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Volumn 12, Issue 1, 2013, Pages 336-346

Identification of potential universal vaccine candidates against group a streptococcus by using high throughput in silico and proteomics approach

Author keywords

Bioinformatics; DNA array; Group A Streptococcus; Universal vaccine candidates

Indexed keywords

STREPTOCOCCUS GROUP A VACCINE; STREPTOCOCCUS VACCINE; UNCLASSIFIED DRUG;

EID: 84874049293     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr3005265     Document Type: Article
Times cited : (18)

References (63)
  • 1
    • 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. 2007, 15, 318-325.
    • (2007) Trends Microbiol. , vol.15 , pp. 318-325
    • Tart, A.H.1    Walker, M.J.2    Musser, J.M.3
  • 4
    • 0037150483 scopus 로고    scopus 로고
    • Protection of mice from group A streptococcal infection by intranasal immunisation with a peptide vaccine that contains a conserved M protein B cell epitope and lacks a T cell autoepitope
    • Olive, C.; Clair, T.; Yarwood, P.; Good, M. F. Protection of mice from group A streptococcal infection by intranasal immunisation with a peptide vaccine that contains a conserved M protein B cell epitope and lacks a T cell autoepitope. Vaccine 2002, 20, 2816-2825.
    • (2002) Vaccine , vol.20 , pp. 2816-2825
    • Olive, C.1    Clair, T.2    Yarwood, P.3    Good, M.F.4
  • 6
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham, M. W. Pathogenesis of group A streptococcal infections. Clin. Microbiol. Rev. 2000, 13, 470-511.
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 470-511
    • Cunningham M., .W.1
  • 7
    • 0035925596 scopus 로고    scopus 로고
    • Reverse vaccinology, a genome-based approach to vaccine development
    • Rappuoli, R. Reverse vaccinology, a genome-based approach to vaccine development. Vaccine 2001, 19, 2688-2691.
    • (2001) Vaccine , vol.19 , pp. 2688-2691
    • Rappuoli, R.1
  • 8
    • 0037833535 scopus 로고    scopus 로고
    • Bioinformatics: How it is being used to identify bacterial vaccine candidates
    • Zagursky, R. J.; Olmsted, S. B.; Russell, D. P.; Wooters, J. L. Bioinformatics: how it is being used to identify bacterial vaccine candidates. Expert Rev. Vaccines 2003, 2, 417-436.
    • (2003) Expert Rev. Vaccines , vol.2 , pp. 417-436
    • Zagursky, R.J.1    Olmsted, S.B.2    Russell, D.P.3    Wooters, J.L.4
  • 14
    • 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.; Zhang, S.; Porcella, S. F.; Nagiec, M. J.; Barbian, K. D.; Beres, S. B.; LeFebvre, R. B.; Musser, J. M. Genome sequence of a serotype M28 strain of group a streptococcus: potential new insights into puerperal sepsis and bacterial disease specificity. J. Infect. Dis. 2005, 192, 760-770.
    • (2005) J. Infect. Dis. , vol.192 , pp. 760-770
    • Green, N.M.1    Zhang, S.2    Porcella, S.F.3    Nagiec, M.J.4    Barbian, K.D.5    Beres, S.B.6    Lefebvre, R.B.7    Musser, J.M.8
  • 16
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady, G. E.; Simon, I. The HMMTOP transmembrane topology prediction server. Bioinformatics 2001, 17, 849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 18
    • 33748659861 scopus 로고    scopus 로고
    • Genes for the majority of group a streptococcal virulence factors and extracellular surface proteins do not confer an increased propensity to cause invasive disease
    • McMillan, D. J.; Beiko, R. G.; Geffers, R.; Buer, J.; Schouls, L. M.; Vlaminckx, B. J.; Wannet, W. J.; Sriprakash, K. S.; Chhatwal, G. S. Genes for the majority of group a streptococcal virulence factors and extracellular surface proteins do not confer an increased propensity to cause invasive disease. Clin. Infect. Dis. 2006, 43, 884-891.
