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Volumn 13, Issue 2, 2014, Pages 650-667

Influence of impaired lipoprotein biogenesis on surface and exoproteome of streptococcus pneumoniae

Author keywords

biotinylation approach; exoproteome; lipoprotein distribution; lipoprotein maturation mutations; lipoprotein processing; S. pneumoniae; shaving with trypsin beads; surface proteome

Indexed keywords

BACTERIAL PROTEINS; BASE SEQUENCE; BIOTIN; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; LIPOPROTEINS; POLYMERASE CHAIN REACTION; PROTEOME; STREPTOCOCCUS PNEUMONIAE; SUBCELLULAR FRACTIONS; TRYPSIN;

EID: 84893837078     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr400768v     Document Type: Article
Times cited : (41)

References (97)
  • 1
    • 0036009312 scopus 로고    scopus 로고
    • Pneumococcal disease in western Europe: Burden of disease, antibiotic resistance and management
    • Cartwright, K. Pneumococcal disease in western Europe: burden of disease, antibiotic resistance and management Eur. J. Pediatr. 2002, 161 (4) 188-95
    • (2002) Eur. J. Pediatr. , vol.161 , Issue.4 , pp. 188-195
    • Cartwright, K.1
  • 2
    • 32244439999 scopus 로고    scopus 로고
    • Versatility of pneumococcal surface proteins
    • Bergmann, S.; Hammerschmidt, S. Versatility of pneumococcal surface proteins Microbiology 2006, 152 (Pt 2) 295-303
    • (2006) Microbiology , vol.152 , Issue.PART 2 , pp. 295-303
    • Bergmann, S.1    Hammerschmidt, S.2
  • 3
    • 77952903334 scopus 로고    scopus 로고
    • Streptococcus pneumoniae: Virulence factors and variation
    • Mitchell, A. M.; Mitchell, T. J. Streptococcus pneumoniae: virulence factors and variation Clin. Microbiol. Infect. 2010, 16 (5) 411-8
    • (2010) Clin. Microbiol. Infect. , vol.16 , Issue.5 , pp. 411-418
    • Mitchell, A.M.1    Mitchell, T.J.2
  • 4
    • 32244437802 scopus 로고    scopus 로고
    • Innate immunity and the pneumococcus
    • Paterson, G. K.; Mitchell, T. J. Innate immunity and the pneumococcus Microbiology 2006, 152 (Pt 2) 285-93
    • (2006) Microbiology , vol.152 , Issue.PART 2 , pp. 285-293
    • Paterson, G.K.1    Mitchell, T.J.2
  • 5
    • 84863599129 scopus 로고    scopus 로고
    • Impact of pneumococcal microbial surface components recognizing adhesive matrix molecules on colonization
    • Voss, S.; Gamez, G.; Hammerschmidt, S. Impact of pneumococcal microbial surface components recognizing adhesive matrix molecules on colonization Mol. Oral Microbiol. 2012, 27 (4) 246-56
    • (2012) Mol. Oral Microbiol. , vol.27 , Issue.4 , pp. 246-256
    • Voss, S.1    Gamez, G.2    Hammerschmidt, S.3
  • 6
    • 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 (1-3) 269-78
    • (2004) Biochim. Biophys. Acta , vol.1694 , Issue.13 , pp. 269-278
    • Ton-That, H.1    Marraffini, L.A.2    Schneewind, O.3
  • 8
    • 64349102718 scopus 로고    scopus 로고
    • Versatility of choline metabolism and choline-binding proteins in Streptococcus pneumoniae and commensal streptococci
    • Hakenbeck, R.; Madhour, A.; Denapaite, D.; Bruckner, R. Versatility of choline metabolism and choline-binding proteins in Streptococcus pneumoniae and commensal streptococci FEMS Microbiol. Rev. 2009, 33 (3) 572-86
    • (2009) FEMS Microbiol. Rev. , vol.33 , Issue.3 , pp. 572-586
    • Hakenbeck, R.1    Madhour, A.2    Denapaite, D.3    Bruckner, R.4
  • 9
    • 0036568587 scopus 로고    scopus 로고
    • Anchorless adhesins and invasins of Gram-positive bacteria: A new class of virulence factors
    • Chhatwal, G. S. Anchorless adhesins and invasins of Gram-positive bacteria: a new class of virulence factors Trends Microbiol. 2002, 10 (5) 205-8
    • (2002) Trends Microbiol. , vol.10 , Issue.5 , pp. 205-208
    • Chhatwal, G.S.1
  • 10
    • 80052329723 scopus 로고    scopus 로고
    • Bacterial virulence in the moonlight: Multitasking bacterial moonlighting proteins are virulence determinants in infectious disease
    • Henderson, B.; Martin, A. Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease Infect. Immun. 2011, 79 (9) 3476-91
    • (2011) Infect. Immun. , vol.79 , Issue.9 , pp. 3476-3491
