메뉴 건너뛰기




Volumn 7, Issue 6, 1996, Pages 659-666

Gram-positive commensal bacteria for mucosal vaccine delivery

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE PROTEIN; IMMUNOGLOBULIN A ANTIBODY; IMMUNOGLOBULIN G ANTIBODY; RECOMBINANT PROTEIN; VACCINE;

EID: 0030561058     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(96)80079-6     Document Type: Article
Times cited : (51)

References (95)
  • 1
    • 0021165561 scopus 로고
    • Cholera toxin B subunit as a carrier protein to stimulate a mucosal immune response
    • McKenzie SJ, Halsey JF. Cholera toxin B subunit as a carrier protein to stimulate a mucosal immune response. J Immunol. 133:1984;1818-1824.
    • (1984) J Immunol , vol.133 , pp. 1818-1824
    • McKenzie, S.J.1    Halsey, J.F.2
  • 2
    • 0024988012 scopus 로고
    • Synthetic peptide vaccine against mucosal colonization by group A streptococci. I. Protection against a heterologous M serotype with shared C repeat region epitopes
    • Bessen D, Fischetti VA. Synthetic peptide vaccine against mucosal colonization by group A streptococci. I. Protection against a heterologous M serotype with shared C repeat region epitopes. J Immunol. 145:1990;1251-1256.
    • (1990) J Immunol , vol.145 , pp. 1251-1256
    • Bessen, D.1    Fischetti, V.A.2
  • 3
    • 0026654831 scopus 로고
    • Enhanced secretory IgA and systemic IgG antibody responses after oral immunization with biodegradable microparticles containing antigen
    • Challacombe SJ, Rahman D, Jeffery H, Davis SS, O'Hagan DT. Enhanced secretory IgA and systemic IgG antibody responses after oral immunization with biodegradable microparticles containing antigen. Immunology. 76:1992;164-168.
    • (1992) Immunology , vol.76 , pp. 164-168
    • Challacombe, S.J.1    Rahman, D.2    Jeffery, H.3    Davis, S.S.4    O'Hagan, D.T.5
  • 7
    • 0025815449 scopus 로고
    • Vaccinia virus: A tool for research and vaccine development
    • Moss B. Vaccinia virus: a tool for research and vaccine development. Science. 252:1991;1662-1667.
    • (1991) Science , vol.252 , pp. 1662-1667
    • Moss, B.1
  • 10
    • 0011852777 scopus 로고
    • Live recombinant viral vaccines
    • M.H.V. Van Regenmorterl, Neurath A.R. Oxford: Elsevier Science
    • Tartaglia J, Paoletti E. Live recombinant viral vaccines. Van Regenmorterl MHV, Neurath AR. Immunochemistry of Viruses. 2:1990;125-151 Elsevier Science, Oxford.
    • (1990) Immunochemistry of Viruses , vol.2 , pp. 125-151
    • Tartaglia, J.1    Paoletti, E.2
  • 12
    • 0026719273 scopus 로고
    • Expression of recombinant proteins on the surface of the coagulase-negative bacterium Staphylococcus xylosus
    • Hansson M, Stahl S, Nguyen TN, Bachi T, Robert A, Binz H, Sjolander A, Uhlen M. Expression of recombinant proteins on the surface of the coagulase-negative bacterium Staphylococcus xylosus. J Bacteriol. 174:1992;4239-4245.
    • (1992) J Bacteriol , vol.174 , pp. 4239-4245
    • Hansson, M.1    Stahl, S.2    Nguyen, T.N.3    Bachi, T.4    Robert, A.5    Binz, H.6    Sjolander, A.7    Uhlen, M.8
  • 13
    • 0029134979 scopus 로고
    • New and safe 'oral' live vacccines based on Lactobacillus
    • of special interest. Trinitrophenol was covalently linked to the surface of Lactobacillus and used to determine the immune response to this antigen expressed in this context. They found that Lactobacilli can offer carrier function for antigens expressed in this way.
    • Claassen E, Van Winsen R, Posno M, Boersma WJA. New and safe 'oral' live vacccines based on Lactobacillus. of special interest Adv Exp Med Biol. 371:1995;1553-1558 Trinitrophenol was covalently linked to the surface of Lactobacillus and used to determine the immune response to this antigen expressed in this context. They found that Lactobacilli can offer carrier function for antigens expressed in this way.
    • (1995) Adv Exp Med Biol , vol.371 , pp. 1553-1558
    • Claassen, E.1    Van Winsen, R.2    Posno, M.3    Boersma, W.J.A.4
  • 14
    • 0028991689 scopus 로고
    • Lactobacilli: Vehicles for antigen delivery to the female urogenital tract
    • Rush CM, Hafner LM, Timms P. Lactobacilli: vehicles for antigen delivery to the female urogenital tract. Adv Exp Med Biol. 371:1995;1547-1552.
    • (1995) Adv Exp Med Biol , vol.371 , pp. 1547-1552
    • Rush, C.M.1    Hafner, L.M.2    Timms, P.3
  • 15
    • 0025080271 scopus 로고
    • Oral immunization with recombinant Streptococcus lactis carrying the Streptococcus mutans surface protein antigen gene
    • Iwaki M, Okahashi N, Takahashi I, Kanamoto T, Sugita-Konishi Y, Aibara K, Koga T. Oral immunization with recombinant Streptococcus lactis carrying the Streptococcus mutans surface protein antigen gene. Infect Immun. 28:1990;2929-2934.
