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Volumn 26, Issue 1, 1999, Pages 49-60

Enterococcus faecalis aggregation substance promotes opsonin-independent binding to human neutrophils via a complement receptor type 3-mediated mechanism

Author keywords

Aggregation substance; Complement receptor; Enterococcus faecalis; Neutrophil

Indexed keywords

ADHESIN; ARGINYLGLYCYLASPARTIC ACID; CD11B ANTIGEN; CD18 ANTIGEN; CD47 ANTIGEN; CELL SURFACE RECEPTOR; COMPLEMENT RECEPTOR; L SELECTIN; MONOCLONAL ANTIBODY; OPSONIN; SEX PHEROMONE;

EID: 0032851640     PISSN: 09288244     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0928-8244(99)00120-0     Document Type: Article
Times cited : (66)

References (53)
  • 1
    • 0025100795 scopus 로고
    • The life and times of the Enterococcus
    • Murray B.E. The life and times of the Enterococcus. Clin. Microbiol. Rev. 3:1990;46-65.
    • (1990) Clin. Microbiol. Rev. , vol.3 , pp. 46-65
    • Murray, B.E.1
  • 2
    • 0002391925 scopus 로고
    • Endocarditis and intravascular infections
    • (Mandell, G.L., Bennett, J.E. and Dolin, R., Eds.), Churchill-Livingstone, New York
    • Scheld, W.M. and Sande, M.A. (1995) Endocarditis and intravascular infections. In: Principles and Practice of Infectious Diseases (Mandell, G.L., Bennett, J.E. and Dolin, R., Eds.), pp. 740-782. Churchill-Livingstone, New York.
    • (1995) In: Principles and Practice of Infectious Diseases , pp. 740-782
    • Scheld, W.M.1    Sande, M.A.2
  • 3
    • 0031862259 scopus 로고    scopus 로고
    • Bacterial pathogens isolated from patients with bloodstream infection: Frequencies of occurrence and antimicrobial susceptibility patterns from the SENTRY antimicrobial surveillance program
    • Pfaller M.A., Jones R.N., Doern G.V., Kugler K. Bacterial pathogens isolated from patients with bloodstream infection: frequencies of occurrence and antimicrobial susceptibility patterns from the SENTRY antimicrobial surveillance program. Antimicrob. Agents Chemother. 42:1998;1762-1770.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1762-1770
    • Pfaller, M.A.1    Jones, R.N.2    Doern, G.V.3    Kugler, K.4
  • 5
    • 0028359024 scopus 로고
    • The sex pheromone system of Enterococcus faecalis
    • Wirth R. The sex pheromone system of Enterococcus faecalis. Eur. J. Biochem. 222:1994;235-246.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 235-246
    • Wirth, R.1
  • 6
    • 0028835708 scopus 로고
    • Pheromone-inducible conjugation in Enterococcus faecalis: Interbacterial and host-parasite chemical communication
    • Dunny G.M., Leonard B.A., Hedberg P.J. Pheromone-inducible conjugation in Enterococcus faecalis: interbacterial and host-parasite chemical communication. J. Bacteriol. 177:1995;871-876.
    • (1995) J. Bacteriol. , vol.177 , pp. 871-876
    • Dunny, G.M.1    Leonard, B.A.2    Hedberg, P.J.3
  • 7
    • 0026501829 scopus 로고
    • Aggregation substance of Enterococcus faecalis mediates adhesion to cultured renal tubular cells
    • Kreft B., Marre R., Schramm U., Wirth R. Aggregation substance of Enterococcus faecalis mediates adhesion to cultured renal tubular cells. Infect. Immun. 60:1992;25-30.
    • (1992) Infect. Immun. , vol.60 , pp. 25-30
    • Kreft, B.1    Marre, R.2    Schramm, U.3    Wirth, R.4
  • 8
    • 0028007337 scopus 로고
    • A plasmid-encoded surface protein on Enterococcus faecalis augments its internalization by cultured intestinal epithelial cells
    • Olmsted S.B., Dunny G.M., Erlandsen S.L., Wells C.L. A plasmid-encoded surface protein on Enterococcus faecalis augments its internalization by cultured intestinal epithelial cells. J. Infect. Dis. 170:1994;1549-1556.