    • Henderson, B.1    Martin, A.2
  • 14
    • 0034931519 scopus 로고    scopus 로고
    • Alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann, S.; Rohde, M.; Chhatwal, G. S.; Hammerschmidt, S. alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface Mol. Microbiol. 2001, 40 (6) 1273-87
    • (2001) Mol. Microbiol. , vol.40 , Issue.6 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 15
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann, S.; Rohde, M.; Hammerschmidt, S. Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein Infect. Immun. 2004, 72 (4) 2416-9
    • (2004) Infect. Immun. , vol.72 , Issue.4 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 16
    • 79960425958 scopus 로고    scopus 로고
    • The cell surface proteome of Staphylococcus aureus
    • Dreisbach, A.; van Dijl, J. M.; Buist, G. The cell surface proteome of Staphylococcus aureus Proteomics 2011, 11 (15) 3154-68
    • (2011) Proteomics , vol.11 , Issue.15 , pp. 3154-3168
    • Dreisbach, A.1    Van Dijl, J.M.2    Buist, G.3
  • 17
    • 42049098165 scopus 로고    scopus 로고
    • Shedding & shaving: Disclosure of proteomic expressions on a bacterial face
    • Tjalsma, H.; Lambooy, L.; Hermans, P. W.; Swinkels, D. W. Shedding & shaving: disclosure of proteomic expressions on a bacterial face Proteomics 2008, 8 (7) 1415-28
    • (2008) Proteomics , vol.8 , Issue.7 , pp. 1415-1428
    • Tjalsma, H.1    Lambooy, L.2    Hermans, P.W.3    Swinkels, D.W.4
  • 20
    • 17444403973 scopus 로고    scopus 로고
    • Proteome analysis of membrane and cell wall associated proteins from Staphylococcus aureus
    • Nandakumar, R.; Nandakumar, M. P.; Marten, M. R.; Ross, J. M. Proteome analysis of membrane and cell wall associated proteins from Staphylococcus aureus J. Proteome Res. 2005, 4 (2) 250-7
    • (2005) J. Proteome Res. , vol.4 , Issue.2 , pp. 250-257
    • Nandakumar, R.1    Nandakumar, M.P.2    Marten, M.R.3    Ross, J.M.4
  • 24
    • 77952372626 scopus 로고    scopus 로고
    • Improved accuracy of cell surface shaving proteomics in Staphylococcus aureus using a false-positive control
    • Solis, N.; Larsen, M. R.; Cordwell, S. J. Improved accuracy of cell surface shaving proteomics in Staphylococcus aureus using a false-positive control Proteomics 2010, 10 (10) 2037-49
    • (2010) Proteomics , vol.10 , Issue.10 , pp. 2037-2049
    • Solis, N.1    Larsen, M.R.2    Cordwell, S.J.3
  • 25
    • 77949797684 scopus 로고    scopus 로고
    • Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach
    • Hempel, K.; Pane-Farre, J.; Otto, A.; Sievers, S.; Hecker, M.; Becher, D. Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach J. Proteome Res. 2010, 9 (3) 1579-90
    • (2010) J. Proteome Res. , vol.9 , Issue.3 , pp. 1579-1590
    • Hempel, K.1    Pane-Farre, J.2    Otto, A.3    Sievers, S.4    Hecker, M.5    Becher, D.6
  • 27
    • 78651266947 scopus 로고    scopus 로고
    • Analysis of cytoplasmic membrane proteome of Streptococcus pneumoniae by shotgun proteomic approach
    • Choi, C. W.; Yun, S. H.; Kwon, S. O.; Leem, S. H.; Choi, J. S.; Yun, C. Y.; Kim, S. I. Analysis of cytoplasmic membrane proteome of Streptococcus pneumoniae by shotgun proteomic approach J. Microbiol. 2010, 48 (6) 872-6
    • (2010) J. Microbiol. , vol.48 , Issue.6 , pp. 872-876
    • Choi, C.W.1    Yun, S.H.2    Kwon, S.O.3    Leem, S.H.4    Choi, J.S.5    Yun, C.Y.6    Kim, S.I.7
  • 28
    • 80053959280 scopus 로고    scopus 로고
    • Proteomic analysis of membrane proteins from Streptococcus pneumoniae with multiple separation methods plus high accuracy mass spectrometry
    • Sun, X.; Yang, X. Y.; Yin, X. F.; Yu, G.; Xiao, C. L.; He, X.; He, Q. Y. Proteomic analysis of membrane proteins from Streptococcus pneumoniae with multiple separation methods plus high accuracy mass spectrometry OMICS 2011, 15 (10) 683-94
    • (2011) OMICS , vol.15 , Issue.10 , pp. 683-694
    • Sun, X.1    Yang, X.Y.2    Yin, X.F.3    Yu, G.4    Xiao, C.L.5    He, X.6    He, Q.Y.7
  • 30
    • 84862238853 scopus 로고    scopus 로고