    • (1990) Infect Immun , vol.28 , pp. 2929-2934
    • Iwaki, M.1    Okahashi, N.2    Takahashi, I.3    Kanamoto, T.4    Sugita-Konishi, Y.5    Aibara, K.6    Koga, T.7
  • 16
    • 0027309534 scopus 로고
    • Lactococcus lactis: High-level expression of tetanus toxin fragment C and protection against lethal challenge
    • Wells JM, Wilson PW, Norton PM, Gasson MJ, LePage RWF. Lactococcus lactis: high-level expression of tetanus toxin fragment C and protection against lethal challenge. Mol Microbiol. 8:1993;1155-1162.
    • (1993) Mol Microbiol , vol.8 , pp. 1155-1162
    • Wells, J.M.1    Wilson, P.W.2    Norton, P.M.3    Gasson, M.J.4    LePage, R.W.F.5
  • 17
    • 0029118119 scopus 로고
    • Mucosal and systemic immune responses to a recombinant protein expressed on the surface of the oral commensal bacterium Streptococcus gordonii after oral colonization
    • of outstanding interest. The induction of a secretory IgA and serum IgG response is described in this article using a recombinant Streptococcus gordonii colonizing the oral cavity of mice.
    • Medaglini D, Pozzi G, King TP, Fischetti VA. Mucosal and systemic immune responses to a recombinant protein expressed on the surface of the oral commensal bacterium Streptococcus gordonii after oral colonization. of outstanding interest Proc Natl Acad Sci USA. 92:1995;6868-6872 The induction of a secretory IgA and serum IgG response is described in this article using a recombinant Streptococcus gordonii colonizing the oral cavity of mice.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6868-6872
    • Medaglini, D.1    Pozzi, G.2    King, T.P.3    Fischetti, V.A.4
  • 19
    • 0027241244 scopus 로고
    • Cell-surface display of heterologous eptiopes on Staphylococcus xylosus as a potential delivery system for oral vaccination
    • Nguyen TN, Hansson M, Stahl S, Bachi T, Robert A, Domzig W, Binz H, Uhlen M. Cell-surface display of heterologous eptiopes on Staphylococcus xylosus as a potential delivery system for oral vaccination. Gene. 128:1993;89-94.
    • (1993) Gene , vol.128 , pp. 89-94
    • Nguyen, T.N.1    Hansson, M.2    Stahl, S.3    Bachi, T.4    Robert, A.5    Domzig, W.6    Binz, H.7    Uhlen, M.8
  • 20
    • 0026719273 scopus 로고
    • Expression of recombinant proteins on the surface of the coagulase-negative bacterium Staphylococcus xylosus
    • Hansson M, Nguyen TN, Bachi T, Robert A, Binz H, Sjolander A, Uhlen M, Stahl S. Expression of recombinant proteins on the surface of the coagulase-negative bacterium Staphylococcus xylosus. J Bacteriol. 174:1992;4239-4245.
    • (1992) J Bacteriol , vol.174 , pp. 4239-4245
    • Hansson, M.1    Nguyen, T.N.2    Bachi, T.3    Robert, A.4    Binz, H.5    Sjolander, A.6    Uhlen, M.7    Stahl, S.8
  • 21
    • 0028953525 scopus 로고
    • Cell surface display of recombinant proteins on Staphylococcus carnosus
    • of special interest. Staphylococci are used in this paper to express an 80 amino acid peptide from the blood-stage antigen of Plasmodium falciparum. The gene for the antigen is expressed from a plasmid. This paper describes the use of fluorescence-activated cell sorting to select for the bacteria expressing the antigen on its surface.
    • Samuelson P, Hansson M, Ahlborg N, Andreoni C, Gotz F, Bachi T, Nguyen TN, Binz H, Uhlen M, Stahl S. Cell surface display of recombinant proteins on Staphylococcus carnosus. of special interest J Bacteriol. 177:1995;1470-1476 Staphylococci are used in this paper to express an 80 amino acid peptide from the blood-stage antigen of Plasmodium falciparum. The gene for the antigen is expressed from a plasmid. This paper describes the use of fluorescence-activated cell sorting to select for the bacteria expressing the antigen on its surface.
    • (1995) J Bacteriol , vol.177 , pp. 1470-1476
    • Samuelson, P.1    Hansson, M.2    Ahlborg, N.3    Andreoni, C.4    Gotz, F.5    Bachi, T.6    Nguyen, T.N.7    Binz, H.8    Uhlen, M.9    Stahl, S.10
  • 22
    • 0029924013 scopus 로고    scopus 로고
    • Suface display of a functional single-chain Fv antibody to staphylococci
    • Gunneriusson E, Samuelson P, Uhlen M, Nygren P, Stahl S. Suface display of a functional single-chain Fv antibody to staphylococci. J Bacteriol. 178:1996;1341-1346.