    • (1994) J. Infect. Dis. , vol.170 , pp. 1549-1556
    • Olmsted, S.B.1    Dunny, G.M.2    Erlandsen, S.L.3    Wells, C.L.4
  • 9
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti E., Pierschbacher M.D. New perspectives in cell adhesion: RGD and integrins. Science. 238:1987;491-497.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 10
    • 0002553601 scopus 로고
    • Receptors for complement and the biology of phagocytosis
    • (Gallin, J.I., Goldstein, I.M. and Snyderman, R., Eds.), Raven Press, New York
    • Wright, S.D. (1992) Receptors for complement and the biology of phagocytosis. In: Inflammation: Basic Principles and Clinical Correlates, 2nd edn. (Gallin, J.I., Goldstein, I.M. and Snyderman, R., Eds.), pp. 477-495. Raven Press, New York.
    • (1992) In: Inflammation: Basic Principles and Clinical Correlates, 2nd Edn. , pp. 477-495
    • Wright, S.D.1
  • 11
    • 0024411402 scopus 로고
    • Cooperative interactions of LFA-1 and Mac-1 with intercellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophils in vitro
    • Smith C.W., Marling S.D., Rothlein R., Toman C., Anderson D.C. Cooperative interactions of LFA-1 and Mac-1 with intercellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophils in vitro. J. Clin. Invest. 83:1989;2008-2017.
    • (1989) J. Clin. Invest. , vol.83 , pp. 2008-2017
    • Smith, C.W.1    Marling, S.D.2    Rothlein, R.3    Toman, C.4    Anderson, D.C.5
  • 12
    • 0027218590 scopus 로고
    • Leukocyte response integrin and integrin-associated protein act as a signal transduction unit in generation of a phagocyte respiratory burst
    • Zhou M., Brown E. Leukocyte response integrin and integrin-associated protein act as a signal transduction unit in generation of a phagocyte respiratory burst. J. Exp. Med. 178:1993;1165-1174.
    • (1993) J. Exp. Med. , vol.178 , pp. 1165-1174
    • Zhou, M.1    Brown, E.2
  • 13
    • 0000118029 scopus 로고
    • Nonopsonic phagocytosis of microorganisms
    • Ofek I., Rest R.F., Sharon N. Nonopsonic phagocytosis of microorganisms. ASM News. 58:1992;429-435.
    • (1992) ASM News , vol.58 , pp. 429-435
    • Ofek, I.1    Rest, R.F.2    Sharon, N.3
  • 14
    • 0028001464 scopus 로고
    • Bordetella pertussis filamentous hemagglutinin interacts with a leukocyte signal transduction complex and stimulates bacterial adherence to monocyte CR3 (CD11b/CD18)
    • Ishibashi Y., Claus S., Relman D.A. Bordetella pertussis filamentous hemagglutinin interacts with a leukocyte signal transduction complex and stimulates bacterial adherence to monocyte CR3 (CD11b/CD18). J. Exp. Med. 180:1994;1225-1233.
    • (1994) J. Exp. Med. , vol.180 , pp. 1225-1233
    • Ishibashi, Y.1    Claus, S.2    Relman, D.A.3
  • 15
    • 0031279203 scopus 로고    scopus 로고
    • Synergy between L-selectin signaling and chemotactic activation during neutrophil adhesion and transmigration
    • Tsang Y.T.M., Neelamegham S., Hu Y., Berg E.L., Burns A.R., Smith C.W., Simon S.I. Synergy between L-selectin signaling and chemotactic activation during neutrophil adhesion and transmigration. J. Immunol. 159:1997;4566-4577.
    • (1997) J. Immunol. , vol.159 , pp. 4566-4577
    • Tsang, Y.T.M.1    Neelamegham, S.2    Hu, Y.3    Berg, E.L.4    Burns, A.R.5    Smith, C.W.6    Simon, S.I.7
  • 16
    • 0022639182 scopus 로고
    • Monoclonal antibody-defined functional epitopes on the adhesion-promoting glycoprotein complex (CDw18) of human neutrophils
    • Wallis W.J., Hickstein D.D., Schwartz B.R., June C.H., Ochs H.D., Beatty P.G., Klebanoff S.J., Harlan J.M. Monoclonal antibody-defined functional epitopes on the adhesion-promoting glycoprotein complex (CDw18) of human neutrophils. Blood. 67:1986;1007-1013.
