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Volumn 23, Issue 4, 1997, Pages 693-704

Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDOGLYCAN;

EID: 0031018135     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.2561621.x     Document Type: Article
Times cited : (66)

References (51)
  • 1
    • 0004058709 scopus 로고
    • New mass spectrometric methods for peptidoglycan analysis
    • de Pedro, M.A., Höltje, J.-V., and Löffelhardt, W. (eds). Plenum Press
    • Allmaier, G., and Schmid, E.R. (1993) New mass spectrometric methods for peptidoglycan analysis. In Bacterial Growth and Lysis: Metabolism and Structure of the Bacterial Sacculus. de Pedro, M.A., Höltje, J.-V., and Löffelhardt, W. (eds). Plenum Press, pp. 23-39.
    • (1993) Bacterial Growth and Lysis: Metabolism and Structure of the Bacterial Sacculus , pp. 23-39
    • Allmaier, G.1    Schmid, E.R.2
  • 2
    • 84990662760 scopus 로고
    • Optimization of sample deposition for plasma desorption mass spectrometry
    • Allmaier, G., Rodriguez, M.C., and Pittenauer, E. (1992) Optimization of sample deposition for plasma desorption mass spectrometry. Rapid Commun Mass Spectrom 6: 284-288.
    • (1992) Rapid Commun Mass Spectrom , vol.6 , pp. 284-288
    • Allmaier, G.1    Rodriguez, M.C.2    Pittenauer, E.3
  • 3
    • 0028931702 scopus 로고
    • Accurate molecular weight determination of the major surface layer protein isolated from Clostridium thermosaccharolyticum by time-of-flight mass spectrometry
    • Allmaier, G., Schäffer, C., Messner, P., Rapp, U., and Mayer-Posner, F.J. (1995) Accurate molecular weight determination of the major surface layer protein isolated from Clostridium thermosaccharolyticum by time-of-flight mass spectrometry. J Bacteriol 177: 1402-1404.
    • (1995) J Bacteriol , vol.177 , pp. 1402-1404
    • Allmaier, G.1    Schäffer, C.2    Messner, P.3    Rapp, U.4    Mayer-Posner, F.J.5
  • 4
    • 0026498184 scopus 로고
    • Salmonella typhimurium activates virulence gene transcription within acidified macrophage phagosomes
    • Alpuche-Aranda, C.M., Swanson, J.A., Loomis, W.P., and Miller, S.I. (1992) Salmonella typhimurium activates virulence gene transcription within acidified macrophage phagosomes. Proc Natl Acad Sci USA 89: 10079-10083.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10079-10083
    • Alpuche-Aranda, C.M.1    Swanson, J.A.2    Loomis, W.P.3    Miller, S.I.4
  • 5
    • 0027321773 scopus 로고
    • A structure-activity relationship for induction of meningeal inflammation by muramyl peptides
    • Burroughs, M., Rozdzinski, E., Geelen, S., and Tuomanen, E. (1993) A structure-activity relationship for induction of meningeal inflammation by muramyl peptides. J Clin Invest 92: 297-302.
    • (1993) J Clin Invest , vol.92 , pp. 297-302
    • Burroughs, M.1    Rozdzinski, E.2    Geelen, S.3    Tuomanen, E.4
  • 6
    • 0026795665 scopus 로고
    • Effect of D-amino acids on structure and synthesis of peptidoglycan in Escherichia coli
    • Caparrós, M., Pisabarro, A.G., and De Pedro, M.A. (1992) Effect of D-amino acids on structure and synthesis of peptidoglycan in Escherichia coli. J Bacteriol 174: 5549-5559.
    • (1992) J Bacteriol , vol.174 , pp. 5549-5559
    • Caparrós, M.1    Pisabarro, A.G.2    De Pedro, M.A.3
  • 7
    • 0027944667 scopus 로고
    • Molecular and cellular mechanisms of Salmonella pathogenesis
    • Finlay, B.B. (1994) Molecular and cellular mechanisms of Salmonella pathogenesis. Curr Top Microbiol Immunol 192: 163-185.