    • (1996) J Bacteriol , vol.178 , pp. 1341-1346
    • Gunneriusson, E.1    Samuelson, P.2    Uhlen, M.3    Nygren, P.4    Stahl, S.5
  • 23
    • 0025077034 scopus 로고
    • Conservation of a hexapeptide sequence in the anchor region of surface proteins of Gram-positive cocci
    • Fischetti VA, Pancholi V, Schneewind O. Conservation of a hexapeptide sequence in the anchor region of surface proteins of Gram-positive cocci. Mol Microbiol. 4:1990;1603-1605.
    • (1990) Mol Microbiol , vol.4 , pp. 1603-1605
    • Fischetti, V.A.1    Pancholi, V.2    Schneewind, O.3
  • 24
    • 0026638608 scopus 로고
    • Sorting of protein A to the staphylococcal cell wall
    • Schneewind O, Model P, Fischetti VA. Sorting of protein A to the staphylococcal cell wall. Cell. 70:1992;267-281.
    • (1992) Cell , vol.70 , pp. 267-281
    • Schneewind, O.1    Model, P.2    Fischetti, V.A.3
  • 25
    • 0003068582 scopus 로고
    • Common characteristics of the surface proteins from Gram-positive cocci
    • G.M. Dunney, P.P. Clearly, McKay L.L. Washington, DC: American Society for Microbiology
    • Fischetti VA, Pancholi V, Schneewind O. Common characteristics of the surface proteins from Gram-positive cocci. Dunney GM, Clearly PP, McKay LL. Genetics and Molecular Biology for Streptococci, Lactococci, and Enterococci. 1991;290-294 American Society for Microbiology, Washington, DC.
    • (1991) Genetics and Molecular Biology for Streptococci, Lactococci, and Enterococci , pp. 290-294
    • Fischetti, V.A.1    Pancholi, V.2    Schneewind, O.3
  • 26
    • 0023897280 scopus 로고
    • Isolation and characterization of the cell-associated region of group A streptococcal M6 protein
    • Pancholi V, Fischetti VA. Isolation and characterization of the cell-associated region of group A streptococcal M6 protein. J Bacteriol. 170:1988;2618-2624.
    • (1988) J Bacteriol , vol.170 , pp. 2618-2624
    • Pancholi, V.1    Fischetti, V.A.2
  • 27
    • 0028987131 scopus 로고
    • Lipoproteins of Gram-positive bacteria
    • Sutcliffe IC, Russell RRB. Lipoproteins of Gram-positive bacteria. J Bacteriol. 177:1995;1123-1128.
    • (1995) J Bacteriol , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.B.2
  • 28
    • 0026501145 scopus 로고
    • Structural properties and evolutionary relationships of PspA, a surface protein of Streptococcus pneumoniae, as revealed by sequence analysis
    • Yother J, Briles DE. Structural properties and evolutionary relationships of PspA, a surface protein of Streptococcus pneumoniae, as revealed by sequence analysis. J Bacteriol. 174:1992;601-609.
    • (1992) J Bacteriol , vol.174 , pp. 601-609
    • Yother, J.1    Briles, D.E.2
  • 29
    • 0011853849 scopus 로고
    • Streptococcal M protein: A common structural motif used by Gram-positive bacteria for biologically active surface molecules
    • T.K. Korhonen, T. Hovi, Makela P.H. New York: Plenum Press
    • Fischetti VA, Pancholi V, Sellers P, Schmidt J, Landau G, Xu X, Schneewind O. Streptococcal M protein: a common structural motif used by Gram-positive bacteria for biologically active surface molecules. Korhonen TK, Hovi T, Makela PH. Molecular Recognition in Host-Parasite Interactions. 1992;31-38 Plenum Press, New York.
    • (1992) Molecular Recognition in Host-Parasite Interactions , pp. 31-38
    • Fischetti, V.A.1    Pancholi, V.2    Sellers, P.3    Schmidt, J.4    Landau, G.5    Xu, X.6    Schneewind, O.7
  • 30
  • 31
    • 0018173811 scopus 로고
    • Crystallization, crystal structure analysis and atomic model of the complex formed by a human Fc fragment and fragment B of protein A from Staphylococcus aureus
    • Deisenhofer J, Jones TA, Huber R, Sjodahl J, Sjoquist J. Crystallization, crystal structure analysis and atomic model of the complex formed by a human Fc fragment and fragment B of protein A from Staphylococcus aureus. Hoppe-Seyler's Z Physiol Chem. 359:1978;975-985.
    • (1978) Hoppe-Seyler's Z Physiol Chem , vol.359 , pp. 975-985
    • Deisenhofer, J.1    Jones, T.A.2    Huber, R.3    Sjodahl, J.4    Sjoquist, J.5
  • 32
    • 0026801084 scopus 로고
    • Three-dimensional solution structure of the B domain of staphylococcal protein A: Comparisons of the solution and crystal structures
    • Gouda H, Torigoe H, Saito A, Sato M, Arata Y, Shimada I. Three-dimensional solution structure of the B domain of staphylococcal protein A: comparisons of the solution and crystal structures. Biochemistry. 31:1992;9665-9672.