    • Another turn of the screw in shaving Gram-positive bacteria: Optimization of proteomics surface protein identification in Streptococcus pneumoniae
    • Olaya-Abril, A.; Gomez-Gascon, L.; Jimenez-Munguia, I.; Obando, I.; Rodriguez-Ortega, M. J. Another turn of the screw in shaving Gram-positive bacteria: Optimization of proteomics surface protein identification in Streptococcus pneumoniae J Proteomics 2012, 75 (12) 3733-46
    • (2012) J Proteomics , vol.75 , Issue.12 , pp. 3733-3746
    • Olaya-Abril, A.1    Gomez-Gascon, L.2    Jimenez-Munguia, I.3    Obando, I.4    Rodriguez-Ortega, M.J.5
  • 32
    • 0017357391 scopus 로고
    • Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane
    • Inouye, S.; Wang, S.; Sekizawa, J.; Halegoua, S.; Inouye, M. Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane Proc. Natl. Acad. Sci. U. S. A. 1977, 74 (3) 1004-8
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , Issue.3 , pp. 1004-1008
    • Inouye, S.1    Wang, S.2    Sekizawa, J.3    Halegoua, S.4    Inouye, M.5
  • 33
    • 33645972887 scopus 로고    scopus 로고
    • A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins
    • Babu, M. M.; Priya, M. L.; Selvan, A. T.; Madera, M.; Gough, J.; Aravind, L.; Sankaran, K. A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins J. Bacteriol. 2006, 188 (8) 2761-73
    • (2006) J. Bacteriol. , vol.188 , Issue.8 , pp. 2761-2773
    • Babu, M.M.1    Priya, M.L.2    Selvan, A.T.3    Madera, M.4    Gough, J.5    Aravind, L.6    Sankaran, K.7
  • 34
    • 77956668312 scopus 로고    scopus 로고
    • The Eubacterial Lipoprotein-Specific (Type II) Signal Peptidase
    • In, 3 rd ed. Dalbey, R. E. Sigman, D. S. Academic Press: San Diego, CA, Vol.
    • Tjalsma, H.; Zanen, G.; Bron, S.; van Dijl, J. M. The Eubacterial Lipoprotein-Specific (Type II) Signal Peptidase. In The Enzymes: Co- and Posttranslational Proteolysis of Proteins, 3 rd ed.; Dalbey, R. E.,; Sigman, D. S., Eds.; Academic Press: San Diego, CA, 2001; Vol. XXII, pp 3-26.
    • (2001) The Enzymes: Co- And Posttranslational Proteolysis of Proteins , vol.22 , pp. 3-26
    • Tjalsma, H.1    Zanen, G.2    Bron, S.3    Van Dijl, J.M.4
  • 35
    • 0028128820 scopus 로고
    • Three highly homologous membrane-bound lipoproteins participate in oligopeptide transport by the Ami system of the gram-positive Streptococcus pneumoniae
    • Alloing, G.; de Philip, P.; Claverys, J. P. Three highly homologous membrane-bound lipoproteins participate in oligopeptide transport by the Ami system of the gram-positive Streptococcus pneumoniae J. Mol. Biol. 1994, 241 (1) 44-58
    • (1994) J. Mol. Biol. , vol.241 , Issue.1 , pp. 44-58
    • Alloing, G.1    De Philip, P.2    Claverys, J.P.3
  • 36
    • 0020353685 scopus 로고
    • Glyceride-cysteine lipoproteins and secretion by Gram-positive bacteria
    • Nielsen, J. B.; Lampen, J. O. Glyceride-cysteine lipoproteins and secretion by Gram-positive bacteria J. Bacteriol. 1982, 152 (1) 315-22
    • (1982) J. Bacteriol. , vol.152 , Issue.1 , pp. 315-322
    • Nielsen, J.B.1    Lampen, J.O.2
  • 37
    • 0028987131 scopus 로고
    • Lipoproteins of gram-positive bacteria
    • Sutcliffe, I. C.; Russell, R. R. Lipoproteins of gram-positive bacteria J. Bacteriol. 1995, 177 (5) 1123-8
    • (1995) J. Bacteriol. , vol.177 , Issue.5 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.2
  • 41
    • 37749051853 scopus 로고    scopus 로고
    • Maturation of Streptococcus pneumoniae lipoproteins by a type II signal peptidase is required for ABC transporter function and full virulence
    • Khandavilli, S.; Homer, K. A.; Yuste, J.; Basavanna, S.; Mitchell, T.; Brown, J. S. Maturation of Streptococcus pneumoniae lipoproteins by a type II signal peptidase is required for ABC transporter function and full virulence Mol. Microbiol. 2008, 67 (3) 541-57
    • (2008) Mol. Microbiol. , vol.67 , Issue.3 , pp. 541-557
    • Khandavilli, S.1    Homer, K.A.2    Yuste, J.3    Basavanna, S.4    Mitchell, T.5    Brown, J.S.6
  • 42
    • 67651233743 scopus 로고    scopus 로고
    • Screening of Streptococcus pneumoniae ABC transporter mutants demonstrates that LivJHMGF, a branched-chain amino acid ABC transporter, is necessary for disease pathogenesis
