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Volumn 84, Issue 3, 2012, Pages 405-413

Protein transport across the cell wall of monoderm Gram-positive bacteria

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; LEVANSUCRASE; LIPOTEICHOIC ACID; METALLOPROTEINASE; PEPTIDOGLYCAN; PHOSPHOLIPASE C; STAPHYLOCOCCUS ENTEROTOXIN B; SUBTILISIN;

EID: 84859939178     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08040.x     Document Type: Review
Times cited : (49)

References (81)
  • 2
    • 67650066622 scopus 로고    scopus 로고
    • The posttranslocation chaperone PrsA2 contributes to multiple facets of Listeria monocytogenes pathogenesis
    • Alonzo, F., 3rd, Port, G.C., Cao, M., and Freitag, N.E. (2009) The posttranslocation chaperone PrsA2 contributes to multiple facets of Listeria monocytogenes pathogenesis. Infect Immun 77: 2612-2623.
    • (2009) Infect Immun , vol.77 , pp. 2612-2623
    • Alonzo 3rd, F.1    Port, G.C.2    Cao, M.3    Freitag, N.E.4
  • 3
    • 79958811002 scopus 로고    scopus 로고
    • Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence
    • Alonzo, F., III, Xayarath, B., Whisstock, J.C., and Freitag, N.E. (2011) Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence. Mol Microbiol 80: 1530-1548.
    • (2011) Mol Microbiol , vol.80 , pp. 1530-1548
    • Alonzo III, F.1    Xayarath, B.2    Whisstock, J.C.3    Freitag, N.E.4
  • 4
    • 0031754136 scopus 로고    scopus 로고
    • Peptidoglycan structural dynamics during germination of Bacillus subtilis 168 endospores
    • Atrih, A., Zollner, P., Allmaier, G., Williamson, M., and Foster, S.J. (1998) Peptidoglycan structural dynamics during germination of Bacillus subtilis 168 endospores. J Bacteriol 180: 4603-4612.
    • (1998) J Bacteriol , vol.180 , pp. 4603-4612
    • Atrih, A.1    Zollner, P.2    Allmaier, G.3    Williamson, M.4    Foster, S.J.5
  • 5
    • 0018830034 scopus 로고
    • Sites of metal deposition in the cell wall of Bacillus subtilis
    • Beveridge, T.J., and Murray, R.G. (1980) Sites of metal deposition in the cell wall of Bacillus subtilis. J Bacteriol 141: 876-887.
    • (1980) J Bacteriol , vol.141 , pp. 876-887
    • Beveridge, T.J.1    Murray, R.G.2
  • 6
    • 37549035018 scopus 로고    scopus 로고
    • The metalloprotease of Listeria monocytogenes is activated by intramolecular autocatalysis
    • Bitar, A.P., Cao, M., and Marquis, H. (2008) The metalloprotease of Listeria monocytogenes is activated by intramolecular autocatalysis. J Bacteriol 190: 107-111.
    • (2008) J Bacteriol , vol.190 , pp. 107-111
    • Bitar, A.P.1    Cao, M.2    Marquis, H.3
  • 7
    • 0023643147 scopus 로고
    • The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry
    • Bode, W., Papamokos, E., and Musil, D. (1987) The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry. Eur J Biochem 166: 673-692.
    • (1987) Eur J Biochem , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 8
    • 12844288619 scopus 로고    scopus 로고
    • EsxA and EsxB are secreted by an ESAT-6-like system that is required for the pathogenesis of Staphylococcus aureus infections
    • Burts, M.L., Williams, W.A., Debord, K., and Missiakas, D.M. (2005) EsxA and EsxB are secreted by an ESAT-6-like system that is required for the pathogenesis of Staphylococcus aureus infections. Proc Natl Acad Sci USA 102: 1169-1174.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1169-1174
    • Burts, M.L.1    Williams, W.A.2    Debord, K.3    Missiakas, D.M.4
  • 9
    • 0035910012 scopus 로고    scopus 로고
    • Evidence that the cell wall of Bacillus subtilis is protonated during respiration
    • Calamita, H.G., Ehringer, W.D., Koch, A.L., and Doyle, R.J. (2001) Evidence that the cell wall of Bacillus subtilis is protonated during respiration. Proc Natl Acad Sci USA 98: 15260-15263.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15260-15263
    • Calamita, H.G.1    Ehringer, W.D.2    Koch, A.L.3    Doyle, R.J.4
  • 10
    • 0032844039 scopus 로고    scopus 로고
    • Anionic polymers of Bacillus subtilis cell wall modulate the folding rate of secreted proteins
    • Chambert, R., and Petit-Glatron, M.F. (1999) Anionic polymers of Bacillus subtilis cell wall modulate the folding rate of secreted proteins. FEMS Microbiol Lett 179: 43-47.