    • (1992) Biochemistry , vol.31 , pp. 9665-9672
    • Gouda, H.1    Torigoe, H.2    Saito, A.3    Sato, M.4    Arata, Y.5    Shimada, I.6
  • 37
    • 0027442464 scopus 로고
    • Cell wall sorting signals in surface proteins of Gram-positive bacteria
    • Schneewind O, Mihaylova-Petkov D, Model P. Cell wall sorting signals in surface proteins of Gram-positive bacteria. EMBO J. 12:1993;4803-4811.
    • (1993) EMBO J , vol.12 , pp. 4803-4811
    • Schneewind, O.1    Mihaylova-Petkov, D.2    Model, P.3
  • 38
    • 0024412074 scopus 로고
    • Streptococcal M protein: Molecular design and biological behavior
    • Fischetti VA. Streptococcal M protein: molecular design and biological behavior. Clin Microbiol Rev. 2:1989;285-314.
    • (1989) Clin Microbiol Rev , vol.2 , pp. 285-314
    • Fischetti, V.A.1
  • 39
    • 0000099160 scopus 로고
    • Cell wall replication in Streptococcus pyogenes
    • Cole RM, Hahn JJ. Cell wall replication in Streptococcus pyogenes. Science. 135:1962;722-724.
    • (1962) Science , vol.135 , pp. 722-724
    • Cole, R.M.1    Hahn, J.J.2
  • 40
    • 0026717035 scopus 로고
    • Expression of M6 protein gene of Streptococcus pyrogenes in Streptococcus gordonii after chromosomal integration and transcriptional fusion
    • Pozzi G, Oggioni MR, Manganelli R, Fischetti VA. Expression of M6 protein gene of Streptococcus pyrogenes in Streptococcus gordonii after chromosomal integration and transcriptional fusion. Res Microbiol. 143:1992;449-457.
    • (1992) Res Microbiol , vol.143 , pp. 449-457
    • Pozzi, G.1    Oggioni, M.R.2    Manganelli, R.3    Fischetti, V.A.4
  • 43
    • 0025829598 scopus 로고
    • The naive repertoire of human T helper cells specific for gp120. The envelope of glycoprotein of HIV
    • Manca F, Habeshaw J, Dalgleish A. The naive repertoire of human T helper cells specific for gp120. The envelope of glycoprotein of HIV. J Immunol. 146:1991;1964-1971.
    • (1991) J Immunol , vol.146 , pp. 1964-1971
    • Manca, F.1    Habeshaw, J.2    Dalgleish, A.3
  • 44
    • 0023263155 scopus 로고
    • Immunochemical observations of antigen 5, a major venom allergen of hornets, yellowjackets and wasps
    • King TP, Kochoumian L, Lam T. Immunochemical observations of antigen 5, a major venom allergen of hornets, yellowjackets and wasps. Mol Immunol. 24:1987;857-864.
    • (1987) Mol Immunol , vol.24 , pp. 857-864
    • King, T.P.1    Kochoumian, L.2    Lam, T.3
  • 45
    • 0022583942 scopus 로고
    • Persistence and spread of the orally-implanted bacterium Streptococcus sanguis between persons
    • Svanberg M, Westergren G. Persistence and spread of the orally-implanted bacterium Streptococcus sanguis between persons. Arch Oral Biol. 31:1986;1-4.
    • (1986) Arch Oral Biol , vol.31 , pp. 1-4
    • Svanberg, M.1    Westergren, G.2
  • 46
    • 0023008552 scopus 로고
    • Complete nucleotide sequence of type 6 M protein of the group A streptococcus: Repetitive structure and membrane anchor
    • Hollingshead SK, Fischetti VA, Scott JR. Complete nucleotide sequence of type 6 M protein of the group A streptococcus: repetitive structure and membrane anchor. J Biol Chem. 261:1986;1677-1686.
    • (1986) J Biol Chem , vol.261 , pp. 1677-1686
    • Hollingshead, S.K.1    Fischetti, V.A.2    Scott, J.R.3
  • 47
    • 0023930662 scopus 로고
    • Antigenic variation among group A streptococcal M proteins: Nucleotide sequence of the serotype 5 M protein gene and its relationship with genes encoding types 6 and 24 M proteins
    • Miller L, Gray L, Beachey EH, Kehoe MA. Antigenic variation among group A streptococcal M proteins: nucleotide sequence of the serotype 5 M protein gene and its relationship with genes encoding types 6 and 24 M proteins. J Biol Chem. 263:1988;5668-5673.
    • (1988) J Biol Chem , vol.263 , pp. 5668-5673
    • Miller, L.1    Gray, L.2    Beachey, E.H.3    Kehoe, M.A.4
  • 49
    • 0023958744 scopus 로고
    • Molecular evolution of streptococcal M protein: Cloning and nucleotide sequence of type 2 M protein gene and relation to other genes of Streptococcus pyogenes
    • Mouw AR, Beachey EH, Burdett V. Molecular evolution of streptococcal M protein: cloning and nucleotide sequence of type 2 M protein gene and relation to other genes of Streptococcus pyogenes. J Bacteriol. 170:1988;676-684.