    • (1986) Blood , vol.67 , pp. 1007-1013
    • Wallis, W.J.1    Hickstein, D.D.2    Schwartz, B.R.3    June, C.H.4    Ochs, H.D.5    Beatty, P.G.6    Klebanoff, S.J.7    Harlan, J.M.8
  • 17
    • 0022617584 scopus 로고
    • Contributions of the Mac-1 glycoprotein family to adherence-dependent granulocytic functions: Structure-function assessments employing subunit-specific monoclonal antibodies
    • Anderson D.C., Miller L.J., Schmalstieg F.C., Rothlein R., Springer T.A. Contributions of the Mac-1 glycoprotein family to adherence-dependent granulocytic functions: structure-function assessments employing subunit-specific monoclonal antibodies. J. Immunol. 137:1986;15-27.
    • (1986) J. Immunol. , vol.137 , pp. 15-27
    • Anderson, D.C.1    Miller, L.J.2    Schmalstieg, F.C.3    Rothlein, R.4    Springer, T.A.5
  • 18
    • 0026445442 scopus 로고
    • Neutrophil induced oxidative injury of cardiac myocytes. A compartmented system requiring CD11b/CD18-ICAM-1 adherence
    • Entman M.L., Youker K., Shoji T., Kukielka G., Shappell S.B., Taylor A.A., Smith C.W. Neutrophil induced oxidative injury of cardiac myocytes. A compartmented system requiring CD11b/CD18-ICAM-1 adherence. J. Clin. Invest. 90:1992;1335-1345.
    • (1992) J. Clin. Invest. , vol.90 , pp. 1335-1345
    • Entman, M.L.1    Youker, K.2    Shoji, T.3    Kukielka, G.4    Shappell, S.B.5    Taylor, A.A.6    Smith, C.W.7
  • 19
    • 0001686945 scopus 로고
    • Identification of the C3bi receptor of human monocytes and macrophages by using monoclonal antibodies
    • Wright S.D., et al. Identification of the C3bi receptor of human monocytes and macrophages by using monoclonal antibodies. Proc. Natl. Acad. Sci. USA. 80:1983;5699-5703.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5699-5703
    • Wright, S.D.1
  • 20
    • 0018154865 scopus 로고
    • Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens-new tools for genetic analysis
    • Barnstable C.J., Bodmer W.F., Brown G., Galfre G., Milstein C., Williams A.F., Ziegler A. Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens-new tools for genetic analysis. Cell. 14:1978;9-20.
    • (1978) Cell , vol.14 , pp. 9-20
    • Barnstable, C.J.1    Bodmer, W.F.2    Brown, G.3    Galfre, G.4    Milstein, C.5    Williams, A.F.6    Ziegler, A.7
  • 21
  • 22
    • 0025743612 scopus 로고
    • Function and evolutionary conservation of distinct epitopes on the leukocyte adhesion molecule-1 (TQ-1, Leu-8) that regulate leukocyte migration
    • Spertini O., Kansas G.S., Reimann K.A., Mackay C.R., Tedder T.F. Function and evolutionary conservation of distinct epitopes on the leukocyte adhesion molecule-1 (TQ-1, Leu-8) that regulate leukocyte migration. J. Immunol. 147:1991;942-949.
    • (1991) J. Immunol. , vol.147 , pp. 942-949
    • Spertini, O.1    Kansas, G.S.2    Reimann, K.A.3    Mackay, C.R.4    Tedder, T.F.5
  • 23
    • 0024506758 scopus 로고
    • A novel member of the integrin receptor family mediates Arg-Gly-Asp-stimulated neutrophil phagocytosis
    • Gresham D.H., Goodwin J.L., Allen D.M., Anderson D.C., Brown E.J. A novel member of the integrin receptor family mediates Arg-Gly-Asp-stimulated neutrophil phagocytosis. J. Cell Biol. 108:1989;1935-1943.
    • (1989) J. Cell Biol. , vol.108 , pp. 1935-1943
    • Gresham, D.H.1    Goodwin, J.L.2    Allen, D.M.3    Anderson, D.C.4    Brown, E.J.5
  • 24
    • 0026639262 scopus 로고
    • Ligand binding specificity of the leukocyte response integrin expressed by human neutrophils
    • Gresham H.D., Adams S.P., Brown E.J. Ligand binding specificity of the leukocyte response integrin expressed by human neutrophils. J. Biol. Chem. 267:1992;13895-13902.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13895-13902
    • Gresham, H.D.1    Adams, S.P.2    Brown, E.J.3
  • 25
    • 0025666501 scopus 로고
    • Integrin associated protein: A 50-kDa plasma membrane antigen physically and functionally associated with integrins
    • Brown E., Hooper L., Ho T., Gresham H. Integrin associated protein: a 50-kDa plasma membrane antigen physically and functionally associated with integrins. J. Cell Biol. 111:1990;2785-2794.