    • Basavanna, S.; Khandavilli, S.; Yuste, J.; Cohen, J. M.; Hosie, A. H.; Webb, A. J.; Thomas, G. H.; Brown, J. S. Screening of Streptococcus pneumoniae ABC transporter mutants demonstrates that LivJHMGF, a branched-chain amino acid ABC transporter, is necessary for disease pathogenesis Infect. Immun. 2009, 77 (8) 3412-23
    • (2009) Infect. Immun. , vol.77 , Issue.8 , pp. 3412-3423
    • Basavanna, S.1    Khandavilli, S.2    Yuste, J.3    Cohen, J.M.4    Hosie, A.H.5    Webb, A.J.6    Thomas, G.H.7    Brown, J.S.8
  • 43
    • 84864270589 scopus 로고    scopus 로고
    • Effects of Deletion of the Streptococcus pneumoniae Lipoprotein Diacylglyceryl Transferase Gene lgt on ABC Transporter Function and on Growth in Vivo
    • Chimalapati, S.; Cohen, J. M.; Camberlein, E.; Macdonald, N.; Durmort, C.; Vernet, T.; Hermans, P. W.; Mitchell, T.; Brown, J. S. Effects of Deletion of the Streptococcus pneumoniae Lipoprotein Diacylglyceryl Transferase Gene lgt on ABC Transporter Function and on Growth In Vivo PLoS One 2012, 7 (7) e41393
    • (2012) PLoS One , vol.7 , Issue.7 , pp. 41393
    • Chimalapati, S.1    Cohen, J.M.2    Camberlein, E.3    MacDonald, N.4    Durmort, C.5    Vernet, T.6    Hermans, P.W.7    Mitchell, T.8    Brown, J.S.9
  • 44
    • 40949162838 scopus 로고    scopus 로고
    • The role of Streptococcus pneumoniae virulence factors in host respiratory colonization and disease
    • Kadioglu, A.; Weiser, J. N.; Paton, J. C.; Andrew, P. W. The role of Streptococcus pneumoniae virulence factors in host respiratory colonization and disease Nat. Rev. Microbiol 2008, 6 (4) 288-301
    • (2008) Nat. Rev. Microbiol , vol.6 , Issue.4 , pp. 288-301
    • Kadioglu, A.1    Weiser, J.N.2    Paton, J.C.3    Andrew, P.W.4
  • 45
    • 84857133789 scopus 로고    scopus 로고
    • Combat pneumococcal infections: Adhesins as candidates for protein- based vaccine development
    • Gamez, G.; Hammerschmidt, S. Combat pneumococcal infections: adhesins as candidates for protein- based vaccine development Curr. Drug Targets 2012, 13 (3) 323-37
    • (2012) Curr. Drug Targets , vol.13 , Issue.3 , pp. 323-337
    • Gamez, G.1    Hammerschmidt, S.2
  • 46
    • 0035948224 scopus 로고    scopus 로고
    • Lipid modification of prelipoproteins is dispensable for growth in vitro but essential for virulence in Streptococcus pneumoniae
    • Petit, C. M.; Brown, J. R.; Ingraham, K.; Bryant, A. P.; Holmes, D. J. Lipid modification of prelipoproteins is dispensable for growth in vitro but essential for virulence in Streptococcus pneumoniae FEMS Microbiol. Lett. 2001, 200 (2) 229-33
    • (2001) FEMS Microbiol. Lett. , vol.200 , Issue.2 , pp. 229-233
    • Petit, C.M.1    Brown, J.R.2    Ingraham, K.3    Bryant, A.P.4    Holmes, D.J.5
  • 47
    • 0030968621 scopus 로고    scopus 로고
    • SpsA, a novel pneumococcal surface protein with specific binding to secretory immunoglobulin A and secretory component
    • Hammerschmidt, S.; Talay, S. R.; Brandtzaeg, P.; Chhatwal, G. S. SpsA, a novel pneumococcal surface protein with specific binding to secretory immunoglobulin A and secretory component Mol. Microbiol. 1997, 25 (6) 1113-24
    • (1997) Mol. Microbiol. , vol.25 , Issue.6 , pp. 1113-1124
    • Hammerschmidt, S.1    Talay, S.R.2    Brandtzaeg, P.3    Chhatwal, G.S.4
  • 48
    • 0036221504 scopus 로고    scopus 로고
    • Construction of new unencapsulated (rough) strains of Streptococcus pneumoniae
    • Pearce, B. J.; Iannelli, F.; Pozzi, G. Construction of new unencapsulated (rough) strains of Streptococcus pneumoniae Res. Microbiol. 2002, 153 (4) 243-7
    • (2002) Res. Microbiol. , vol.153 , Issue.4 , pp. 243-247
    • Pearce, B.J.1    Iannelli, F.2    Pozzi, G.3
  • 49
    • 35248817950 scopus 로고    scopus 로고
    • Thrombospondin-1 promotes cellular adherence of gram-positive pathogens via recognition of peptidoglycan
    • Rennemeier, C.; Hammerschmidt, S.; Niemann, S.; Inamura, S.; Zahringer, U.; Kehrel, B. E. Thrombospondin-1 promotes cellular adherence of gram-positive pathogens via recognition of peptidoglycan FASEB J. 2007, 21 (12) 3118-32
