bacterial-binding property in the type III repeat domain of fibronectin

Author keywords

Bacterial adherence; Bacterial infections; Fibronectin; Granulicatella adiacens; Infective endocarditis; Monoclonal antibodies; Staphylococcus aureus; Streptococcus pyogenes

Indexed keywords

EPITOPE; FIBRONECTIN; LYSYLENDOPEPTIDASE; MONOCLONAL ANTIBODY; PROTEIN; THERMOLYSIN; UNCLASSIFIED DRUG;

EID: 2942720646     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.05.170     Document Type: Article
Times cited : (8)

References (30)
  • 1
    • 0019412005 scopus 로고
    • Bacterial adherence: Adhesin-receptor interactions mediating the attachment of bacteria to mucosal surface
    • Beachey E.H. Bacterial adherence: adhesin-receptor interactions mediating the attachment of bacteria to mucosal surface. J. Infect. Dis. 73:1993;325-345
    • (1993) J. Infect. Dis. , vol.73 , pp. 325-345
    • Beachey, E.H.1
  • 3
    • 0032767986 scopus 로고    scopus 로고
    • Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells
    • Joh D., Wann E.R., Kreikemeyer B., Speziale P., Höök M. Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells. Matrix Biol. 18:1999;211-223
    • (1999) Matrix Biol. , vol.18 , pp. 211-223
    • Joh, D.1    Wann, E.R.2    Kreikemeyer, B.3    Speziale, P.4    Höök, M.5
  • 4
    • 0028074251 scopus 로고
    • Microbial adhesins recognizing extracellular matrix macromolecules
    • Patti J.M., Höök M. Microbial adhesins recognizing extracellular matrix macromolecules. Curr. Opin. Cell Biol. 245:1994;752-758
    • (1994) Curr. Opin. Cell Biol. , vol.245 , pp. 752-758
    • Patti, J.M.1    Höök, M.2
  • 5
    • 0022329619 scopus 로고
    • Microbial adhesion to fibronectin in vitro correlates with production of endocarditis in rabbits
    • Scheld W.M., Strunk R.W., Balian G., Calderone R.A. Microbial adhesion to fibronectin in vitro correlates with production of endocarditis in rabbits. Proc. Soc. Exp. Biol. Med. 180:1985;474-482
    • (1985) Proc. Soc. Exp. Biol. Med. , vol.180 , pp. 474-482
    • Scheld, W.M.1    Strunk, R.W.2    Balian, G.3    Calderone, R.A.4
  • 7
    • 0027292986 scopus 로고
    • Bacterial proteins binding to the mammalian extracellular matrix
    • Westerlund B., Korhonen T.K. Bacterial proteins binding to the mammalian extracellular matrix. Mol. Microbiol. 9:1993;687-694
    • (1993) Mol. Microbiol. , vol.9 , pp. 687-694
    • Westerlund, B.1    Korhonen, T.K.2
  • 8
    • 0001479623 scopus 로고    scopus 로고
    • Role of fibronectin in infective endocarditis
    • Hamill R.J. Role of fibronectin in infective endocarditis. Rev. Infect. Dis. 18:1999;S360-S371
    • (1999) Rev. Infect. Dis. , vol.18 , pp. 360-S371
    • Hamill, R.J.1
  • 9
    • 0028177278 scopus 로고
    • Fibronectin receptors from gram-positive bacteria: Comparison of active sites
    • Joh H.J., House-Pompeo K., Patti J.M., Gurusiddappa S., Höök M. Fibronectin receptors from gram-positive bacteria: comparison of active sites. Biochemistry. 33:1994;6086-6092
    • (1994) Biochemistry , vol.33 , pp. 6086-6092
    • Joh, H.J.1    House-Pompeo, K.2    Patti, J.M.3    Gurusiddappa, S.4    Höök, M.5
  • 10
    • 0032401520 scopus 로고    scopus 로고
    • Multiple specificities of the staphylococcal and streptococcal fibronectin-binding microbial surface components recognizing adhesive matrix molecules
    • Joh D., Speziale P., Gurusiddappa S., Manor J., Höök M. Multiple specificities of the staphylococcal and streptococcal fibronectin-binding microbial surface components recognizing adhesive matrix molecules. Eur. J. Biochem. 258:1998;897-905
    • (1998) Eur. J. Biochem. , vol.258 , pp. 897-905
    • Joh, D.1    Speziale, P.2    Gurusiddappa, S.3    Manor, J.4    Höök, M.5
  • 12
    • 0025884213 scopus 로고
    • Nutritionally variant streptococci
    • Ruoff K.L. Nutritionally variant streptococci. Clin. Microbiol. Rev. 4:1991;184-190