    • (1999) FEMS Microbiol Lett , vol.179 , pp. 43-47
    • Chambert, R.1    Petit-Glatron, M.F.2
  • 11
    • 0025191308 scopus 로고
    • Secretion of Bacillus subtilis levansucrase. Fe(III) could act as a cofactor in an efficient coupling of the folding and translocation processes
    • Chambert, R., Benyahia, F., and Petit-Glatron, M.F. (1990) Secretion of Bacillus subtilis levansucrase. Fe(III) could act as a cofactor in an efficient coupling of the folding and translocation processes. Biochem J 265: 375-382.
    • (1990) Biochem J , vol.265 , pp. 375-382
    • Chambert, R.1    Benyahia, F.2    Petit-Glatron, M.F.3
  • 12
    • 3042596928 scopus 로고    scopus 로고
    • DNA uptake during bacterial transformation
    • Chen, I., and Dubnau, D. (2004) DNA uptake during bacterial transformation. Nat Rev Microbiol 2: 241-249.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 241-249
    • Chen, I.1    Dubnau, D.2
  • 13
    • 0034107664 scopus 로고    scopus 로고
    • Characteristics of the biologically active 35-kDa metalloprotease virulence factor from Listeria monocytogenes
    • Coffey, A., van den Burg, B., Veltman, R., and Abee, T. (2000) Characteristics of the biologically active 35-kDa metalloprotease virulence factor from Listeria monocytogenes. J Appl Microbiol 88: 132-141.
    • (2000) J Appl Microbiol , vol.88 , pp. 132-141
    • Coffey, A.1    van den Burg, B.2    Veltman, R.3    Abee, T.4
  • 14
    • 0030047151 scopus 로고    scopus 로고
    • The permeability of the wall fabric of Escherichia coli and Bacillus subtilis
    • Demchick, P., and Koch, A.L. (1996) The permeability of the wall fabric of Escherichia coli and Bacillus subtilis. J Bacteriol 178: 768-773.
    • (1996) J Bacteriol , vol.178 , pp. 768-773
    • Demchick, P.1    Koch, A.L.2
  • 15
    • 33746903479 scopus 로고    scopus 로고
    • The protein secretion systems in Listeria: inside out bacterial virulence
    • Desvaux, M., and Hebraud, M. (2006) The protein secretion systems in Listeria: inside out bacterial virulence. FEMS Microbiol Rev 30: 774-805.
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 774-805
    • Desvaux, M.1    Hebraud, M.2
  • 16
    • 63549137674 scopus 로고    scopus 로고
    • Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue
    • Desvaux, M., Hebraud, M., Talon, R., and Henderson, I.R. (2009) Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Trends Microbiol 17: 139-145.
    • (2009) Trends Microbiol , vol.17 , pp. 139-145
    • Desvaux, M.1    Hebraud, M.2    Talon, R.3    Henderson, I.R.4
  • 19
    • 80055050377 scopus 로고    scopus 로고
    • Posttranslocation chaperone PrsA2 regulates the maturation and secretion of Listeria monocytogenes proprotein virulence factors
    • Forster, B.M., Zemansky, J., Portnoy, D.A., and Marquis, H. (2011b) Posttranslocation chaperone PrsA2 regulates the maturation and secretion of Listeria monocytogenes proprotein virulence factors. J Bacteriol 193: 5961-5970.
    • (2011) J Bacteriol , vol.193 , pp. 5961-5970
    • Forster, B.M.1    Zemansky, J.2    Portnoy, D.A.3    Marquis, H.4
  • 20
    • 0016671593 scopus 로고
    • Release of extracellular enzymes from Bacillus amyloliquefaciens
    • Gould, A.R., May, B.K., and Elliott, W.H. (1975) Release of extracellular enzymes from Bacillus amyloliquefaciens. J Bacteriol 122: 34-40.
    • (1975) J Bacteriol , vol.122 , pp. 34-40
    • Gould, A.R.1    May, B.K.2    Elliott, W.H.3
  • 21
    • 0030691082 scopus 로고    scopus 로고
    • Characterization of a stable intermediate trapped during reversible refolding of Bacillus subtilis alpha-amylase
    • Haddaoui, E.A., Leloup, L., Petit-Glatron, M.F., and Chambert, R. (1997) Characterization of a stable intermediate trapped during reversible refolding of Bacillus subtilis alpha-amylase. Eur J Biochem 249: 505-509.