    • (2007) FASEB J. , vol.21 , Issue.12 , pp. 3118-3132
    • Rennemeier, C.1    Hammerschmidt, S.2    Niemann, S.3    Inamura, S.4    Zahringer, U.5    Kehrel, B.E.6
  • 50
    • 0025886123 scopus 로고
    • Cloning and nucleotide base sequence analysis of a spectinomycin adenyltransferase AAD(9) determinant from Enterococcus faecalis
    • LeBlanc, D. J.; Lee, L. N.; Inamine, J. M. Cloning and nucleotide base sequence analysis of a spectinomycin adenyltransferase AAD(9) determinant from Enterococcus faecalis Antimicrob. Agents Chemother. 1991, 35 (9) 1804-10
    • (1991) Antimicrob. Agents Chemother. , vol.35 , Issue.9 , pp. 1804-1810
    • Leblanc, D.J.1    Lee, L.N.2    Inamine, J.M.3
  • 51
    • 0028845364 scopus 로고
    • An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae
    • Havarstein, L. S.; Coomaraswamy, G.; Morrison, D. A. An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae Proc. Natl. Acad. Sci. U. S. A. 1995, 92 (24) 11140-4
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , Issue.24 , pp. 11140-11144
    • Havarstein, L.S.1    Coomaraswamy, G.2    Morrison, D.A.3
  • 53
    • 5644280025 scopus 로고    scopus 로고
    • The influence of agr and sigmaB in growth phase dependent regulation of virulence factors in Staphylococcus aureus
    • Ziebandt, A. K.; Becher, D.; Ohlsen, K.; Hacker, J.; Hecker, M.; Engelmann, S. The influence of agr and sigmaB in growth phase dependent regulation of virulence factors in Staphylococcus aureus Proteomics 2004, 4 (10) 3034-47
    • (2004) Proteomics , vol.4 , Issue.10 , pp. 3034-3047
    • Ziebandt, A.K.1    Becher, D.2    Ohlsen, K.3    Hacker, J.4    Hecker, M.5    Engelmann, S.6
  • 54
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 1970, 227 (5259) 680-5
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 55
    • 33748319353 scopus 로고    scopus 로고
    • Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae
    • Zybailov, B.; Mosley, A. L.; Sardiu, M. E.; Coleman, M. K.; Florens, L.; Washburn, M. P. Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae J. Proteome Res. 2006, 5 (9) 2339-47
    • (2006) J. Proteome Res. , vol.5 , Issue.9 , pp. 2339-2347
    • Zybailov, B.1    Mosley, A.L.2    Sardiu, M.E.3    Coleman, M.K.4    Florens, L.5    Washburn, M.P.6
  • 57
    • 78651335914 scopus 로고    scopus 로고
    • PSORTdb - An expanded, auto-updated, user-friendly protein subcellular localization database for Bacteria and Archaea
    • Yu, N. Y.; Laird, M. R.; Spencer, C.; Brinkman, F. S. PSORTdb - an expanded, auto-updated, user-friendly protein subcellular localization database for Bacteria and Archaea Nucleic Acids Res. 2011, 39 (Database issue) D241-4
    • (2011) Nucleic Acids Res. , vol.39 , Issue.DATABASE ISSUE , pp. 241-244
    • Yu, N.Y.1    Laird, M.R.2    Spencer, C.3    Brinkman, F.S.4
  • 58
    • 42549137778 scopus 로고    scopus 로고
    • LocateP: Genome-scale subcellular-location predictor for bacterial proteins
    • Zhou, M.; Boekhorst, J.; Francke, C.; Siezen, R. J. LocateP: genome-scale subcellular-location predictor for bacterial proteins BMC Bioinf. 2008, 9, 173
    • (2008) BMC Bioinf. , vol.9 , pp. 173
    • Zhou, M.1    Boekhorst, J.2    Francke, C.3    Siezen, R.J.4
  • 59
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes J. Mol. Biol. 2001, 305 (3) 567-80
    • (2001) J. Mol. Biol. , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 60
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Petersen, T. N.; Brunak, S.; von Heijne, G.; Nielsen, H. SignalP 4.0: discriminating signal peptides from transmembrane regions Nat. Methods 2011, 8 (10) 785-6
    • (2011) Nat. Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 61
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson, O.; Brunak, S.; von Heijne, G.; Nielsen, H. Locating proteins in the cell using TargetP, SignalP and related tools Nat. Protoc. 2007, 2 (4) 953-71
    • (2007) Nat. Protoc. , vol.2 , Issue.4 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 62
    • 52449085554 scopus 로고    scopus 로고