    • (1994) Curr Top Microbiol Immunol , vol.192 , pp. 163-185
    • Finlay, B.B.1
  • 8
    • 0030033212 scopus 로고
    • Molecular and cellular bases of Salmonella entry into non-phagocytic cells
    • Galán, J.E. (1995) Molecular and cellular bases of Salmonella entry into non-phagocytic cells. Curr Top Microbiol Immunol 209: 43-60.
    • (1995) Curr Top Microbiol Immunol , vol.209 , pp. 43-60
    • Galán, J.E.1
  • 9
    • 0029879556 scopus 로고    scopus 로고
    • Molecular genetic bases of Salmonella entry into host cells
    • Galán, J.E. (1996) Molecular genetic bases of Salmonella entry into host cells. Mol Microbiol 20: 263-271.
    • (1996) Mol Microbiol , vol.20 , pp. 263-271
    • Galán, J.E.1
  • 10
    • 0027250140 scopus 로고
    • Peptidoglycan synthesis in S. typhimurium 2616
    • Gally, D., and Cooper, S. (1993) Peptidoglycan synthesis in S. typhimurium 2616. J Gen Microbiol 139: 1469-1476.
    • (1993) J Gen Microbiol , vol.139 , pp. 1469-1476
    • Gally, D.1    Cooper, S.2
  • 11
    • 0024370481 scopus 로고
    • Lytic response of Escherichia coli cells to inhibitors of penicillin-binding proteins 1a and 1b as a timed event related to cell division
    • Garcia-del Portillo, F., de Pedro, M.A., Joseleau-Petit, D., and D'Ari, R. (1989) Lytic response of Escherichia coli cells to inhibitors of penicillin-binding proteins 1a and 1b as a timed event related to cell division. J Bacteriol 171: 4217-4221.
    • (1989) J Bacteriol , vol.171 , pp. 4217-4221
    • Garcia-del Portillo, F.1    De Pedro, M.A.2    Joseleau-Petit, D.3    D'Ari, R.4
  • 12
    • 0026441192 scopus 로고
    • Characterization of the micro-environment of Salmonella typhimurium-containing vacuoles in MDCK epithelial cells
    • Garcia-del Portillo, F., Foster, J.W., Maguire, M.E., and Finlay, B.B. (1992) Characterization of the micro-environment of Salmonella typhimurium-containing vacuoles in MDCK epithelial cells. Mol Microbiol 6: 3289-3297.
    • (1992) Mol Microbiol , vol.6 , pp. 3289-3297
    • Garcia-del Portillo, F.1    Foster, J.W.2    Maguire, M.E.3    Finlay, B.B.4
  • 13
    • 0027375512 scopus 로고
    • Salmonella induces the formation of filamentous structures containing lysosomal membrane glycoproteins in epithelial cells
    • Garcia-del Portillo, F., Zwick, M.B., Leung, K.Y., and Finlay, B.B. (1993) Salmonella induces the formation of filamentous structures containing lysosomal membrane glycoproteins in epithelial cells. Proc Natl Acad Sci USA 90: 10544-10548.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10544-10548
    • Garcia-del Portillo, F.1    Zwick, M.B.2    Leung, K.Y.3    Finlay, B.B.4
  • 14
    • 0031014146 scopus 로고    scopus 로고
    • Release of lipopolysaccharide from intracellular compartments containing Salmonella typhimurium to vesicles of the host epithelial cell
    • in press
    • Garcia-del Portillo, F., Stein, M., and Finlay, B.B. (1997) Release of lipopolysaccharide from intracellular compartments containing Salmonella typhimurium to vesicles of the host epithelial cell. Infect Immun 65: in press.
    • (1997) Infect Immun , vol.65
    • Garcia-del Portillo, F.1    Stein, M.2    Finlay, B.B.3
  • 15
    • 0029671310 scopus 로고    scopus 로고
    • 2+ as an extracellular signal: Environmental regulation of Salmonella virulence
    • 2+ as an extracellular signal: environmental regulation of Salmonella virulence. Cell 84: 165-174.