    • (1997) Eur J Biochem , vol.249 , pp. 505-509
    • Haddaoui, E.A.1    Leloup, L.2    Petit-Glatron, M.F.3    Chambert, R.4
  • 22
    • 78149443620 scopus 로고    scopus 로고
    • Bacterial contact-dependent delivery systems
    • Hayes, C.S., Aoki, S.K., and Low, D.A. (2010) Bacterial contact-dependent delivery systems. Annu Rev Genet 44: 71-90.
    • (2010) Annu Rev Genet , vol.44 , pp. 71-90
    • Hayes, C.S.1    Aoki, S.K.2    Low, D.A.3
  • 24
    • 0034282698 scopus 로고    scopus 로고
    • d-alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis
    • Hyyrylainen, H.L., Vitikainen, M., Thwaite, J., Wu, H., Sarvas, M., Harwood, C.R., etal. (2000) d-alanine substitution of teichoic acids as a modulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis. J Biol Chem 275: 26696-26703.
    • (2000) J Biol Chem , vol.275 , pp. 26696-26703
    • Hyyrylainen, H.L.1    Vitikainen, M.2    Thwaite, J.3    Wu, H.4    Sarvas, M.5    Harwood, C.R.6
  • 25
    • 77953985332 scopus 로고    scopus 로고
    • Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis
    • Hyyrylainen, H.L., Marciniak, B.C., Dahncke, K., Pietiainen, M., Courtin, P., Vitikainen, M., etal. (2010) Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis. Mol Microbiol 77: 108-127.
    • (2010) Mol Microbiol , vol.77 , pp. 108-127
    • Hyyrylainen, H.L.1    Marciniak, B.C.2    Dahncke, K.3    Pietiainen, M.4    Courtin, P.5    Vitikainen, M.6
  • 26
    • 0027264910 scopus 로고
    • Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro-sequences
    • Jacobs, M., Andersen, J.B., Kontinen, V., and Sarvas, M. (1993) Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro-sequences. Mol Microbiol 8: 957-966.
    • (1993) Mol Microbiol , vol.8 , pp. 957-966
    • Jacobs, M.1    Andersen, J.B.2    Kontinen, V.3    Sarvas, M.4
  • 27
    • 0019452877 scopus 로고
    • The energized membrane and cellular autolysis in Bacillus subtilis
    • Jolliffe, L.K., Doyle, R.J., and Streips, U.N. (1981) The energized membrane and cellular autolysis in Bacillus subtilis. Cell 25: 753-763.
    • (1981) Cell , vol.25 , pp. 753-763
    • Jolliffe, L.K.1    Doyle, R.J.2    Streips, U.N.3
  • 29
    • 0027236008 scopus 로고
    • Proton motive force may regulate cell wall-associated enzymes of Bacillus subtilis
    • Kemper, M.A., Urrutia, M.M., Beveridge, T.J., Koch, A.L., and Doyle, R.J. (1993) Proton motive force may regulate cell wall-associated enzymes of Bacillus subtilis. J Bacteriol 175: 5690-5696.
    • (1993) J Bacteriol , vol.175 , pp. 5690-5696
    • Kemper, M.A.1    Urrutia, M.M.2    Beveridge, T.J.3    Koch, A.L.4    Doyle, R.J.5
  • 30
    • 0022344822 scopus 로고
    • Inside-to-outside growth and turnover of the wall of gram-positive rods
    • Koch, A.L., and Doyle, R.J. (1985) Inside-to-outside growth and turnover of the wall of gram-positive rods. J Theor Biol 117: 137-157.
    • (1985) J Theor Biol , vol.117 , pp. 137-157
    • Koch, A.L.1    Doyle, R.J.2
  • 31
    • 79954784829 scopus 로고    scopus 로고
    • Molecular aspects of bacterial pH sensing and homeostasis
    • Krulwich, T.A., Sachs, G., and Padan, E. (2011) Molecular aspects of bacterial pH sensing and homeostasis. Nat Rev Microbiol 9: 330-343.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 330-343
    • Krulwich, T.A.1    Sachs, G.2    Padan, E.3
  • 32
    • 0030831592 scopus 로고    scopus 로고
    • Characterization of the rate-limiting step of the secretion of Bacillus subtilis alpha-amylase overproduced during the exponential phase of growth
    • Leloup, L., Haddaoui, el-A, Chambert, R., and Petit-Glatron, M.F. (1997) Characterization of the rate-limiting step of the secretion of Bacillus subtilis alpha-amylase overproduced during the exponential phase of growth. Microbiology 143 (Part 10): 3295-3303.