    • Methods for the bioinformatic identification of bacterial lipoproteins encoded in the genomes of Gram-positive bacteria
    • Rahman, O.; Cummings, S.; Harrington, D.; Sutcliffe, I. Methods for the bioinformatic identification of bacterial lipoproteins encoded in the genomes of Gram-positive bacteria World J. Microbiol. Biotechnol. 2008, 24 (11) 2377-2382
    • (2008) World J. Microbiol. Biotechnol. , vol.24 , Issue.11 , pp. 2377-2382
    • Rahman, O.1    Cummings, S.2    Harrington, D.3    Sutcliffe, I.4
  • 63
    • 33750980713 scopus 로고    scopus 로고
    • Augur - A computational pipeline for whole genome microbial surface protein prediction and classification
    • Billion, A.; Ghai, R.; Chakraborty, T.; Hain, T. Augur - a computational pipeline for whole genome microbial surface protein prediction and classification Bioinformatics 2006, 22 (22) 2819-20
    • (2006) Bioinformatics , vol.22 , Issue.22 , pp. 2819-2820
    • Billion, A.1    Ghai, R.2    Chakraborty, T.3    Hain, T.4
  • 64
    • 21844433171 scopus 로고    scopus 로고
    • Genome-wide detection and analysis of cell wall-bound proteins with LPxTG-like sorting motifs
    • Boekhorst, J.; de Been, M. W.; Kleerebezem, M.; Siezen, R. J. Genome-wide detection and analysis of cell wall-bound proteins with LPxTG-like sorting motifs J. Bacteriol. 2005, 187 (14) 4928-34
    • (2005) J. Bacteriol. , vol.187 , Issue.14 , pp. 4928-4934
    • Boekhorst, J.1    De Been, M.W.2    Kleerebezem, M.3    Siezen, R.J.4
  • 65
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley, L. A.; Sternberg, M. J. Protein structure prediction on the Web: a case study using the Phyre server Nat. Protoc. 2009, 4 (3) 363-71
    • (2009) Nat. Protoc. , vol.4 , Issue.3 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 66
    • 0030989690 scopus 로고    scopus 로고
    • The pneumococcal cell wall degrading enzymes: A modular design to create new lysins?
    • Lopez, R.; Garcia, E.; Garcia, P.; Garcia, J. L. The pneumococcal cell wall degrading enzymes: a modular design to create new lysins? Microb. Drug Resist. 1997, 3 (2) 199-211
    • (1997) Microb. Drug Resist. , vol.3 , Issue.2 , pp. 199-211
    • Lopez, R.1    Garcia, E.2    Garcia, P.3    Garcia, J.L.4
  • 67
    • 27744484159 scopus 로고    scopus 로고
    • Crystal structures of active LytM
    • Firczuk, M.; Mucha, A.; Bochtler, M. Crystal structures of active LytM J. Mol. Biol. 2005, 354 (3) 578-90
    • (2005) J. Mol. Biol. , vol.354 , Issue.3 , pp. 578-590
    • Firczuk, M.1    Mucha, A.2    Bochtler, M.3
  • 68
    • 0022425319 scopus 로고
    • Interaction of the pneumococcal amidase with lipoteichoic acid and choline
    • Briese, T.; Hakenbeck, R. Interaction of the pneumococcal amidase with lipoteichoic acid and choline Eur. J. Biochem. 1985, 146 (2) 417-27
    • (1985) Eur. J. Biochem. , vol.146 , Issue.2 , pp. 417-427
    • Briese, T.1    Hakenbeck, R.2
  • 69
    • 5144224570 scopus 로고    scopus 로고
    • Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: Crystal structure and evaluation of plasmin(ogen)-binding sites
    • Ehinger, S.; Schubert, W. D.; Bergmann, S.; Hammerschmidt, S.; Heinz, D. W. Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites J. Mol. Biol. 2004, 343 (4) 997-1005
    • (2004) J. Mol. Biol. , vol.343 , Issue.4 , pp. 997-1005
    • Ehinger, S.1    Schubert, W.D.2    Bergmann, S.3    Hammerschmidt, S.4    Heinz, D.W.5
  • 70
    • 84862577056 scopus 로고    scopus 로고
    • Membrane proteases in the bacterial protein secretion and quality control pathway
    • Dalbey, R. E.; Wang, P.; van Dijl, J. M. Membrane proteases in the bacterial protein secretion and quality control pathway Microbiol. Mol. Biol. Rev. 2012, 76 (2) 311-30
    • (2012) Microbiol. Mol. Biol. Rev. , vol.76 , Issue.2 , pp. 311-330
    • Dalbey, R.E.1    Wang, P.2    Van Dijl, J.M.3
  • 72
    • 0014227389 scopus 로고
    • Biological consequences of the replacement of choline by ethanolamine in the cell wall of Pneumococcus: Chain formation, loss of transformability, and loss of autolysis