    • (2006) Clin. Infect. Dis. , vol.43 , pp. 884-891
    • McMillan, D.J.1    Beiko, R.G.2    Geffers, R.3    Buer, J.4    Schouls, L.M.5    Vlaminckx, B.J.6    Wannet, W.J.7    Sriprakash, K.S.8    Chhatwal, G.S.9
  • 19
    • 33847704984 scopus 로고    scopus 로고
    • Transcriptional and proteomic profiles of group B Streptococcus type v reveal potential adherence proteins associated with high-level invasion
    • Johri, A. K.; Margarit, I.; Broenstrup, M.; Brettoni, C.; Hua, L.; Gygi, S. P.; Telford, J. L.; Grandi, G.; Paoletti, L. C. Transcriptional and proteomic profiles of group B Streptococcus type V reveal potential adherence proteins associated with high-level invasion. Infect. Immun. 2007, 75, 1473-1483.
    • (2007) Infect. Immun. , vol.75 , pp. 1473-1483
    • Johri, A.K.1    Margarit, I.2    Broenstrup, M.3    Brettoni, C.4    Hua, L.5    Gygi, S.P.6    Telford, J.L.7    Grandi, G.8    Paoletti, L.C.9
  • 21
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A.; Wilm, M.; Varm, O.; Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 1996, 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Varm, O.3    Mann, M.4
  • 23
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J.; McCormick, A.; Yates, J. R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 1994, 5, 976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.1    McCormick, A.2    Yates, J.R.3
  • 24
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng, J.; Elias, J. E.; Thoreen, C. C.; Licklider, L. J.; Gygi, S. P. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2003, 2, 43-50.
    • (2003) J. Proteome Res. , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 25
    • 12844278673 scopus 로고    scopus 로고
    • Surface proteins of Streptococcus agalactiae and related proteins in other bacterial pathogens
    • Lindahl, G.; Stalhammar-Carlemalm, M.; Areschoug, T. Surface proteins of Streptococcus agalactiae and related proteins in other bacterial pathogens. Clin. Microbiol. Rev. 2005, 18, 102-127.
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 102-127
    • Lindahl, G.1    Stalhammar-Carlemalm, M.2    Areschoug, T.3
  • 26
    • 0002376433 scopus 로고    scopus 로고
    • Rinciples, methods and applications
    • An, Y. N., Friedman, R. J., Eds.; Human Press: Totowa, NJ
    • Courtney, H. S.; Dale, J. B.; Hasty, D. L. Principles, Methods and Applications. In Handbook of Bacterial Adhesion; An, Y. N., Friedman, R. J., Eds.; Human Press: Totowa, NJ, 2002; pp 553-579.
    • (2002) Handbook of Bacterial Adhesion , pp. 553-579
    • Courtney, H.S.1    Dale, J.B.2    Hasty, D.L.3
  • 27
    • 0036221733 scopus 로고    scopus 로고
    • Outer membrane proteins: Key players for bacterial adaptation in host niches
    • Lin, J.; Huang, S.; Zhang, Q. Outer membrane proteins: key players for bacterial adaptation in host niches. Microbes Infect. 2002, 4, 325-331.
    • (2002) Microbes Infect. , vol.4 , pp. 325-331
    • Lin, J.1    Huang, S.2    Zhang, Q.3
  • 28
    • 1642493657 scopus 로고    scopus 로고
    • Adhesins and invasins of pathogenic bacteria: A structural view
    • Niemann, H. H.; Schubert, W. D.; Heinz, D. W. Adhesins and invasins of pathogenic bacteria: a structural view. Microbes Infect. 2004, 6, 101-112.