    • (1997) Microbiology , vol.143 , Issue.PART 10 , pp. 3295-3303
    • Leloup, L.1    Haddaoui, E.-A.2    Chambert, R.3    Petit-Glatron, M.F.4
  • 33
    • 73849167296 scopus 로고
    • Cellular resistance to infection
    • Mackaness, G.B. (1962) Cellular resistance to infection. J Exp Med 116: 381-406.
    • (1962) J Exp Med , vol.116 , pp. 381-406
    • Mackaness, G.B.1
  • 34
    • 0033955871 scopus 로고    scopus 로고
    • pH-regulated activation and release of a bacteria-associated phospholipase C during intracellular infection by Listeria monocytogenes
    • Marquis, H., and Hager, E.J. (2000) pH-regulated activation and release of a bacteria-associated phospholipase C during intracellular infection by Listeria monocytogenes. Mol Microbiol 35: 289-298.
    • (2000) Mol Microbiol , vol.35 , pp. 289-298
    • Marquis, H.1    Hager, E.J.2
  • 35
    • 0028822997 scopus 로고
    • The broad-range phospholipase C and a metalloprotease mediate listeriolysin O-independent escape of Listeria monocytogenes from a primary vacuole in human epithelial cells
    • Marquis, H., Doshi, V., and Portnoy, D.A. (1995) The broad-range phospholipase C and a metalloprotease mediate listeriolysin O-independent escape of Listeria monocytogenes from a primary vacuole in human epithelial cells. Infect Immun 63: 4531-4534.
    • (1995) Infect Immun , vol.63 , pp. 4531-4534
    • Marquis, H.1    Doshi, V.2    Portnoy, D.A.3
  • 36
    • 0030955705 scopus 로고    scopus 로고
    • Proteolytic pathways of activation and degradation of a bacterial phospholipase C during intracellular infection by Listeria monocytogenes
    • Marquis, H., Goldfine, H., and Portnoy, D.A. (1997) Proteolytic pathways of activation and degradation of a bacterial phospholipase C during intracellular infection by Listeria monocytogenes. J Cell Biol 137: 1381-1392.
    • (1997) J Cell Biol , vol.137 , pp. 1381-1392
    • Marquis, H.1    Goldfine, H.2    Portnoy, D.A.3
  • 37
    • 16244387909 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space
    • Matias, V.R., and Beveridge, T.J. (2005) Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space. Mol Microbiol 56: 240-251.
    • (2005) Mol Microbiol , vol.56 , pp. 240-251
    • Matias, V.R.1    Beveridge, T.J.2
  • 38
    • 31344459535 scopus 로고    scopus 로고
    • Native cell wall organization shown by cryo-electron microscopy confirms the existence of a periplasmic space in Staphylococcus aureus
    • Matias, V.R., and Beveridge, T.J. (2006) Native cell wall organization shown by cryo-electron microscopy confirms the existence of a periplasmic space in Staphylococcus aureus. J Bacteriol 188: 1011-1021.
    • (2006) J Bacteriol , vol.188 , pp. 1011-1021
    • Matias, V.R.1    Beveridge, T.J.2
  • 39
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian, S.K., Liu, G., Ton-That, H., and Schneewind, O. (1999) Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 285: 760-763.
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 40
    • 0025977915 scopus 로고
    • Identification of a new operon involved in Listeria monocytogenes virulence: its first gene encodes a protein homologous to bacterial metalloproteases
    • Mengaud, J., Geoffroy, C., and Cossart, P. (1991) Identification of a new operon involved in Listeria monocytogenes virulence: its first gene encodes a protein homologous to bacterial metalloproteases. Infect Immun 59: 1043-1049.
    • (1991) Infect Immun , vol.59 , pp. 1043-1049
    • Mengaud, J.1    Geoffroy, C.2    Cossart, P.3
  • 41
    • 0034861858 scopus 로고    scopus 로고
    • Superantigen bacterial toxins: state of the art
    • Muller-Alouf, H., Carnoy, C., Simonet, M., and Alouf, J.E. (2001) Superantigen bacterial toxins: state of the art. Toxicon 39: 1691-1701.
    • (2001) Toxicon , vol.39 , pp. 1691-1701
    • Muller-Alouf, H.1    Carnoy, C.2    Simonet, M.3    Alouf, J.E.4
  • 42
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre, W.W., and Schneewind, O. (1999) Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol Mol Biol Rev 63: 174-229.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 43
    • 66149141835 scopus 로고    scopus 로고
    • The propeptide of the metalloprotease of Listeria monocytogenes controls compartmentalization of the zymogen during intracellular infection
    • O'Neil, H.S., Forster, B.M., Roberts, K.L., Chambers, A.J., Bitar, A., and Marquis, H. (2009) The propeptide of the metalloprotease of Listeria monocytogenes controls compartmentalization of the zymogen during intracellular infection. J Bacteriol 191: 3594-3603.