    • (1990) J. Cell Biol. , vol.111 , pp. 2785-2794
    • Brown, E.1    Hooper, L.2    Ho, T.3    Gresham, H.4
  • 27
    • 0026601096 scopus 로고
    • Divalent cation regulation of the function of the leukocyte integrin LFA-1
    • Dransfield I., Cabanas C., Craig A., Hogg N. Divalent cation regulation of the function of the leukocyte integrin LFA-1. J. Cell Biol. 116:1992;219-226.
    • (1992) J. Cell Biol. , vol.116 , pp. 219-226
    • Dransfield, I.1    Cabanas, C.2    Craig, A.3    Hogg, N.4
  • 28
    • 0024814732 scopus 로고
    • Regulated expression of Mg+2 binding epitope on leukocyte integrin alpha subunits
    • Dransfield I., Hogg N. Regulated expression of Mg+2 binding epitope on leukocyte integrin alpha subunits. EMBO J. 8:1989;3759-3765.
    • (1989) EMBO J. , vol.8 , pp. 3759-3765
    • Dransfield, I.1    Hogg, N.2
  • 29
    • 0025787981 scopus 로고
    • Role of the pheromone-inducible surface protein Asc10 in mating aggregate formation and conjugal transfer of the Enterococcus faecalis plasmid pCF10
    • Olmsted S.B., Kao S.-M., van Putte L.J., Gallo J.C., Dunny G.M. Role of the pheromone-inducible surface protein Asc10 in mating aggregate formation and conjugal transfer of the Enterococcus faecalis plasmid pCF10. J. Bacteriol. 173:1991;7665-7672.
    • (1991) J. Bacteriol. , vol.173 , pp. 7665-7672
    • Olmsted, S.B.1    Kao, S.-M.2    Van Putte, L.J.3    Gallo, J.C.4    Dunny, G.M.5
  • 30
    • 0027258080 scopus 로고
    • Cloning and characterization of a region of the Enterococcus faecalis conjugative plasmid, pCF10, encoding a sex pheromone-binding function
    • Ruhfel R.E., Manias D.A., Dunny G.M. Cloning and characterization of a region of the Enterococcus faecalis conjugative plasmid, pCF10, encoding a sex pheromone-binding function. J. Bacteriol. 175:1993;5253-5259.
    • (1993) J. Bacteriol. , vol.175 , pp. 5253-5259
    • Ruhfel, R.E.1    Manias, D.A.2    Dunny, G.M.3
  • 31
    • 0025999897 scopus 로고
    • Phagocytosis of opsonized oil droplets by neutrophils
    • Rosen H., Michel B.R., Chait A. Phagocytosis of opsonized oil droplets by neutrophils. J. Immunol. Methods. 144:1991;117-125.
    • (1991) J. Immunol. Methods , vol.144 , pp. 117-125
    • Rosen, H.1    Michel, B.R.2    Chait, A.3
  • 32
    • 0027530684 scopus 로고
    • The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands
    • Diamond M.S., Garcia-Aguilar J., Bickford J.K., Corbi A.L., Springer T.A. The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands. J. Cell Biol. 120:1993;1031-1043.
    • (1993) J. Cell Biol. , vol.120 , pp. 1031-1043
    • Diamond, M.S.1    Garcia-Aguilar, J.2    Bickford, J.K.3    Corbi, A.L.4    Springer, T.A.5
  • 33
    • 0028104551 scopus 로고
    • Resistance of Enterococcus faecium to neutrophil-mediated phagocytosis
    • Arduino R.C., Jacques-Palaz K., Murray B.E., Rakita R.M. Resistance of Enterococcus faecium to neutrophil-mediated phagocytosis. Infect. Immun. 62:1994;5587-5594.
    • (1994) Infect. Immun. , vol.62 , pp. 5587-5594
    • Arduino, R.C.1    Jacques-Palaz, K.2    Murray, B.E.3    Rakita, R.M.4
  • 34
    • 0025861150 scopus 로고
    • Macrophage phagocytosis: Use of fluorescence microscopy to distinguish between extracellular and intracellular bacteria
    • Drevets D.A., Campbell P.A. Macrophage phagocytosis: use of fluorescence microscopy to distinguish between extracellular and intracellular bacteria. J. Immunol. Methods. 142:1991;31-38.