    • (2004) Microbes Infect. , vol.6 , pp. 101-112
    • Niemann, H.H.1    Schubert, W.D.2    Heinz, D.W.3
  • 29
    • 8844240627 scopus 로고    scopus 로고
    • Protein sorting to the cell wall envelope of Gram-positive bacteria
    • Ton-That, H.; Marraffini, L. A.; Schneewind, O. Protein sorting to the cell wall envelope of Gram-positive bacteria. Biochim. Biophys. Acta 2004, 1694, 269-278.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 269-278
    • Ton-That, H.1    Marraffini, L.A.2    Schneewind, O.3
  • 30
    • 0035010116 scopus 로고    scopus 로고
    • Improved pattern for genomebased screening identifies novel cell wall-attached proteins in grampositive bacteria
    • Janulczyk, R.; Rasmussen, M. Improved pattern for genomebased screening identifies novel cell wall-attached proteins in grampositive bacteria. Infect. Immun. 2001, 69, 4019-4026.
    • (2001) Infect. Immun. , vol.69 , pp. 4019-4026
    • Janulczyk, R.1    Rasmussen, M.2
  • 34
    • 32044466276 scopus 로고    scopus 로고
    • Characterization of group A streptococci (Streptococcus pyogenes): Correlation of M-protein and emm-gene type with T-protein agglutination pattern and serum opacity factor
    • Johnson, D. R.; Kaplan, E. L.; VanGheem, A.; Facklam, R. R.; Beall, B. Characterization of group A streptococci (Streptococcus pyogenes): correlation of M-protein and emm-gene type with T-protein agglutination pattern and serum opacity factor. J. Med. Microbiol. 2006, 55, 157-164.
    • (2006) J. Med. Microbiol. , vol.55 , pp. 157-164
    • Johnson, D.R.1    Kaplan, E.L.2    Vangheem, A.3    Facklam, R.R.4    Beall, B.5
  • 35
    • 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. 2004, 72, 94-105.
    • (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
  • 36
    • 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. 1998, 273, 14503-14515.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 37
    • 0038501069 scopus 로고    scopus 로고
    • Identification of a novel plasmin(ogen)-binding motif in surface displayed enolase of Streptococcus pneumoniae
    • Bergmann, S.; Wild, D.; Diekmann, O.; Frank, R.; Bracht, D.; Chhatwal, G. S.; Hammerschmidt, S. Identification of a novel plasmin(ogen)-binding motif in surface displayed enolase of Streptococcus pneumoniae. Mol. Microbiol. 2003, 49, 411-423.
    • (2003) Mol. Microbiol. , vol.49 , pp. 411-423
    • Bergmann, S.1    Wild, D.2    Diekmann, O.3    Frank, R.4    Bracht, D.5    Chhatwal, G.S.6    Hammerschmidt, S.7
  • 38
    • 0242321265 scopus 로고    scopus 로고
    • Plasminogen-mediated group A streptococcal adherence to and pericellular invasion of human pharyngeal cells
    • Pancholi, V.; Fontan, P.; Jin, H. Plasminogen-mediated group A streptococcal adherence to and pericellular invasion of human pharyngeal cells. Microb. Pathog. 2003, 35, 293-303.
    • (2003) Microb. Pathog. , vol.35 , pp. 293-303
    • Pancholi, V.1    Fontan, P.2    Jin, H.3
  • 39
    • 0029799009 scopus 로고    scopus 로고
    • The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase
    • Winram, S. B.; Lottenberg, R. The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase. Microbiology 1996, 142, 2311-2320.
    • (1996) Microbiology , vol.142 , pp. 2311-2320
    • Winram, S.B.1    Lottenberg, R.2
  • 40
    • 0030661706 scopus 로고    scopus 로고
    • Regulation of the phosphorylation of human pharyngeal cell proteins by group A streptococcal surface dehydrogenase: Signal transduction between streptococci and pharyngeal cells
    • Pancholi, V.; Fischetti, V. A. Regulation of the phosphorylation of human pharyngeal cell proteins by group A streptococcal surface dehydrogenase: signal transduction between streptococci and pharyngeal cells. J. Exp. Med. 1997, 186, 1633-1643.