    • (1991) Clin. Microbiol. Rev. , vol.4 , pp. 184-190
    • Ruoff, K.L.1
  • 13
    • 0029004222 scopus 로고
    • Human endocarditis due to nutritionally variant streptococci: Streptococcus adjacens and Streptococcus defectivus
    • Bouvet A. Human endocarditis due to nutritionally variant streptococci: Streptococcus adjacens and Streptococcus defectivus. Eur. Heart J. 16S:1995;24-27
    • (1995) Eur. Heart J. , vol.16 , pp. 24-27
    • Bouvet, A.1
  • 14
    • 0030296659 scopus 로고    scopus 로고
    • Isolation and properties of bacteriolytic enzyme-producing cocci from the human mouth
    • Kanamoto T., Eifuku-Koreeda H., Inoue M. Isolation and properties of bacteriolytic enzyme-producing cocci from the human mouth. FEMS Microbiol. Lett. 144:1996;135-140
    • (1996) FEMS Microbiol. Lett. , vol.144 , pp. 135-140
    • Kanamoto, T.1    Eifuku-Koreeda, H.2    Inoue, M.3
  • 15
    • 0033973931 scopus 로고    scopus 로고
    • Endocardiac infectivity and binding to extracellular matrix proteins of oral Abiotrophia species
    • Okada Y., Kitada K., Takagaki M., Ito H.-O., Inoue M. Endocardiac infectivity and binding to extracellular matrix proteins of oral Abiotrophia species. FEMS Immunol. Med. Microbiol. 27:2000;257-261
    • (2000) FEMS Immunol. Med. Microbiol. , vol.27 , pp. 257-261
    • Okada, Y.1    Kitada, K.2    Takagaki, M.3    Ito, H.-O.4    Inoue, M.5
  • 16
    • 0022388612 scopus 로고
    • Role of culture conditions and immunization in experimental nutritionally variant streptococcal endocarditis
    • van de Rijn I. Role of culture conditions and immunization in experimental nutritionally variant streptococcal endocarditis. Infect. Immun. 50:1985;641-646
    • (1985) Infect. Immun. , vol.50 , pp. 641-646
    • Van De Rijn, I.1
  • 17
    • 0142091814 scopus 로고    scopus 로고
    • Inhibition of fibronectin binding of some bacterial cells by subtle pH increase within the physiological range
    • Ito H.-O., Soutome S., Inoue M. Inhibition of fibronectin binding of some bacterial cells by subtle pH increase within the physiological range. J. Microbiol. Methods. 55:2003;29-34
    • (2003) J. Microbiol. Methods , vol.55 , pp. 29-34
    • Ito, H.-O.1    Soutome, S.2    Inoue, M.3
  • 18
    • 2942726560 scopus 로고    scopus 로고
    • Adherence of Streptococcus sanguis to conformationally specific determinants in fibronectin
    • Lowrance J.H., Hasty D.L., Simpson W.A. Adherence of Streptococcus sanguis to conformationally specific determinants in fibronectin. Infect. Immun. 64:1996;2279-2285
    • (1996) Infect. Immun. , vol.64 , pp. 2279-2285
    • Lowrance, J.H.1    Hasty, D.L.2    Simpson, W.A.3
  • 19
    • 0029794139 scopus 로고    scopus 로고
    • Cell surface polypeptide CshA mediates binding of Streptococcus gordonii to other oral bacteria and to immobilized fibronectin
    • McNab R., Holmes A.R., Clarke J.M., Tannock G.W., Jenkinson H.F. Cell surface polypeptide CshA mediates binding of Streptococcus gordonii to other oral bacteria and to immobilized fibronectin. Infect. Immun. 64:1996;4204-4210
    • (1996) Infect. Immun. , vol.64 , pp. 4204-4210
    • McNab, R.1    Holmes, A.R.2    Clarke, J.M.3    Tannock, G.W.4    Jenkinson, H.F.5
  • 21
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler G., Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 256:1975;495-497
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 22
    • 0027498434 scopus 로고
    • Rapid induction of anti-idiotypic responses to unmodified monoclonal antibodies from syngeneic mice following primary immunization
    • Grivel J.C., Ferrier P., Renard N., Jolly G., Jarry T., Leserman L. Rapid induction of anti-idiotypic responses to unmodified monoclonal antibodies from syngeneic mice following primary immunization. J. Immunol. Methods. 158:1993;173-182
    • (1993) J. Immunol. Methods , vol.158 , pp. 173-182