    • (1991) J. Immunol. Methods , vol.142 , pp. 31-38
    • Drevets, D.A.1    Campbell, P.A.2
  • 35
    • 0026655108 scopus 로고
    • Consequences of microbial attachment: Directing host cell functions with adhesins
    • Hoepelman A.I.M., Tuomanen E.I. Consequences of microbial attachment: directing host cell functions with adhesins. Infect. Immun. 60:1992;1729-1733.
    • (1992) Infect. Immun. , vol.60 , pp. 1729-1733
    • Hoepelman, A.I.M.1    Tuomanen, E.I.2
  • 36
    • 0025719026 scopus 로고
    • Identification of the leukocyte adhesion molecules CD11and CD18 as receptors for type 1-fimbriated (mannose-specific) Escherichia coli
    • Gbarah A., Gahmberg C.G., Ofek I., Jacobi U., Sharon N. Identification of the leukocyte adhesion molecules CD11and CD18 as receptors for type 1-fimbriated (mannose-specific) Escherichia coli. Infect. Immun. 59:1991;4524-4530.
    • (1991) Infect. Immun. , vol.59 , pp. 4524-4530
    • Gbarah, A.1    Gahmberg, C.G.2    Ofek, I.3    Jacobi, U.4    Sharon, N.5
  • 38
    • 0027483226 scopus 로고
    • A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding
    • Michishita M., Videm V., Arnaout M.A. A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell. 72:1993;857-867.
    • (1993) Cell , vol.72 , pp. 857-867
    • Michishita, M.1    Videm, V.2    Arnaout, M.A.3
  • 39
    • 0029062047 scopus 로고
    • Energetics of leukocyte integrin activation
    • Cai T.-Q., Wright S.D. Energetics of leukocyte integrin activation. J. Biol. Chem. 270:1995;14358-14365.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14358-14365
    • Cai, T.-Q.1    Wright, S.D.2
  • 41
    • 0029852227 scopus 로고    scopus 로고
    • Nonopsonic binding of Mycobacterium tuberculosis to human complement receptor type 3 expressed in chinese hamster ovary cells
    • Cywes C., Godenir N.L., Noppe H.C., Scholle R.R., Steyn L.M., Kirsch R.E., Ehlers M.R.W. Nonopsonic binding of Mycobacterium tuberculosis to human complement receptor type 3 expressed in chinese hamster ovary cells. Infect. Immun. 64:1996;5373-5383.
    • (1996) Infect. Immun. , vol.64 , pp. 5373-5383
    • Cywes, C.1    Godenir, N.L.2    Noppe, H.C.3    Scholle, R.R.4    Steyn, L.M.5    Kirsch, R.E.6    Ehlers, M.R.W.7
  • 42
    • 14444270344 scopus 로고    scopus 로고
    • Nonopsonic binding of Mycobacterium tuberculosis to complement receptor type 3 is mediated by capsular polysaccharides and is strain dependent
    • Cywes C., Hoppe H.C., Daffe M., Ehlers M.R.W. Nonopsonic binding of Mycobacterium tuberculosis to complement receptor type 3 is mediated by capsular polysaccharides and is strain dependent. Infect. Immun. 65:1997;4258-4266.
    • (1997) Infect. Immun. , vol.65 , pp. 4258-4266
    • Cywes, C.1    Hoppe, H.C.2    Daffe, M.3    Ehlers, M.R.W.4
  • 43
    • 0029949714 scopus 로고    scopus 로고
    • Role for L-selectin in lipopolysaccharide-induced activation of neutrophils
    • Malhotra R., Priest R., Bird M.I. Role for L-selectin in lipopolysaccharide-induced activation of neutrophils. Biochem. J. 320:1996;589-593.
    • (1996) Biochem. J. , vol.320 , pp. 589-593
    • Malhotra, R.1    Priest, R.2    Bird, M.I.3
  • 44
    • 0021080912 scopus 로고
    • Receptors for C3b and C3bi promote phagocytosis but not the release of toxic oxygen from human phagocytes
    • Wright S.D., Silverstein S.C. Receptors for C3b and C3bi promote phagocytosis but not the release of toxic oxygen from human phagocytes. J. Exp. Med. 158:1983;2016-2023.
    • (1983) J. Exp. Med. , vol.158 , pp. 2016-2023
    • Wright, S.D.1    Silverstein, S.C.2
  • 46
  • 47
    • 0023192968 scopus 로고
    • High incidence of hemolysin production by Enterococcus (Streptococcus) faecalis strains associated with human parenteral infections
    • Ike Y., Hashimoto H., Clewell D.B. High incidence of hemolysin production by Enterococcus (Streptococcus) faecalis strains associated with human parenteral infections. J. Clin. Microbiol. 25:1987;1524-1528.