    • Tomasz, A. Biological consequences of the replacement of choline by ethanolamine in the cell wall of Pneumococcus: chain formation, loss of transformability, and loss of autolysis Proc. Natl. Acad. Sci. U. S. A. 1968, 59 (1) 86-93
    • (1968) Proc. Natl. Acad. Sci. U. S. A. , vol.59 , Issue.1 , pp. 86-93
    • Tomasz, A.1
  • 73
    • 33745101406 scopus 로고    scopus 로고
    • Comparison of extraction procedures for proteome analysis of Streptococcus pneumoniae and a basic reference map
    • Encheva, V.; Gharbia, S. E.; Wait, R.; Begum, S.; Shah, H. N. Comparison of extraction procedures for proteome analysis of Streptococcus pneumoniae and a basic reference map Proteomics 2006, 6 (11) 3306-17
    • (2006) Proteomics , vol.6 , Issue.11 , pp. 3306-3317
    • Encheva, V.1    Gharbia, S.E.2    Wait, R.3    Begum, S.4    Shah, H.N.5
  • 76
    • 44049105749 scopus 로고    scopus 로고
    • Sequential extraction of proteins by chemical reagents
    • Cordwell, S. J. Sequential extraction of proteins by chemical reagents Methods Mol. Biol. 2008, 424, 139-46
    • (2008) Methods Mol. Biol. , vol.424 , pp. 139-146
    • Cordwell, S.J.1
  • 77
    • 79953718512 scopus 로고    scopus 로고
    • Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions
    • Hempel, K.; Herbst, F. A.; Moche, M.; Hecker, M.; Becher, D. Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions J. Proteome Res. 2011, 10 (4) 1657-66
    • (2011) J. Proteome Res. , vol.10 , Issue.4 , pp. 1657-1666
    • Hempel, K.1    Herbst, F.A.2    Moche, M.3    Hecker, M.4    Becher, D.5
  • 79
    • 84869105723 scopus 로고    scopus 로고
    • Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity
    • Potter, A. J.; Trappetti, C.; Paton, J. C. Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity J. Bacteriol. 2012, 194 (22) 6248-54
    • (2012) J. Bacteriol. , vol.194 , Issue.22 , pp. 6248-6254
    • Potter, A.J.1    Trappetti, C.2    Paton, J.C.3
  • 81
    • 0345687929 scopus 로고    scopus 로고
    • Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the fenton reaction
    • Pericone, C. D.; Park, S.; Imlay, J. A.; Weiser, J. N. Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the fenton reaction J. Bacteriol. 2003, 185 (23) 6815-25
    • (2003) J. Bacteriol. , vol.185 , Issue.23 , pp. 6815-6825
    • Pericone, C.D.1    Park, S.2    Imlay, J.A.3    Weiser, J.N.4
  • 82
    • 34548583324 scopus 로고    scopus 로고
    • SpxB is a suicide gene of Streptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model
    • Regev-Yochay, G.; Trzcinski, K.; Thompson, C. M.; Lipsitch, M.; Malley, R. SpxB is a suicide gene of Streptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model J. Bacteriol. 2007, 189 (18) 6532-9
    • (2007) J. Bacteriol. , vol.189 , Issue.18 , pp. 6532-6539
    • Regev-Yochay, G.1    Trzcinski, K.2    Thompson, C.M.3    Lipsitch, M.4    Malley, R.5
  • 83
    • 0027222723 scopus 로고
    • The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion
    • Kontinen, V. P.; Sarvas, M. The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion Mol. Microbiol. 1993, 8 (4) 727-37
    • (1993) Mol. Microbiol. , vol.8 , Issue.4 , pp. 727-737
    • Kontinen, V.P.1    Sarvas, M.2
  • 84
    • 8844264456 scopus 로고    scopus 로고
    • Post-translocational folding of secretory proteins in Gram-positive bacteria
    • Sarvas, M.; Harwood, C. R.; Bron, S.; van Dijl, J. M. Post-translocational folding of secretory proteins in Gram-positive bacteria Biochim. Biophys. Acta 2004, 1694 (1-3) 311-27
    • (2004) Biochim. Biophys. Acta , vol.1694 , Issue.13 , pp. 311-327
    • Sarvas, M.1    Harwood, C.R.2    Bron, S.3    Van Dijl, J.M.4
  • 85
    • 69949143516 scopus 로고    scopus 로고
    • Surface-associated lipoprotein PpmA of Streptococcus pneumoniae is involved in colonization in a strain-specific manner
    • Cron, L. E.; Bootsma, H. J.; Noske, N.; Burghout, P.; Hammerschmidt, S.; Hermans, P. W. Surface-associated lipoprotein PpmA of Streptococcus pneumoniae is involved in colonization in a strain-specific manner Microbiology 2009, 155 (Pt 7) 2401-10
    • (2009) Microbiology , vol.155 , Issue.PART 7 , pp. 2401-2410