    • Grivel, J.C.1    Ferrier, P.2    Renard, N.3    Jolly, G.4    Jarry, T.5    Leserman, L.6
  • 23
    • 2642682427 scopus 로고    scopus 로고
    • A novel approach for detecting an immunodominant antigen of Porphyromonas gingivalis in diagnosis of adult periodontitis
    • Kawai T., Ito H.-O., Sakato N., Okada H. A novel approach for detecting an immunodominant antigen of Porphyromonas gingivalis in diagnosis of adult periodontitis. Clin. Diagn. Lab. Immunol. 5:1998;11-17
    • (1998) Clin. Diagn. Lab. Immunol. , vol.5 , pp. 11-17
    • Kawai, T.1    Ito, H.-O.2    Sakato, N.3    Okada, H.4
  • 24
    • 0020553956 scopus 로고
    • Domain structure of human plasma fibronectin. Differences and similarities between human and hamster fibronectins
    • Sekiguchi K., Hakomori S. Domain structure of human plasma fibronectin. Differences and similarities between human and hamster fibronectins. J. Biol. Chem. 258:1983;3967-3973
    • (1983) J. Biol. Chem. , vol.258 , pp. 3967-3973
    • Sekiguchi, K.1    Hakomori, S.2
  • 25
    • 0021855104 scopus 로고
    • Differences in domain structure between human fibronectins isolated from plasma and from culture supernatants of normal and transformed fibroblasts. Studies with domain-specific antibodies
    • Sekiguchi K., Siri A., Zardi L., Hakomori S. Differences in domain structure between human fibronectins isolated from plasma and from culture supernatants of normal and transformed fibroblasts. Studies with domain-specific antibodies. J. Biol. Chem. 260:1985;5105-5114
    • (1985) J. Biol. Chem. , vol.260 , pp. 5105-5114
    • Sekiguchi, K.1    Siri, A.2    Zardi, L.3    Hakomori, S.4
  • 26
    • 0030799765 scopus 로고    scopus 로고
    • Quaternary structure-dependent idiotope and antigen binding of a monoclonal antibody specific for conformational epitope on type II collagen
    • Ito H.-O., Ueda T., Hashimoto Y., Imoto T., Koga T. Quaternary structure-dependent idiotope and antigen binding of a monoclonal antibody specific for conformational epitope on type II collagen. Cell. Mol. Life Sci. 53:1997;51-60
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 51-60
    • Ito, H.-O.1    Ueda, T.2    Hashimoto, Y.3    Imoto, T.4    Koga, T.5
  • 27
    • 0022102304 scopus 로고
    • Primary structure of human fibronectin: Differential splicing may generate at least 10 polypeptides from a single gene
    • Kornblihtt A.R., Umezawa K., Vibe-Pedersen K., Baralle F.E. Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene. EMBO J. 4:1985;1755-1759
    • (1985) EMBO J. , vol.4 , pp. 1755-1759
    • Kornblihtt, A.R.1    Umezawa, K.2    Vibe-Pedersen, K.3    Baralle, F.E.4
  • 28
    • 0034045243 scopus 로고    scopus 로고
    • Fibronectin peptides in cell migration and wound repair
    • Yamada K.M. Fibronectin peptides in cell migration and wound repair. J. Clin. Invest. 105:2000;1507-1509
    • (2000) J. Clin. Invest. , vol.105 , pp. 1507-1509
    • Yamada, K.M.1
  • 29
    • 0028649494 scopus 로고
    • Binding of plasma fibronectin to Candida albicans occurs through the cell binding domain
    • Penn C., Klotz S.A. Binding of plasma fibronectin to Candida albicans occurs through the cell binding domain. Microb. Pathog. 17:1994;387-393
    • (1994) Microb. Pathog. , vol.17 , pp. 387-393
    • Penn, C.1    Klotz, S.A.2
  • 30
    • 0027153128 scopus 로고
    • Effects of polystyrene surface chemistry on the biological activity of solid phase fibronectin and vitronectin, analysed with monoclonal antibodies
    • Underwood P.A., Steele J.G., Dalton B.A. Effects of polystyrene surface chemistry on the biological activity of solid phase fibronectin and vitronectin, analysed with monoclonal antibodies. J. Cell Sci. 104:1993;793-803
    • (1993) J. Cell Sci. , vol.104 , pp. 793-803
    • Underwood, P.A.1    Steele, J.G.2    Dalton, B.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.