    • (1996) Cell , vol.84 , pp. 165-174
    • Garcia-Véscovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 16
    • 0842299014 scopus 로고
    • The analysis of murein composition with high-pressure-liquid-chromatography
    • Hakenbeck, R., Holtje, J.-V., and Labinschinski, H. (eds). Berlin: Walter de Gruyter
    • Glauner, B., and Schwarz, U. (1983) The analysis of murein composition with high-pressure-liquid-chromatography. In The Target of Penicillin. Hakenbeck, R., Holtje, J.-V., and Labinschinski, H. (eds). Berlin: Walter de Gruyter, pp. 29-34.
    • (1983) The Target of Penicillin , pp. 29-34
    • Glauner, B.1    Schwarz, U.2
  • 17
    • 0023677844 scopus 로고
    • The composition of the murein of Escherichia coli
    • Glauner, B., Höltje, J.-V., and Schwarz, U. (1988) The composition of the murein of Escherichia coli. J Biol Chem 263: 10088-10095.
    • (1988) J Biol Chem , vol.263 , pp. 10088-10095
    • Glauner, B.1    Höltje, J.-V.2    Schwarz, U.3
  • 18
    • 0021981840 scopus 로고
    • Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli
    • Goodell, E.W., and Higgins, C.F. (1987) Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli. J Bacteriol 162: 391-397.
    • (1987) J Bacteriol , vol.162 , pp. 391-397
    • Goodell, E.W.1    Higgins, C.F.2
  • 19
    • 0016708116 scopus 로고
    • Envelope-bound N-acetylmuramyl-L-alanine amidase of Escherichia coli K-12. Purification and properties of the enzyme
    • van Heijenoort, J, Parquet, C., Flouret, B., and van Heijenoort, Y. (1975) Envelope-bound N-acetylmuramyl-L-alanine amidase of Escherichia coli K-12. Purification and properties of the enzyme. Eur J Biochem 58: 611-619.
    • (1975) Eur J Biochem , vol.58 , pp. 611-619
    • Van Heijenoort, J.1    Parquet, C.2    Flouret, B.3    Van Heijenoort, Y.4
  • 20
    • 0029670071 scopus 로고    scopus 로고
    • Purification and characterization of N-acetylmuramyl-L-alanine amidase from human plasma using monoclonal antibodies
    • Hoijer, M.A., Melief, M.J., Keck, W., and Hazenberg, M.P. (1996) Purification and characterization of N-acetylmuramyl-L-alanine amidase from human plasma using monoclonal antibodies. Biochem Biophys Acta 1289: 57-64.
    • (1996) Biochem Biophys Acta , vol.1289 , pp. 57-64
    • Hoijer, M.A.1    Melief, M.J.2    Keck, W.3    Hazenberg, M.P.4
  • 21
    • 0019407618 scopus 로고
    • Aromatic-dependent Salmonella typhimurium are non-virulent and effective as live vaccines
    • Hoiseth, S.K., and Stocker, B.A. (1981) Aromatic-dependent Salmonella typhimurium are non-virulent and effective as live vaccines. Nature 291: 238-239.
    • (1981) Nature , vol.291 , pp. 238-239
    • Hoiseth, S.K.1    Stocker, B.A.2
  • 22
    • 0028168986 scopus 로고
    • The negative regulator of beta-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase
    • Höltje, J.V., Kopp, U., Ursinus, A., and Wiedemann, B. (1994) The negative regulator of beta-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase. FEMS Microbiol Lett 122: 159-164.