    • Cron, L.E.1    Bootsma, H.J.2    Noske, N.3    Burghout, P.4    Hammerschmidt, S.5    Hermans, P.W.6
  • 86
    • 16244390503 scopus 로고    scopus 로고
    • Staphylococcus aureus deficient in lipidation of prelipoproteins is attenuated in growth and immune activation
    • Stoll, H.; Dengjel, J.; Nerz, C.; Gotz, F. Staphylococcus aureus deficient in lipidation of prelipoproteins is attenuated in growth and immune activation Infect. Immun. 2005, 73 (4) 2411-23
    • (2005) Infect. Immun. , vol.73 , Issue.4 , pp. 2411-2423
    • Stoll, H.1    Dengjel, J.2    Nerz, C.3    Gotz, F.4
  • 89
    • 33846247863 scopus 로고    scopus 로고
    • Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes
    • Baumgartner, M.; Karst, U.; Gerstel, B.; Loessner, M.; Wehland, J.; Jansch, L. Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes J. Bacteriol. 2007, 189 (2) 313-24
    • (2007) J. Bacteriol. , vol.189 , Issue.2 , pp. 313-324
    • Baumgartner, M.1    Karst, U.2    Gerstel, B.3    Loessner, M.4    Wehland, J.5    Jansch, L.6
  • 90
    • 0033043496 scopus 로고    scopus 로고
    • Lipid modification of prelipoproteins is dispensable for growth but essential for efficient protein secretion in Bacillus subtilis: Characterization of the lgt gene
    • Leskela, S.; Wahlstrom, E.; Kontinen, V. P.; Sarvas, M. Lipid modification of prelipoproteins is dispensable for growth but essential for efficient protein secretion in Bacillus subtilis: characterization of the lgt gene Mol. Microbiol. 1999, 31 (4) 1075-85
    • (1999) Mol. Microbiol. , vol.31 , Issue.4 , pp. 1075-1085
    • Leskela, S.1    Wahlstrom, E.2    Kontinen, V.P.3    Sarvas, M.4
  • 91
    • 28244497055 scopus 로고    scopus 로고
    • A proteomic analysis of penicillin resistance in Streptococcus pneumoniae reveals a novel role for PstS, a subunit of the phosphate ABC transporter
    • Soualhine, H.; Brochu, V.; Menard, F.; Papadopoulou, B.; Weiss, K.; Bergeron, M. G.; Legare, D.; Drummelsmith, J.; Ouellette, M. A proteomic analysis of penicillin resistance in Streptococcus pneumoniae reveals a novel role for PstS, a subunit of the phosphate ABC transporter Mol. Microbiol. 2005, 58 (5) 1430-40
    • (2005) Mol. Microbiol. , vol.58 , Issue.5 , pp. 1430-1440
    • Soualhine, H.1    Brochu, V.2    Menard, F.3    Papadopoulou, B.4    Weiss, K.5    Bergeron, M.G.6    Legare, D.7    Drummelsmith, J.8    Ouellette, M.9
  • 93
    • 28444440285 scopus 로고    scopus 로고
    • Proteomics-based consensus prediction of protein retention in a bacterial membrane
    • Tjalsma, H.; van Dijl, J. M. Proteomics-based consensus prediction of protein retention in a bacterial membrane Proteomics 2005, 5 (17) 4472-82
    • (2005) Proteomics , vol.5 , Issue.17 , pp. 4472-4482
    • Tjalsma, H.1    Van Dijl, J.M.2
  • 94
    • 61449214011 scopus 로고    scopus 로고
    • In the absence of Lgt, lipoproteins are shed from Streptococcus uberis independently of Lsp
    • Denham, E. L.; Ward, P. N.; Leigh, J. A. In the absence of Lgt, lipoproteins are shed from Streptococcus uberis independently of Lsp Microbiology 2009, 155 (Pt 1) 134-41
    • (2009) Microbiology , vol.155 , Issue.PART 1 , pp. 134-141
    • Denham, E.L.1    Ward, P.N.2    Leigh, J.A.3
  • 95
    • 67849130558 scopus 로고    scopus 로고
    • TOPCONS: Consensus prediction of membrane protein topology
    • Bernsel, A.; Viklund, H.; Hennerdal, A.; Elofsson, A. TOPCONS: consensus prediction of membrane protein topology Nucleic Acids Res. 2009, 37 (Web Server issue) W465-8
    • (2009) Nucleic Acids Res. , vol.37 , Issue.WEB SERVER ISSUE , pp. 465-468
    • Bernsel, A.1    Viklund, H.2    Hennerdal, A.3    Elofsson, A.4
  • 97
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • Tjalsma, H.; Bolhuis, A.; Jongbloed, J. D.; Bron, S.; van Dijl, J. M. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome Microbiol. Mol. Biol. Rev. 2000, 64 (3) 515-47
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , Issue.3 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    Van Dijl, J.M.5


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