    • (1987) J. Clin. Microbiol. , vol.25 , pp. 1524-1528
    • Ike, Y.1    Hashimoto, H.2    Clewell, D.B.3
  • 48
    • 0028929250 scopus 로고
    • Incidence of hemolysin, gelatinase, and aggregation substance among Enterococci isolated from patients with endocarditis and other infections and from feces of hospitalized and community-based persons
    • Coque T.M., Patterson M.E., Steckelberg J.M., Murray B.E. Incidence of hemolysin, gelatinase, and aggregation substance among Enterococci isolated from patients with endocarditis and other infections and from feces of hospitalized and community-based persons. J. Infect. Dis. 171:1995;1223-1229.
    • (1995) J. Infect. Dis. , vol.171 , pp. 1223-1229
    • Coque, T.M.1    Patterson, M.E.2    Steckelberg, J.M.3    Murray, B.E.4
  • 49
    • 0028078913 scopus 로고
    • Complement and tumor necrosis factor-α contribute to Mac-1 (CD11b/CD18) up-regulation and systemic neutrophil activation during endotoxemia in vivo
    • Witthaut R., Farhood A., Smith C.W., Jaeschke H. Complement and tumor necrosis factor-α contribute to Mac-1 (CD11b/CD18) up-regulation and systemic neutrophil activation during endotoxemia in vivo. J. Leukoc. Biol. 55:1994;105-111.
    • (1994) J. Leukoc. Biol. , vol.55 , pp. 105-111
    • Witthaut, R.1    Farhood, A.2    Smith, C.W.3    Jaeschke, H.4
  • 50
    • 0018746513 scopus 로고
    • Plasmid transfer in Streptococcus faecalis: Production of multiple pheromones by recipients
    • Dunny G.M., Craig R.A., Carron R.L., Clewell D.B. Plasmid transfer in Streptococcus faecalis: production of multiple pheromones by recipients. Plasmid. 2:1979;454-465.
    • (1979) Plasmid , vol.2 , pp. 454-465
    • Dunny, G.M.1    Craig, R.A.2    Carron, R.L.3    Clewell, D.B.4
  • 51
    • 0022479582 scopus 로고
    • Highly efficient protoplast transformation system for Streptococcus faecalis and a new Escherichia coli-S. faecalis shuttle vector
    • Wirth R., An F.Y., Clewell D.B. Highly efficient protoplast transformation system for Streptococcus faecalis and a new Escherichia coli-S. faecalis shuttle vector. J. Bacteriol. 165:1986;831-836.
    • (1986) J. Bacteriol. , vol.165 , pp. 831-836
    • Wirth, R.1    An, F.Y.2    Clewell, D.B.3
  • 52
    • 0003487249 scopus 로고
    • Comparative analysis of cAD1 and cCF10 induced aggregation substances of Enterococcus faecalis
    • (Dunny, G.M., Cleary, P.P. and McKay, L.L., Eds.), American Society for Microbiology, Washington, DC
    • Wirth, R., Olmsted, S.B., Galli, D. and Dunny, G.M. (1991) Comparative analysis of cAD1 and cCF10 induced aggregation substances of Enterococcus faecalis. In: Genetics and Molecular Biology of Streptococci, Lactococci and Enterococci (Dunny, G.M., Cleary, P.P. and McKay, L.L., Eds.), pp. 34-38. American Society for Microbiology, Washington, DC.
    • (1991) In: Genetics and Molecular Biology of Streptococci, Lactococci and Enterococci , pp. 34-38
    • Wirth, R.1    Olmsted, S.B.2    Galli, D.3    Dunny, G.M.4
  • 53
    • 0025876070 scopus 로고
    • Molecular and genetic analysis of a region of plasmid pCF10 containing positive control genes and structural genes encoding surface proteins involved in pheromone-inducible conjugation in Enterococcus faecalis
    • Kao S.M., Olmsted S.B., Viksnins A.S., Gallo J.C., Dunny G.M. Molecular and genetic analysis of a region of plasmid pCF10 containing positive control genes and structural genes encoding surface proteins involved in pheromone-inducible conjugation in Enterococcus faecalis. J. Bacteriol. 197:1991;7650-7664.
    • (1991) J. Bacteriol. , vol.197 , pp. 7650-7664
    • Kao, S.M.1    Olmsted, S.B.2    Viksnins, A.S.3    Gallo, J.C.4    Dunny, G.M.5


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