    • (1994) FEMS Microbiol Lett , vol.122 , pp. 159-164
    • Höltje, J.V.1    Kopp, U.2    Ursinus, A.3    Wiedemann, B.4
  • 23
    • 0027533303 scopus 로고
    • The Salmonella typhimurium nadC gene: Sequence determination by use of Mud-P22 and purification of quinolinate phosphoribosyltransferase
    • Hughes, K.T., Dessen, A., Gray, J.P., and Grubmeyer, C. (1993). The Salmonella typhimurium nadC gene: sequence determination by use of Mud-P22 and purification of quinolinate phosphoribosyltransferase. J Bacteriol 175: 479-486.
    • (1993) J Bacteriol , vol.175 , pp. 479-486
    • Hughes, K.T.1    Dessen, A.2    Gray, J.P.3    Grubmeyer, C.4
  • 24
    • 0028147092 scopus 로고
    • Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction
    • Jacobs, C., Huang, L.-J., Bartowsky, E., Normark, S., and Park, J.T. (1994) Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction. EMBO J 13: 4684-4694.
    • (1994) EMBO J , vol.13 , pp. 4684-4694
    • Jacobs, C.1    Huang, L.-J.2    Bartowsky, E.3    Normark, S.4    Park, J.T.5
  • 26
    • 0022497809 scopus 로고
    • Transglycosylase and endopeptidase participate in the degradation of murein during autolysis of Escherichia coli
    • Kitano, K., Tuomanen, E., and Tomasz, A. (1986) Transglycosylase and endopeptidase participate in the degradation of murein during autolysis of Escherichia coli. J Bacteriol 167: 759-765.
    • (1986) J Bacteriol , vol.167 , pp. 759-765
    • Kitano, K.1    Tuomanen, E.2    Tomasz, A.3
  • 27
    • 0025334009 scopus 로고
    • The ability of Salmonella to enter mammalian cells is affected by bacterial growth state
    • Lee, C., and Falkow, S. (1990) The ability of Salmonella to enter mammalian cells is affected by bacterial growth state. Proc Natl Acad Sci USA 87: 4304-4308.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4304-4308
    • Lee, C.1    Falkow, S.2
  • 28
    • 50449147866 scopus 로고
    • Transduction of linked genetic characters of the host by bacteriophage P1
    • Lennox, E.S. (1955) Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1: 190-206.
    • (1955) Virology , vol.1 , pp. 190-206
    • Lennox, E.S.1
  • 29
    • 0026345034 scopus 로고
    • Intracellular replication is essential for the virulence of Salmonella typhimurium
    • Leung, K.Y., and Finlay, B.B. (1991) Intracellular replication is essential for the virulence of Salmonella typhimurium. Proc Natl Acad Sci USA 88: 11470-11474.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11470-11474
    • Leung, K.Y.1    Finlay, B.B.2
  • 30
    • 0027499306 scopus 로고
    • Bordetella pertussis tracheal cytotoxin and other muramyl peptides: Distinct structure-activity relationships for respiratory epithelial cytopathology
    • Luker, K.E., Collier, J.L., Kolodziej, E.W., Marshall, G.R., and Goldman, W.E. (1993) Bordetella pertussis tracheal cytotoxin and other muramyl peptides: distinct structure-activity relationships for respiratory epithelial cytopathology. Proc Natl Acad Sci USA 90: 2365-2369.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2365-2369
    • Luker, K.E.1    Collier, J.L.2    Kolodziej, E.W.3    Marshall, G.R.4    Goldman, W.E.5
  • 31
    • 0029018206 scopus 로고
    • Tracheal cytotoxin structural requirements for respiratory epithelial damage in pertussis
    • Luker, K.E., Tyler, A.N., Marshall, G.R., and Goldman, W.E. (1995) Tracheal cytotoxin structural requirements for respiratory epithelial damage in pertussis. Mol Microbiol 16: 733-743.