    • (2009) J Bacteriol , vol.191 , pp. 3594-3603
    • O'Neil, H.S.1    Forster, B.M.2    Roberts, K.L.3    Chambers, A.J.4    Bitar, A.5    Marquis, H.6
  • 44
    • 0014711579 scopus 로고
    • Electromechanical interactions in cell walls of gram-positive cocci
    • Ou, L.T., and Marquis, R.E. (1970) Electromechanical interactions in cell walls of gram-positive cocci. J Bacteriol 101: 92-101.
    • (1970) J Bacteriol , vol.101 , pp. 92-101
    • Ou, L.T.1    Marquis, R.E.2
  • 45
    • 0023691688 scopus 로고
    • The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case
    • Pantoliano, M.W., Whitlow, M., Wood, J.F., Rollence, M.L., Finzel, B.C., Gilliland, G.L., etal. (1988) The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case. Biochemistry 27: 8311-8317.
    • (1988) Biochemistry , vol.27 , pp. 8311-8317
    • Pantoliano, M.W.1    Whitlow, M.2    Wood, J.F.3    Rollence, M.L.4    Finzel, B.C.5    Gilliland, G.L.6
  • 46
    • 0032549518 scopus 로고    scopus 로고
    • Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors
    • Papageorgiou, A.C., Tranter, H.S., and Acharya, K.R. (1998) Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors. J Mol Biol 277: 61-79.
    • (1998) J Mol Biol , vol.277 , pp. 61-79
    • Papageorgiou, A.C.1    Tranter, H.S.2    Acharya, K.R.3
  • 47
    • 0028982844 scopus 로고
    • Incorporation of d-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation
    • Perego, M., Glaser, P., Minutello, A., Strauch, M.A., Leopold, K., and Fischer, W. (1995) Incorporation of d-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation. J Biol Chem 270: 15598-15606.
    • (1995) J Biol Chem , vol.270 , pp. 15598-15606
    • Perego, M.1    Glaser, P.2    Minutello, A.3    Strauch, M.A.4    Leopold, K.5    Fischer, W.6
  • 48
    • 0027297013 scopus 로고
    • The contribution of the cell wall to a transmembrane calcium gradient could play a key role in Bacillus subtilis protein secretion
    • Petit-Glatron, M.F., Grajcar, L., Munz, A., and Chambert, R. (1993) The contribution of the cell wall to a transmembrane calcium gradient could play a key role in Bacillus subtilis protein secretion. Mol Microbiol 9: 1097-1106.
    • (1993) Mol Microbiol , vol.9 , pp. 1097-1106
    • Petit-Glatron, M.F.1    Grajcar, L.2    Munz, A.3    Chambert, R.4
  • 50
    • 77956107104 scopus 로고    scopus 로고
    • Heterologous protein secretion by Bacillus species from the cradle to the grave
    • Pohl, S., and Harwood, C.R. (2010) Heterologous protein secretion by Bacillus species from the cradle to the grave. Adv Appl Microbiol 73: 1-25.
    • (2010) Adv Appl Microbiol , vol.73 , pp. 1-25
    • Pohl, S.1    Harwood, C.R.2
  • 51
    • 0026587933 scopus 로고
    • Molecular determinants of Listeria monocytogenes pathogenesis
    • Portnoy, D.A., Chakraborty, T., Goebel, W., and Cossart, P. (1992) Molecular determinants of Listeria monocytogenes pathogenesis. Infect Immun 60: 1263-1267.
    • (1992) Infect Immun , vol.60 , pp. 1263-1267
    • Portnoy, D.A.1    Chakraborty, T.2    Goebel, W.3    Cossart, P.4
  • 52
    • 0000295996 scopus 로고
    • Secretion and autoproteolytic maturation of subtilisin
    • Power, S.D., Adams, R.M., and Wells, J.A. (1986) Secretion and autoproteolytic maturation of subtilisin. Proc Natl Acad Sci USA 83: 3096-3100.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3096-3100
    • Power, S.D.1    Adams, R.M.2    Wells, J.A.3
  • 53
    • 0027416460 scopus 로고
    • The zinc metalloprotease of Listeria monocytogenes is required for maturation of phosphatidylcholine phospholipase C: direct evidence obtained by gene complementation
    • Poyart, C., Abachin, E., Razafimanantsoa, I., and Berche, P. (1993) The zinc metalloprotease of Listeria monocytogenes is required for maturation of phosphatidylcholine phospholipase C: direct evidence obtained by gene complementation. Infect Immun 61: 1576-1580.