    • (1988) J Bacteriol , vol.170 , pp. 676-684
    • Mouw, A.R.1    Beachey, E.H.2    Burdett, V.3
  • 50
    • 0024408743 scopus 로고
    • Identification of a divergent M protein gene and an M protein related gene family in serotype 49 Streptococcus pyogenes
    • Haanes EJ, Cleary PP. Identification of a divergent M protein gene and an M protein related gene family in serotype 49 Streptococcus pyogenes. J Bacteriol. 171:1989;6397-6408.
    • (1989) J Bacteriol , vol.171 , pp. 6397-6408
    • Haanes, E.J.1    Cleary, P.P.2
  • 51
    • 0025785594 scopus 로고
    • Heptad motifs within the distal subdomain of the coiled-coil rod region of M protein from rheumatic fever and nephritis associated serotypes of group A streptococci are distinct from each other: Nucleotide sequence of the M57 gene and relation of the deduced amino acid sequence of other M proteins
    • Manjula BN, Khandke KM, Fairwell T, Relf WA, Sripakash KS. Heptad motifs within the distal subdomain of the coiled-coil rod region of M protein from rheumatic fever and nephritis associated serotypes of group A streptococci are distinct from each other: nucleotide sequence of the M57 gene and relation of the deduced amino acid sequence of other M proteins. J Protein Chem. 10:1991;369-383.
    • (1991) J Protein Chem , vol.10 , pp. 369-383
    • Manjula, B.N.1    Khandke, K.M.2    Fairwell, T.3    Relf, W.A.4    Sripakash, K.S.5
  • 52
    • 0026595486 scopus 로고
    • Nucleotide sequences of two adjacent M and M-like protein genes of group A streptococci: Different RNA transcript levels and identification of a unique IgA-binding protein
    • Bessen DE, Fischetti VA. Nucleotide sequences of two adjacent M and M-like protein genes of group A streptococci: different RNA transcript levels and identification of a unique IgA-binding protein. Infect Immun. 60:1992;124-135.
    • (1992) Infect Immun , vol.60 , pp. 124-135
    • Bessen, D.E.1    Fischetti, V.A.2
  • 53
    • 0028434945 scopus 로고
    • Cloning and nucleotide sequence of type 3 M protein gene (emm3) consisting on an N-terminal variable portion and C-terminal conserved C repeat regions: Relation to other genes of Streptococcus pyogenes
    • Katsukawa C. Cloning and nucleotide sequence of type 3 M protein gene (emm3) consisting on an N-terminal variable portion and C-terminal conserved C repeat regions: relation to other genes of Streptococcus pyogenes. J Jpn Assoc Infect Dis. 68:1994;698-705.
    • (1994) J Jpn Assoc Infect Dis , vol.68 , pp. 698-705
    • Katsukawa, C.1
  • 54
    • 0024339939 scopus 로고
    • Extensive sequence homology between IgA receptor and M protein in Streptococcus pyogenes
    • Frithz E, Heden L, Lindahl G. Extensive sequence homology between IgA receptor and M protein in Streptococcus pyogenes. Mol Microbiol. 3:1989;1111-1119.
    • (1989) Mol Microbiol , vol.3 , pp. 1111-1119
    • Frithz, E.1    Heden, L.2    Lindahl, G.3
  • 56
    • 0008005003 scopus 로고
    • Fc-receptor and M protein genes of group A streptococci are products of gene duplication
    • Heath DG, Cleary PP. Fc-receptor and M protein genes of group A streptococci are products of gene duplication. Proc Natl Acad Sci USA. 86:1989;4741-4745.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4741-4745
    • Heath, D.G.1    Cleary, P.P.2
  • 58
    • 0025248124 scopus 로고
    • Complete nucleotide sequence of the streptococcal C5a peptidase gene of Streptococcus pyogenes
    • Chen CC, Cleary PP. Complete nucleotide sequence of the streptococcal C5a peptidase gene of Streptococcus pyogenes. J Biol Chem. 265:1990;3161-3167.
    • (1990) J Biol Chem , vol.265 , pp. 3161-3167
    • Chen, C.C.1    Cleary, P.P.2
  • 59
    • 0025346175 scopus 로고
    • Sequence and structural characterization of the trypsin-resistant T6 surface protein of group A streptococci
    • Schneewind O, Jones KF, Fischetti VA. Sequence and structural characterization of the trypsin-resistant T6 surface protein of group A streptococci. J Bacteriol. 172:1990;3310-3317.
    • (1990) J Bacteriol , vol.172 , pp. 3310-3317
    • Schneewind, O.1    Jones, K.F.2    Fischetti, V.A.3
  • 60
    • 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. 63:1995;622-631.
    • (1995) Infect Immun , vol.63 , pp. 622-631
    • Rakonjac, J.V.1    Robbins, J.C.2    Fischetti, V.A.3
  • 61
    • 0026706763 scopus 로고
    • Fibrorectin-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, Timmis KN, Chhatwal GS. Fibrorectin-binding protein of Streptococcus pyogenes: sequence of the binding domain involved in adherence of streptococci to epithelial cells. Infect Immun. 60:1992;3837-3844.