    • (1995) Mol Microbiol , vol.16 , pp. 733-743
    • Luker, K.E.1    Tyler, A.N.2    Marshall, G.R.3    Goldman, W.E.4
  • 32
    • 0024470615 scopus 로고
    • Nucleotide sequence of the Salmonella typhimurium mutL gene required for mismatch repair: Homology of MutL to HexB of Streptococcus pneumoniae and to PMS1 of the yeast Saccharomyces cerevisiae
    • Mankovich, J.A., McIntyre, C.A., and Walker, G.C. (1989) Nucleotide sequence of the Salmonella typhimurium mutL gene required for mismatch repair: homology of MutL to HexB of Streptococcus pneumoniae and to PMS1 of the yeast Saccharomyces cerevisiae. J Bacteriol 171: 5325-5331.
    • (1989) J Bacteriol , vol.171 , pp. 5325-5331
    • Mankovich, J.A.1    McIntyre, C.A.2    Walker, G.C.3
  • 34
    • 0027516518 scopus 로고
    • Peptidoglycan tripeptide and cross-linking are altered in Enterobacter cloacae induced to produce AmpC β-lactamase by glycine and D-amino acids
    • Ottolenghi, A.C., Caparrós, M., and de Pedro, M.A. (1993) Peptidoglycan tripeptide and cross-linking are altered in Enterobacter cloacae induced to produce AmpC β-lactamase by glycine and D-amino acids. J Bacteriol 175: 1537-1542.
    • (1993) J Bacteriol , vol.175 , pp. 1537-1542
    • Ottolenghi, A.C.1    Caparrós, M.2    De Pedro, M.A.3
  • 35
    • 0027514558 scopus 로고
    • Turnover and recycling of the murein sacculus in oligopeptide permease-negative strains of Escherichia coli: Indirect evidence for an alternative permease system and for a monolayered sacculus
    • Park, J.T. (1993) Turnover and recycling of the murein sacculus in oligopeptide permease-negative strains of Escherichia coli: indirect evidence for an alternative permease system and for a monolayered sacculus. J Bacteriol 175: 7-11.
    • (1993) J Bacteriol , vol.175 , pp. 7-11
    • Park, J.T.1
  • 36
    • 0029154488 scopus 로고
    • Why does Escherichia coli recycle its cell wall peptides?
    • Park, J.T. (1995) Why does Escherichia coli recycle its cell wall peptides? Mol Microbiol 17: 421-426.
    • (1995) Mol Microbiol , vol.17 , pp. 421-426
    • Park, J.T.1
  • 39
    • 0021944190 scopus 로고
    • Structural modifications in the peptidoglycan of Escherichia coli associated with the state of growth of the culture
    • Pisabarro, A.G., de Pedro, M.A., and Vázquez, D. (1985) Structural modifications in the peptidoglycan of Escherichia coli associated with the state of growth of the culture. J Bacteriol 161: 238-242.
    • (1985) J Bacteriol , vol.161 , pp. 238-242
    • Pisabarro, A.G.1    De Pedro, M.A.2    Vázquez, D.3
  • 40
    • 0024397723 scopus 로고
    • Normal growth and division of Escherichia coli with a reduced amount of murein
    • Prats, R., and de Pedro, M.A. (1989) Normal growth and division of Escherichia coli with a reduced amount of murein. J Bacteriol 171: 3740-3745.
    • (1989) J Bacteriol , vol.171 , pp. 3740-3745
    • Prats, R.1    De Pedro, M.A.2
  • 41
    • 0028878573 scopus 로고
    • Variability of peptidoglycan structural parameters in Gramnegative bacteria
    • Quintela, J.C., Caparrós, M., and de Pedro, M.A (1995a) Variability of peptidoglycan structural parameters in Gramnegative bacteria. FEMS Microbiol Lett 125: 95-100.
    • (1995) FEMS Microbiol Lett , vol.125 , pp. 95-100
    • Quintela, J.C.1    Caparrós, M.2    De Pedro, M.A.3
  • 43
    • 0029994912 scopus 로고    scopus 로고
    • Acidification of phagosomes containing Salmonella typhimurium in murine macrophages
    • Rathman, M., Sjaastad, M.D., and Falkow, S. (1996) Acidification of phagosomes containing Salmonella typhimurium in murine macrophages. Infect Immun 64: 2765-2773.