    • (1997) J. Exp. Med. , vol.186 , pp. 1633-1643
    • Pancholi, V.1    Fischetti, V.A.2
  • 41
    • 20444425311 scopus 로고    scopus 로고
    • Group A streptococcal surface GAPDH, SDH, recognizes uPAR/CD87 as its receptor on the human pharyngeal cell and mediates bacterial adherence to host cells
    • Jin, H.; Song, Y. P.; Boel, G.; Kochar, G.; Pancholi, V. Group A streptococcal surface GAPDH, SDH, recognizes uPAR/CD87 as its receptor on the human pharyngeal cell and mediates bacterial adherence to host cells. J. Mol. Biol. 2005, 350, 27-41.
    • (2005) J. Mol. Biol. , vol.350 , pp. 27-41
    • Jin, H.1    Song, Y.P.2    Boel, G.3    Kochar, G.4    Pancholi, V.5
  • 42
    • 17644397901 scopus 로고    scopus 로고
    • Surface analyses and immune reactivities of major cell wall-associated proteins of group A Streptococcus
    • Cole, J. N.; Ramirez, R. D.; Currie, B. J.; Cordwell, S. J.; Djordjevic, S. P.; Walker, M. J. Surface analyses and immune reactivities of major cell wall-associated proteins of group A Streptococcus. Infect. Immun. 2005, 73, 3137-3146.
    • (2005) Infect. Immun. , vol.73 , pp. 3137-3146
    • Cole, J.N.1    Ramirez, R.D.2    Currie, B.J.3    Cordwell, S.J.4    Djordjevic, S.P.5    Walker, M.J.6
  • 43
    • 1842431723 scopus 로고    scopus 로고
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins
    • Granato, D.; Bergonzelli, G. E.; Pridmore, R. D.; Marvin, L.; Rouvet, M.; Corthe?sy-Theulaz, I. E. Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins. Infect. Immun. 2004, 72, 2160-2169.
    • (2004) Infect. Immun. , vol.72 , pp. 2160-2169
    • Granato, D.1    Bergonzelli, G.E.2    Pridmore, R.D.3    Marvin, L.4    Rouvet, M.5    Corthesy-Theulaz, I.E.6
  • 44
    • 25444445823 scopus 로고    scopus 로고
    • Identification of immunogenic and serum binding proteins of Staphylococcus epidermidis
    • Sellman, B. R.; Howell, A. P.; Kelly-Boyd, C.; Baker, S. M. Identification of immunogenic and serum binding proteins of Staphylococcus epidermidis. Infect. Immun. 2005, 73, 6591-6600.
    • (2005) Infect. Immun. , vol.73 , pp. 6591-6600
    • Sellman, B.R.1    Howell, A.P.2    Kelly-Boyd, C.3    Baker, S.M.4
  • 45
    • 0036249166 scopus 로고    scopus 로고
    • Identification of vaccine candidate antigens of Staphylococcus aureus by serological proteome analysis
    • Vytvytska, O.; Nagy, E.; Bluggel, M.; Meyer, H. E.; Kurzbauer, R.; Huber, L. A.; Klade, C. S. Identification of vaccine candidate antigens of Staphylococcus aureus by serological proteome analysis. Proteomics 2002, 2, 580-590.
    • (2002) Proteomics , vol.2 , pp. 580-590
    • Vytvytska, O.1    Nagy, E.2    Bluggel, M.3    Meyer, H.E.4    Kurzbauer, R.5    Huber, L.A.6    Klade, C.S.7
  • 46
    • 0141593638 scopus 로고    scopus 로고
    • Effect of acidic pH on expression of surface-associated proteins of Streptococcus oralis
    • Wilkins, J. C.; Beighton, D.; Homer, K. A. Effect of acidic pH on expression of surface-associated proteins of Streptococcus oralis. Appl. Environ. Microbiol. 2003, 69, 5290-5296.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5290-5296
    • Wilkins, J.C.1    Beighton, D.2    Homer, K.A.3
  • 47
    • 0036434714 scopus 로고    scopus 로고
    • Elongation factor Tu and E1 b subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae
    • Dallo, S. F.; Kannan, T. R.; Blaylock, M. W.; Baseman, J. B. Elongation factor Tu and E1 b subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae. Mol. Microbiol. 2002, 46, 1041-1051.