    • (1993) Infect Immun , vol.61 , pp. 1576-1580
    • Poyart, C.1    Abachin, E.2    Razafimanantsoa, I.3    Berche, P.4
  • 54
    • 79956141388 scopus 로고    scopus 로고
    • Location, synthesis and function of glycolipids and polyglycerolphosphate lipoteichoic acid in Gram-positive bacteria of the phylum Firmicutes
    • Reichmann, N.T., and Grundling, A. (2011) Location, synthesis and function of glycolipids and polyglycerolphosphate lipoteichoic acid in Gram-positive bacteria of the phylum Firmicutes. FEMS Microbiol Lett 319: 97-105.
    • (2011) FEMS Microbiol Lett , vol.319 , pp. 97-105
    • Reichmann, N.T.1    Grundling, A.2
  • 55
    • 78650507281 scopus 로고    scopus 로고
    • Bacillus anthracis produces membrane-derived vesicles containing biologically active toxins
    • Rivera, J., Cordero, R.J., Nakouzi, A.S., Frases, S., Nicola, A., and Casadevall, A. (2010) Bacillus anthracis produces membrane-derived vesicles containing biologically active toxins. Proc Natl Acad Sci USA 107: 19002-19007.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19002-19007
    • Rivera, J.1    Cordero, R.J.2    Nakouzi, A.S.3    Frases, S.4    Nicola, A.5    Casadevall, A.6
  • 56
    • 79851514906 scopus 로고    scopus 로고
    • Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria
    • Robinson, C., Matos, C.F., Beck, D., Ren, C., Lawrence, J., Vasisht, N., and Mendel, S. (2011) Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria. Biochim Biophys Acta 1808: 876-884.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 876-884
    • Robinson, C.1    Matos, C.F.2    Beck, D.3    Ren, C.4    Lawrence, J.5    Vasisht, N.6    Mendel, S.7
  • 57
    • 2642540881 scopus 로고    scopus 로고
    • A microdomain for protein secretion in gram-positive bacteria
    • Rosch, J., and Caparon, M. (2004) A microdomain for protein secretion in gram-positive bacteria. Science 304: 1513-1515.
    • (2004) Science , vol.304 , pp. 1513-1515
    • Rosch, J.1    Caparon, M.2
  • 58
    • 39649099979 scopus 로고    scopus 로고
    • Lytic transglycosylases: bacterial space-making autolysins
    • Scheurwater, E., Reid, C.W., and Clarke, A.J. (2008) Lytic transglycosylases: bacterial space-making autolysins. Int J Biochem Cell Biol 40: 586-591.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 586-591
    • Scheurwater, E.1    Reid, C.W.2    Clarke, A.J.3
  • 59
    • 78649832487 scopus 로고    scopus 로고
    • Differentiation of propeptide residues regulating the compartmentalization, maturation and activity of the broad-range phospholipase C of Listeria monocytogenes
    • Slepkov, E.R., Pavinski Bitar, A., and Marquis, H. (2010) Differentiation of propeptide residues regulating the compartmentalization, maturation and activity of the broad-range phospholipase C of Listeria monocytogenes. Biochem J 432: 557-563.
    • (2010) Biochem J , vol.432 , pp. 557-563
    • Slepkov, E.R.1    Pavinski Bitar, A.2    Marquis, H.3
  • 60
    • 0028828198 scopus 로고
    • The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread
    • Smith, G.A., Marquis, H., Jones, S., Johnston, N.C., Portnoy, D.A., and Goldfine, H. (1995) The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread. Infect Immun 63: 4231-4237.
    • (1995) Infect Immun , vol.63 , pp. 4231-4237
    • Smith, G.A.1    Marquis, H.2    Jones, S.3    Johnston, N.C.4    Portnoy, D.A.5    Goldfine, H.6
  • 61
    • 0141925909 scopus 로고    scopus 로고
    • Restricted translocation across the cell wall regulates secretion of the broad-range phospholipase C of Listeria monocytogenes
    • Snyder, A., and Marquis, H. (2003) Restricted translocation across the cell wall regulates secretion of the broad-range phospholipase C of Listeria monocytogenes. J Bacteriol 185: 5953-5958.
    • (2003) J Bacteriol , vol.185 , pp. 5953-5958
    • Snyder, A.1    Marquis, H.2
  • 62
    • 0032479216 scopus 로고    scopus 로고
    • The influence of protein folding on late stages of the secretion of alpha-amylases from Bacillus subtilis
    • Stephenson, K., Carter, N.M., Harwood, C.R., Petit-Glatron, M.F., and Chambert, R. (1998) The influence of protein folding on late stages of the secretion of alpha-amylases from Bacillus subtilis. FEBS Lett 430: 385-389.