    • (1996) Infect Immun , vol.64 , pp. 2765-2773
    • Rathman, M.1    Sjaastad, M.D.2    Falkow, S.3
  • 44
    • 77956866741 scopus 로고
    • Microbial peptidoglycan (murein) hydrolases
    • Ghuysen, J.-M., and Hakenbeck, R. (eds). Amsterdam: Elsevier Science Publisher BV
    • Shockman, G.D., and Höltje, J.-V. (1994) Microbial peptidoglycan (murein) hydrolases. In Bacterial Cell Wall. Ghuysen, J.-M., and Hakenbeck, R. (eds). Amsterdam: Elsevier Science Publisher BV, pp. 131-166.
    • (1994) Bacterial Cell Wall , pp. 131-166
    • Shockman, G.D.1    Höltje, J.-V.2
  • 45
    • 0020559318 scopus 로고
    • Mutation of the N-acetylmuramyl-L-alanine amidase gene of Escherichia coli K-12
    • Tomioka, S., Nikaido, T., Miyakawa, T., and Matsuhashi, M. (1983) Mutation of the N-acetylmuramyl-L-alanine amidase gene of Escherichia coli K-12. J Bacteriol 156: 436-465.
    • (1983) J Bacteriol , vol.156 , pp. 436-465
    • Tomioka, S.1    Nikaido, T.2    Miyakawa, T.3    Matsuhashi, M.4
  • 46
    • 0028107485 scopus 로고
    • Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEM13 mutant
    • Troup, B., Jahn, M., Hungerer, C., and Jahn, D. (1994) Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEM13 mutant. J Bacteriol 176: 673-680.
    • (1994) J Bacteriol , vol.176 , pp. 673-680
    • Troup, B.1    Jahn, M.2    Hungerer, C.3    Jahn, D.4
  • 47
    • 0028228191 scopus 로고
    • The mutL gene of Escherichia coli K-12 forms a superoperon with a gene encoding a new cell-wall amidase
    • Tsui, H.C., Zhao, G., Feng, G., Leung, H.C., and Winkler, M.E. (1994) The mutL gene of Escherichia coli K-12 forms a superoperon with a gene encoding a new cell-wall amidase. Mol Microbiol 11: 189-202.
    • (1994) Mol Microbiol , vol.11 , pp. 189-202
    • Tsui, H.C.1    Zhao, G.2    Feng, G.3    Leung, H.C.4    Winkler, M.E.5
  • 49
    • 0028949862 scopus 로고
    • The human and mammalian N-acetylmuramyl-L-alanine amidase: Distribution, action on different bacterial peptidoglycans, and comparison with the human lysozyme activities
    • Vanderwinkel, E., De Pauw, P., Philipp, D., Ten Have, J.-P., and Bainter, K. (1995) The human and mammalian N-acetylmuramyl-L-alanine amidase: distribution, action on different bacterial peptidoglycans, and comparison with the human lysozyme activities. Biochem Mol Med 54: 26-32.
    • (1995) Biochem Mol Med , vol.54 , pp. 26-32
    • Vanderwinkel, E.1    De Pauw, P.2    Philipp, D.3    Ten Have, J.-P.4    Bainter, K.5
  • 50
    • 0000094029 scopus 로고
    • Improved resolution of very high sensitivity in MALDI TOF of matrix surfaces made by fast evaporation
    • Vorm, O., Roepstorff, P., and Mann, M. (1994) Improved resolution of very high sensitivity in MALDI TOF of matrix surfaces made by fast evaporation. Anal Chem 66: 3281-3287.
    • (1994) Anal Chem , vol.66 , pp. 3281-3287
    • Vorm, O.1    Roepstorff, P.2    Mann, M.3
  • 51
    • 0027205487 scopus 로고
    • An oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium
    • Xu, K. and Elliott, T. (1993) An oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium. J Bacteriol 175: 4990-4999.
    • (1993) J Bacteriol , vol.175 , pp. 4990-4999
    • Xu, K.1    Elliott, T.2


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