    • (1992) Infect Immun , vol.60 , pp. 3837-3844
    • Talay, S.R.1    Valentin-Weigand, P.2    Jerlstrom, P.G.3    Timmis, K.N.4    Chhatwal, G.S.5
  • 62
    • 0028018488 scopus 로고
    • Domain structure and conserved epitopes of Sfb protein, the fibronectin binding adhesion of Streptococcus pyogenes
    • Talay SR, Valentin-Weigand P, Timmis KN, Chhatwal GS. Domain structure and conserved epitopes of Sfb protein, the fibronectin binding adhesion of Streptococcus pyogenes. Mol Microbiol. 13:1994;531-539.
    • (1994) Mol Microbiol , vol.13 , pp. 531-539
    • Talay, S.R.1    Valentin-Weigand, P.2    Timmis, K.N.3    Chhatwal, G.S.4
  • 63
    • 0027763194 scopus 로고
    • Protein F: An adhesin of Streptococcus pyogenes binds fibronectin via two distinct domains
    • Sela S, Aviv A, Tovi A, Burstein I, Caparon MG, Hanski E. Protein F: an adhesin of Streptococcus pyogenes binds fibronectin via two distinct domains. Mol Microbiol. 10:1993;1049-1055.
    • (1993) Mol Microbiol , vol.10 , pp. 1049-1055
    • Sela, S.1    Aviv, A.2    Tovi, A.3    Burstein, I.4    Caparon, M.G.5    Hanski, E.6
  • 64
    • 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. 268:1993;25417-25424.
    • (1993) J Biol Chem , vol.268 , pp. 25417-25424
    • Berge, A.1    Sjobring, U.2
  • 65
    • 0026680289 scopus 로고
    • Structure of peptostreptococcal protein L and identification of a repeated immunoglobulin light chain-binding domain
    • Kastern W, Sjobring U, Bjorck L. Structure of peptostreptococcal protein L and identification of a repeated immunoglobulin light chain-binding domain. J Biol Chem. 267:1992;12820-12825.
    • (1992) J Biol Chem , vol.267 , pp. 12820-12825
    • Kastern, W.1    Sjobring, U.2    Bjorck, L.3
  • 66
    • 0028341151 scopus 로고
    • Protein PAB, a mosaic albumin-binding bacterial protein representing the first contemporary example of module shuffling
    • De Chateau M, Bjorck L. Protein PAB, a mosaic albumin-binding bacterial protein representing the first contemporary example of module shuffling. J Biol Chem. 269:1994;12147-12151.
    • (1994) J Biol Chem , vol.269 , pp. 12147-12151
    • De Chateau, M.1    Bjorck, L.2
  • 67
    • 0025908172 scopus 로고
    • Molecular characterization of an IgA receptor from Group B streptococci: Sequence of the gene, identification of a proline-rich region with unique structure and isolation of N-terminal fragments with IgA-binding capacity
    • Heden L, Frithz E, Lindahl G. Molecular characterization of an IgA receptor from Group B streptococci: sequence of the gene, identification of a proline-rich region with unique structure and isolation of N-terminal fragments with IgA-binding capacity. Eur J Immunol. 21:1991;1481-1490.
    • (1991) Eur J Immunol , vol.21 , pp. 1481-1490
    • Heden, L.1    Frithz, E.2    Lindahl, G.3
  • 68
    • 0026483706 scopus 로고
    • Large, identical, tandem repeating units in the C protein alpha antigen gene, bca, of group B streptococci
    • Michel JL, Madoff LC, Olson K, King DE, Kasper DL, Ausubel FM. Large, identical, tandem repeating units in the C protein alpha antigen gene, bca, of group B streptococci. Proc Natl Acad Sci USA. 89:1992;10060-10064.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10060-10064
    • Michel, J.L.1    Madoff, L.C.2    Olson, K.3    King, D.E.4    Kasper, D.L.5    Ausubel, F.M.6
  • 69
    • 0027280396 scopus 로고
    • Two different genes coding for fibronectin binding proteins from Streptococcus dysgalactiae. The complete nucleotide sequences and characterization of the binding domain
    • Lindgren P, McGavin MJ, Signas C, Guss B, Gurusiddappa S, Hook M, Lindberg M. Two different genes coding for fibronectin binding proteins from Streptococcus dysgalactiae. The complete nucleotide sequences and characterization of the binding domain. Eur J Biochem. 214:1993;819-827.
    • (1993) Eur J Biochem , vol.214 , pp. 819-827
    • Lindgren, P.1    McGavin, M.J.2    Signas, C.3    Guss, B.4    Gurusiddappa, S.5    Hook, M.6    Lindberg, M.7
  • 71
    • 0026658626 scopus 로고
    • Group G streptococcal M protein exhibits structural features analogous to those of class I M protein of group A streptococci
    • Collins CM, Kimura A, Bisno AL. Group G streptococcal M protein exhibits structural features analogous to those of class I M protein of group A streptococci. Infect Immun. 60:1992;3689-3696.
    • (1992) Infect Immun , vol.60 , pp. 3689-3696
    • Collins, C.M.1    Kimura, A.2    Bisno, A.L.3
  • 72
    • 0026661064 scopus 로고
    • Isolation and molecular characterization of a novel albumin-binding protein from group G streptococci
    • Sjobring U. Isolation and molecular characterization of a novel albumin-binding protein from group G streptococci. Infect Immun. 60:1992;3601-3608.