    • (1998) FEBS Lett , vol.430 , pp. 385-389
    • Stephenson, K.1    Carter, N.M.2    Harwood, C.R.3    Petit-Glatron, M.F.4    Chambert, R.5
  • 63
    • 77956988767 scopus 로고    scopus 로고
    • A phylum level perspective on bacterial cell envelope architecture
    • Sutcliffe, I.C. (2010) A phylum level perspective on bacterial cell envelope architecture. Trends Microbiol 18: 464-470.
    • (2010) Trends Microbiol , vol.18 , pp. 464-470
    • Sutcliffe, I.C.1
  • 64
    • 79952446159 scopus 로고    scopus 로고
    • New insights into the distribution of WXG100 protein secretion systems
    • Sutcliffe, I.C. (2011) New insights into the distribution of WXG100 protein secretion systems. Antonie Van Leeuwenhoek 99: 127-131.
    • (2011) Antonie Van Leeuwenhoek , vol.99 , pp. 127-131
    • Sutcliffe, I.C.1
  • 65
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes
    • Tilney, L.G., and Portnoy, D.A. (1989) Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J Cell Biol 109: 1597-1608.
    • (1989) J Cell Biol , vol.109 , pp. 1597-1608
    • Tilney, L.G.1    Portnoy, D.A.2
  • 66
    • 0020584796 scopus 로고
    • Transport and processing of staphylococcal enterotoxin B
    • Tweten, R.K., and Iandolo, J.J. (1983) Transport and processing of staphylococcal enterotoxin B. J Bacteriol 153: 297-303.
    • (1983) J Bacteriol , vol.153 , pp. 297-303
    • Tweten, R.K.1    Iandolo, J.J.2
  • 67
    • 0026502412 scopus 로고
    • Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread
    • Vazquez-Boland, J.-A., Kocks, C., Dramsi, S., Ohayon, H., Geoffroy, C., Mengaud, J., and Cossart, P. (1992) Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread. Infect Immun 60: 219-230.
    • (1992) Infect Immun , vol.60 , pp. 219-230
    • Vazquez-Boland, J.-A.1    Kocks, C.2    Dramsi, S.3    Ohayon, H.4    Geoffroy, C.5    Mengaud, J.6    Cossart, P.7
  • 68
    • 0035108399 scopus 로고    scopus 로고
    • Quantitation of the capacity of the secretion apparatus and requirement for PrsA in growth and secretion of alpha-amylase in Bacillus subtilis
    • Vitikainen, M., Pummi, T., Airaksinen, U., Wahlstrom, E., Wu, H., Sarvas, M., and Kontinen, V.P. (2001) Quantitation of the capacity of the secretion apparatus and requirement for PrsA in growth and secretion of alpha-amylase in Bacillus subtilis. J Bacteriol 183: 1881-1890.
    • (2001) J Bacteriol , vol.183 , pp. 1881-1890
    • Vitikainen, M.1    Pummi, T.2    Airaksinen, U.3    Wahlstrom, E.4    Wu, H.5    Sarvas, M.6    Kontinen, V.P.7
  • 69
    • 2442446271 scopus 로고    scopus 로고
    • Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis
    • Vitikainen, M., Lappalainen, I., Seppala, R., Antelmann, H., Boer, H., Taira, S., etal. (2004) Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis. J Biol Chem 279: 19302-19314.
    • (2004) J Biol Chem , vol.279 , pp. 19302-19314
    • Vitikainen, M.1    Lappalainen, I.2    Seppala, R.3    Antelmann, H.4    Boer, H.5    Taira, S.6
  • 71
    • 0033768655 scopus 로고    scopus 로고
    • Holins: the protein clocks of bacteriophage infections
    • Wang, I.N., Smith, D.L., and Young, R. (2000) Holins: the protein clocks of bacteriophage infections. Annu Rev Microbiol 54: 799-825.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 799-825
    • Wang, I.N.1    Smith, D.L.2    Young, R.3
  • 72
    • 0015848145 scopus 로고
    • The chain length of the glycans in bacterial cell walls
    • Ward, J.B. (1973) The chain length of the glycans in bacterial cell walls. Biochem J 133: 395-398.
    • (1973) Biochem J , vol.133 , pp. 395-398
    • Ward, J.B.1
  • 73
    • 40949089662 scopus 로고    scopus 로고
    • Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions
    • Weidenmaier, C., and Peschel, A. (2008) Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions. Nat Rev Microbiol 6: 276-287.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 276-287
    • Weidenmaier, C.1    Peschel, A.2
  • 74
    • 82155168230 scopus 로고    scopus 로고
    • Super-resolution microscopy reveals cell wall dynamics and peptidoglycan architecture in ovococcal bacteria
    • Wheeler, R., Mesnage, S., Boneca, I.G., Hobbs, J.K., and Foster, S.J. (2011) Super-resolution microscopy reveals cell wall dynamics and peptidoglycan architecture in ovococcal bacteria. Mol Microbiol 82: 1096-1109.