    • (2002) Mol. Microbiol. , vol.46 , pp. 1041-1051
    • Dallo, S.F.1    Kannan, T.R.2    Blaylock, M.W.3    Baseman, J.B.4
  • 48
    • 8144221393 scopus 로고    scopus 로고
    • Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse
    • Ling, E. G.; Feldman, M.; Portnoi, R.; Dagan, K.; Overweg, F.; Mulholland, F.; Chalifa-Caspi, V.; Wells, J.; Mizrachi-Nebenzahl, Y. Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse. Clin. Exp. Immunol. 2004, 138, 290-298.
    • (2004) Clin. Exp. Immunol. , vol.138 , pp. 290-298
    • Ling, E.G.1    Feldman, M.2    Portnoi, R.3    Dagan, K.4    Overweg, F.5    Mulholland, F.6    Chalifa-Caspi, V.7    Wells, J.8    Mizrachi-Nebenzahl, Y.9
  • 49
    • 0036259796 scopus 로고    scopus 로고
    • Proteomic analysis of differentially expressed Chlamydia pneumoniae genes during persistent infection of HEp-2 cells
    • Molestina, R. E.; Klein, J. B.; Miller, R. D.; Pierce, W. H.; Ramirez, J. A.; Summersgill, J. T. Proteomic analysis of differentially expressed Chlamydia pneumoniae genes during persistent infection of HEp-2 cells. Infect. Immun. 2002, 70, 2976-2981.
    • (2002) Infect. Immun. , vol.70 , pp. 2976-2981
    • Molestina, R.E.1    Klein, J.B.2    Miller, R.D.3    Pierce, W.H.4    Ramirez, J.A.5    Summersgill, J.T.6
  • 51
    • 17844401762 scopus 로고    scopus 로고
    • Comparative proteome analysis of secretory proteins from pathogenic and nonpathogenic Listeria species
    • Trost, M.; Wehmhoner, D.; Karst, U.; Dieterich, G.; Wehland, J.; Ja?nsch, L. Comparative proteome analysis of secretory proteins from pathogenic and nonpathogenic Listeria species. Proteomics 2005, 5, 1544-1557.
    • (2005) Proteomics , vol.5 , pp. 1544-1557
    • Trost, M.1    Wehmhoner, D.2    Karst, U.3    Dieterich, G.4    Wehland, J.5    Jansch, L.6
  • 53
    • 0036568587 scopus 로고    scopus 로고
    • Anchorless adhesins and invasins of Grampositive bacteria: A new class of virulence factors
    • Chhatwal, G. S. Anchorless adhesins and invasins of Grampositive bacteria: a new class of virulence factors. Trends Microbiol. 2002, 10, 205-208.
    • (2002) Trends Microbiol. , vol.10 , pp. 205-208
    • Chhatwal G., .S.1
  • 54
    • 38749129192 scopus 로고    scopus 로고
    • SipA is required for pilus formation in Streptococcus pyogenes serotype M3
    • Zahner, D.; Scott, J. R. SipA is required for pilus formation in Streptococcus pyogenes serotype M3. J. Bacteriol. 2008, 190, 527-35.
    • (2008) J. Bacteriol. , vol.190 , pp. 527-535
    • Zahner, D.1    Scott, J.R.2
  • 56
    • 40449109110 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary crystallographic analysis of Streptococcus pyogenes laminin-binding protein Lbp
    • Linke, C.; Caradoc-Davis, T. T.; Proft, T.; Baker, E. N. Purification, crystallization and preliminary crystallographic analysis of Streptococcus pyogenes laminin-binding protein Lbp. Acta. Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 2008, 64, 141-3.