    • (1992) Infect Immun , vol.60 , pp. 3601-3608
    • Sjobring, U.1
  • 73
    • 0026725379 scopus 로고
    • Cloning and nucleotide sequence of the gene encoding the 136-kilodalton surface protein (muramidase-released protein) of Streptococcus suis type 2
    • Smith HE, Vecht U, Gielkens ALJ, Smits MA. Cloning and nucleotide sequence of the gene encoding the 136-kilodalton surface protein (muramidase-released protein) of Streptococcus suis type 2. Infect Immun. 60:1992;2361-2367.
    • (1992) Infect Immun , vol.60 , pp. 2361-2367
    • Smith, H.E.1    Vecht, U.2    Gielkens, A.L.J.3    Smits, M.A.4
  • 74
    • 0024660048 scopus 로고
    • Molecular characterization of a surface protein antigen gene from serotype c Streptococcus mutans implicated in dental caries
    • Okahashi N, Sasakawa C, Yoshikawa S, Hamada S, Koga T. Molecular characterization of a surface protein antigen gene from serotype c Streptococcus mutans implicated in dental caries. Mol Microbiol. 3:1989;673-678.
    • (1989) Mol Microbiol , vol.3 , pp. 673-678
    • Okahashi, N.1    Sasakawa, C.2    Yoshikawa, S.3    Hamada, S.4    Koga, T.5
  • 76
    • 0025874078 scopus 로고
    • Complete nucleotide sequence of the gene for a surface protein antigen of Streptococcus sobrinus
    • Tokuda M, Okahashi N, Takahashi I, Nakai M, Nagaoka S, Kawagoe M, Koga T. Complete nucleotide sequence of the gene for a surface protein antigen of Streptococcus sobrinus. Infect Immun. 59:1991;3309-3312.
    • (1991) Infect Immun , vol.59 , pp. 3309-3312
    • Tokuda, M.1    Okahashi, N.2    Takahashi, I.3    Nakai, M.4    Nagaoka, S.5    Kawagoe, M.6    Koga, T.7
  • 77
    • 0024448172 scopus 로고
    • Sequence analysis of the wall-associated protein precursor of Streptococcus mutans antigen A
    • Ferretti JJ, Russell RRB, Dao ML. Sequence analysis of the wall-associated protein precursor of Streptococcus mutans antigen A. Mol Microbiol. 3:1989;469-478.
    • (1989) Mol Microbiol , vol.3 , pp. 469-478
    • Ferretti, J.J.1    Russell, R.R.B.2    Dao, M.L.3
  • 78
    • 0026439820 scopus 로고
    • Characterization of the Streptococcus mutants GS-5 fruA gene encoding Exo-β-D-fructosidase
    • Burne RA, Penders JEC. Characterization of the Streptococcus mutants GS-5 fruA gene encoding Exo-β-D-fructosidase. Infect Immun. 60:1993;4621-4632.
    • (1993) Infect Immun , vol.60 , pp. 4621-4632
    • Burne, R.A.1    Penders, J.E.C.2
  • 79
    • 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, Olmsted SB, Viksnins AS, Gallo JC, Dunny GM. 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. 173:1991;7650-7664.
    • (1991) J Bacteriol , vol.173 , pp. 7650-7664
    • Kao, S.1    Olmsted, S.B.2    Viksnins, A.S.3    Gallo, J.C.4    Dunny, G.M.5
  • 80
    • 0025280384 scopus 로고
    • Sequence analysis of Enterococcus faecalis aggregation substance encoded by the sex pheromone plasmid pAD1
    • Galli D, Lottspeich F, Wirth R. Sequence analysis of Enterococcus faecalis aggregation substance encoded by the sex pheromone plasmid pAD1. Mol Microbiol. 4:1990;895-904.
    • (1990) Mol Microbiol , vol.4 , pp. 895-904
    • Galli, D.1    Lottspeich, F.2    Wirth, R.3
  • 82
    • 0000535851 scopus 로고
    • Nucleotide sequence of the gene for fibronectin-binding protein from Staphylococcus aureus: Use of this peptide sequence in the synthesis of biologically active peptides
    • Signas C, Raucci G, Jonsson K, Lindgren P, Anantharamaiah GM, Hook M, Lindberg M. Nucleotide sequence of the gene for fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides. Proc Natl Acad Sci USA. 86:1989;699-703.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 699-703
    • Signas, C.1    Raucci, G.2    Jonsson, K.3    Lindgren, P.4    Anantharamaiah, G.M.5    Hook, M.6    Lindberg, M.7
  • 83
    • 0026334144 scopus 로고
    • Two different genes encode fibronectin binding proteins in Staphylococcus aureus
    • Jonsson K, Signas C, Muller H, Lindberg M. Two different genes encode fibronectin binding proteins in Staphylococcus aureus. Eur J Biochem. 202:1991;1041-1048.
    • (1991) Eur J Biochem , vol.202 , pp. 1041-1048
    • Jonsson, K.1    Signas, C.2    Muller, H.3    Lindberg, M.4
  • 84
    • 0026738861 scopus 로고
    • Molecular characterizations and expression of a gene encoding a Staphylococcus aureus collagen adhesin
    • Patti JM, Jonsson H, Guss B, Switalski LM, Wiberg K, Lindberg M, Hook M. Molecular characterizations and expression of a gene encoding a Staphylococcus aureus collagen adhesin. J Biol Chem. 267:1992;4766-4772.