    • (2011) Mol Microbiol , vol.82 , pp. 1096-1109
    • Wheeler, R.1    Mesnage, S.2    Boneca, I.G.3    Hobbs, J.K.4    Foster, S.J.5
  • 75
    • 0035976917 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin
    • Yabuta, Y., Takagi, H., Inouye, M., and Shinde, U. (2001) Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin. J Biol Chem 276: 44427-44434.
    • (2001) J Biol Chem , vol.276 , pp. 44427-44434
    • Yabuta, Y.1    Takagi, H.2    Inouye, M.3    Shinde, U.4
  • 76
    • 16844364774 scopus 로고    scopus 로고
    • The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C
    • Yeung, P.S., Zagorski, N., and Marquis, H. (2005) The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C. J Bacteriol 187: 2601-2608.
    • (2005) J Bacteriol , vol.187 , pp. 2601-2608
    • Yeung, P.S.1    Zagorski, N.2    Marquis, H.3
  • 77
    • 33846024757 scopus 로고    scopus 로고
    • Compartmentalization of the broad-range phospholipase C activity to the spreading vacuole is critical for Listeria monocytogenes virulence
    • Yeung, P.S., Na, Y., Kreuder, A.J., and Marquis, H. (2007) Compartmentalization of the broad-range phospholipase C activity to the spreading vacuole is critical for Listeria monocytogenes virulence. Infect Immun 75: 44-51.
    • (2007) Infect Immun , vol.75 , pp. 44-51
    • Yeung, P.S.1    Na, Y.2    Kreuder, A.J.3    Marquis, H.4
  • 78
    • 67549122388 scopus 로고    scopus 로고
    • Development of a mariner-based transposon and identification of Listeria monocytogenes determinants, including the peptidyl-prolyl isomerase PrsA2, that contribute to its hemolytic phenotype
    • Zemansky, J., Kline, B.C., Woodward, J.J., Leber, J.H., Marquis, H., and Portnoy, D.A. (2009) Development of a mariner-based transposon and identification of Listeria monocytogenes determinants, including the peptidyl-prolyl isomerase PrsA2, that contribute to its hemolytic phenotype. J Bacteriol 191: 3950-3964.
    • (2009) J Bacteriol , vol.191 , pp. 3950-3964
    • Zemansky, J.1    Kline, B.C.2    Woodward, J.J.3    Leber, J.H.4    Marquis, H.5    Portnoy, D.A.6
  • 79
    • 0024409494 scopus 로고
    • Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process
    • Zhu, X.L., Ohta, Y., Jordan, F., and Inouye, M. (1989) Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Nature 339: 483-484.
    • (1989) Nature , vol.339 , pp. 483-484
    • Zhu, X.L.1    Ohta, Y.2    Jordan, F.3    Inouye, M.4
  • 80
    • 33748804439 scopus 로고    scopus 로고
    • Granular layer in the periplasmic space of gram-positive bacteria and fine structures of Enterococcus gallinarum and Streptococcus gordonii septa revealed by cryo-electron microscopy of vitreous sections
    • Zuber, B., Haenni, M., Ribeiro, T., Minnig, K., Lopes, F., Moreillon, P., and Dubochet, J. (2006) Granular layer in the periplasmic space of gram-positive bacteria and fine structures of Enterococcus gallinarum and Streptococcus gordonii septa revealed by cryo-electron microscopy of vitreous sections. J Bacteriol 188: 6652-6660.
    • (2006) J Bacteriol , vol.188 , pp. 6652-6660
    • Zuber, B.1    Haenni, M.2    Ribeiro, T.3    Minnig, K.4    Lopes, F.5    Moreillon, P.6    Dubochet, J.7
  • 81
    • 0031711951 scopus 로고    scopus 로고
    • Modulation of enzymatic activity and biological function of Listeria monocytogenes broad-range phospholipase C by amino acid substitutions and by replacement with the Bacillus cereus ortholog
    • Zuckert, W.R., Marquis, H., and Goldfine, H. (1998) Modulation of enzymatic activity and biological function of Listeria monocytogenes broad-range phospholipase C by amino acid substitutions and by replacement with the Bacillus cereus ortholog. Infect Immun 66: 4823-4831.
    • (1998) Infect Immun , vol.66 , pp. 4823-4831
    • Zuckert, W.R.1    Marquis, H.2    Goldfine, H.3


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