    • (2008) Acta. Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.64 , pp. 141-143
    • Linke, C.1    Caradoc-Davis, T.T.2    Proft, T.3    Baker, E.N.4
  • 57
    • 33744901493 scopus 로고    scopus 로고
    • Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils
    • Terao, Y.; Yamaguchi, M.; Hamada, S.; Kawabata, S. Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils. J. Biol. Chem. 2006, 281, 14215-14223.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14215-14223
    • Terao, Y.1    Yamaguchi, M.2    Hamada, S.3    Kawabata, S.4
  • 58
    • 0029823130 scopus 로고    scopus 로고
    • Internalin A can mediate phagocytosis of Listeria monocytogenes by mouse macrophage cell lines
    • Sawyer, R. T.; Drevets, D. A.; Campbell, P. A.; Potter, T. A. Internalin A can mediate phagocytosis of Listeria monocytogenes by mouse macrophage cell lines. J. Leukocyte Biol. 1996, 60, 603-10.
    • (1996) J. Leukocyte Biol. , vol.60 , pp. 603-610
    • Sawyer, R.T.1    Drevets, D.A.2    Campbell, P.A.3    Potter, T.A.4
  • 59
    • 0031813761 scopus 로고    scopus 로고
    • Cytoplasmic membrane lipoprotein LppC of Streptococcus equisimilis functions as an acid phosphatase
    • Malke, H. Cytoplasmic membrane lipoprotein LppC of Streptococcus equisimilis functions as an acid phosphatase. Appl. Environ. Microbiol. 1998, 64, 2439-2442.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2439-2442
    • Malke, H.1
  • 60
    • 0036322876 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactis
    • Drouault, S.; Anba, J.; Bonneau, S.; Bolotin, A.; Ehrlich, S. D.; Renault, P. The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactis. Appl. Environ. Microbiol. 2002, 68, 3932-3942.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3932-3942
    • Drouault, S.1    Anba, J.2    Bonneau, S.3    Bolotin, A.4    Ehrlich, S.D.5    Renault, P.6
  • 61
    • 33644849516 scopus 로고    scopus 로고
    • The streptococcal lipoprotein rotamase A (SlrA) is a functional peptidyl-prolyl isomerase involved in pneumococcal colonization
    • Hermans, P. W.; Adrian, P. V.; Albert, C.; Estevao, S.; Hoogenboezem, T.; Kamphausen, I. H.; Hammerschmidt, S. The streptococcal lipoprotein rotamase A (SlrA) is a functional peptidyl-prolyl isomerase involved in pneumococcal colonization. J. Biol. Chem. 2006, 281, 968-976.
    • (2006) J. Biol. Chem. , vol.281 , pp. 968-976
    • Hermans, P.W.1    Adrian, P.V.2    Albert, C.3    Estevao, S.4    Hoogenboezem, T.5    Kamphausen, I.H.6    Hammerschmidt, S.7
  • 62
    • 11144342769 scopus 로고    scopus 로고
    • Trigger factor in Streptococcus mutans is involved in stress tolerance, competence development, and biofilm formation
    • Wen, Z. T.; Suntharalingham, P.; Cvitkovitch, D. G.; Burne., R. A. Trigger factor in Streptococcus mutans is involved in stress tolerance, competence development, and biofilm formation. Infect. Immun. 2005, 73, 219-225.
    • (2005) Infect. Immun. , vol.73 , pp. 219-225
    • Wen, Z.T.1    Suntharalingham, P.2    Cvitkovitch, D.G.3    Burne, R.A.4
  • 63
    • 33749575659 scopus 로고    scopus 로고
    • Manganese transport and the role of manganese in virulence
    • Papp-wallace, K. M.; Maguire, M. E. Manganese transport and the role of manganese in virulence. Annu. Rev. Microbiol. 2006, 60, 187-209.
    • (2006) Annu. Rev. Microbiol. , vol.60 , pp. 187-209
    • Papp-Wallace, K.M.1    Maguire, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.