    • (1992) J Biol Chem , vol.267 , pp. 4766-4772
    • Patti, J.M.1    Jonsson, H.2    Guss, B.3    Switalski, L.M.4    Wiberg, K.5    Lindberg, M.6    Hook, M.7
  • 85
    • 0028334112 scopus 로고
    • Molecular characterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus
    • McDevitt D, Francois P, Vaudaux P, Foster TJ. Molecular characterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus. Mol Microbiol. 11:1994;237-248.
    • (1994) Mol Microbiol , vol.11 , pp. 237-248
    • McDevitt, D.1    Francois, P.2    Vaudaux, P.3    Foster, T.J.4
  • 86
  • 87
    • 0026784132 scopus 로고
    • Cloning, sequencing and expression of the gene encoding the cell-envelope-associated proteinase from Lactobaccillus paracasei subsp. paracasei NCDO 151
    • Holck A, Naes H. Cloning, sequencing and expression of the gene encoding the cell-envelope-associated proteinase from Lactobaccillus paracasei subsp. paracasei NCDO 151. J Gen Microbiol. 138:1992;1353-1364.
    • (1992) J Gen Microbiol , vol.138 , pp. 1353-1364
    • Holck, A.1    Naes, H.2
  • 89
    • 0025739814 scopus 로고
    • Entry of L. monocytogenes into cells is mediated by a repeat protein analogous to surface antigens from Gram-positive, extracellular pathogens
    • Gaillard JL, Berche P, Frehel C, Gouin E, Cossart P. Entry of L. monocytogenes into cells is mediated by a repeat protein analogous to surface antigens from Gram-positive, extracellular pathogens. Cell. 65:1991;1127-1141.
    • (1991) Cell , vol.65 , pp. 1127-1141
    • Gaillard, J.L.1    Berche, P.2    Frehel, C.3    Gouin, E.4    Cossart, P.5
  • 90
    • 0025272711 scopus 로고
    • Sequence homology between the subunits of two immunologically and functionally distinct types of fimbriae of Actinomyces spp
    • Yeung MK, Cisar JO. Sequence homology between the subunits of two immunologically and functionally distinct types of fimbriae of Actinomyces spp. J Bacteriol. 172:1990;2462-2468.
    • (1990) J Bacteriol , vol.172 , pp. 2462-2468
    • Yeung, M.K.1    Cisar, J.O.2
  • 91
    • 0023684707 scopus 로고
    • Cloning and nucleotide sequence of a gene for Actinomyces naeslundii 45 type 2 fimbriae
    • Yeung MK, Cisar JO. Cloning and nucleotide sequence of a gene for Actinomyces naeslundii 45 type 2 fimbriae. J Bacteriol. 170:1988;3803-3809.
    • (1988) J Bacteriol , vol.170 , pp. 3803-3809
    • Yeung, M.K.1    Cisar, J.O.2
  • 92
    • 0028069664 scopus 로고
    • Cloning and nucleotide sequence of the Streptococcus pneumoniae hyaluronidase gene and purification of the enzyme from recombinant Escherichia coli
    • Berry AM, Lock RA, Thomas SM, Rajan DP, Hansman D, Paton JC. Cloning and nucleotide sequence of the Streptococcus pneumoniae hyaluronidase gene and purification of the enzyme from recombinant Escherichia coli. Infect Immun. 62:1994;1101-1108.
    • (1994) Infect Immun , vol.62 , pp. 1101-1108
    • Berry, A.M.1    Lock, R.A.2    Thomas, S.M.3    Rajan, D.P.4    Hansman, D.5    Paton, J.C.6
  • 93
    • 0027999183 scopus 로고
    • A neuraminidase from Streptococcus pneumoniae has the features of a surface protein
    • Camara M, Boulnois GJ, Andrew PW, Mitchell TJ. A neuraminidase from Streptococcus pneumoniae has the features of a surface protein. Infect Immun. 62:1994;3688-3695.
    • (1994) Infect Immun , vol.62 , pp. 3688-3695
    • Camara, M.1    Boulnois, G.J.2    Andrew, P.W.3    Mitchell, T.J.4
  • 94
    • 0018410511 scopus 로고
    • Uptake of circular deoxyribonucleic acid and mechanism of deoxyribonucleic acid transport in genetic transformation of Streptococcus pneumoniae
    • Lacks S. Uptake of circular deoxyribonucleic acid and mechanism of deoxyribonucleic acid transport in genetic transformation of Streptococcus pneumoniae. J Bacterial. 138:1979;404-409.
    • (1979) J Bacterial , vol.138 , pp. 404-409
    • Lacks, S.1
  • 95
    • 0019464012 scopus 로고
    • Pathway of plasmid transformation in pneumococcus: Open circular molecules and linear molecules are active
    • Saunders CW, Guild WR. Pathway of plasmid transformation in pneumococcus: open circular molecules and linear molecules are active. J Bacteriol. 146:1981;517-526.
    • (1981) J Bacteriol , vol.146 , pp. 517-526
    • Saunders, C.W.1    Guild, W.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.