메뉴 건너뛰기




Volumn 68, Issue 12, 2000, Pages 7069-7077

OppA of listeria monocytogenes, an oligopeptide-binding protein required for bacterial growth at low temperature and involved in intracellular survival

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; GENE PRODUCT; OLIGOPEPTIDE; PERMEASE;

EID: 0034441194     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.68.12.7069-7077.2000     Document Type: Article
Times cited : (170)

References (45)
  • 1
    • 0028893914 scopus 로고
    • The role of peptide metabolism in the growth of Listeria monocytogenes ATCC 23074 at high osmolarity
    • Amezaga, M. R., I. Davidson. D. McLaggan, A. Verheul, T. Abee, and I. R. Booth. 1995. The role of peptide metabolism in the growth of Listeria monocytogenes ATCC 23074 at high osmolarity. Microbiology 141:41-49.
    • (1995) Microbiology , vol.141 , pp. 41-49
    • Amezaga, M.R.1    Davidson, I.2    McLaggan, D.3    Verheul, A.4    Abee, T.5    Booth, I.R.6
  • 2
    • 0034062054 scopus 로고    scopus 로고
    • Osmoprotectants and cryoprotectants for Listeria monocytogenes
    • Bayles, D. O., and B. J. Wilkinson. 2000. Osmoprotectants and cryoprotectants for Listeria monocytogenes. Lett. Appl. Microbiol. 30:23-27.
    • (2000) Lett. Appl. Microbiol. , vol.30 , pp. 23-27
    • Bayles, D.O.1    Wilkinson, B.J.2
  • 3
    • 0033818945 scopus 로고    scopus 로고
    • Identification in Listeria monocytogenes of MecA, a homologue of the Bacillus subtilis competence regulatory protein
    • Borezée, E., T. Msadek, L. Durant, and P. Berche. 2000. Identification in Listeria monocytogenes of MecA, a homologue of the Bacillus subtilis competence regulatory protein. J. Bacteriol. 182:5931-5934.
    • (2000) J. Bacteriol. , vol.182 , pp. 5931-5934
    • Borezée, E.1    Msadek, T.2    Durant, L.3    Berche, P.4
  • 4
    • 0031921950 scopus 로고    scopus 로고
    • Circularization of Tn916 is required for expression of the transposon-encoded transfer functions: Characterization of long tetracycline-inducible transcripts reading through the attachment site
    • Celli, J., and P. Trieu-Cuot. 1998. Circularization of Tn916 is required for expression of the transposon-encoded transfer functions: characterization of long tetracycline-inducible transcripts reading through the attachment site. Mol. Microbiol. 28:103-117.
    • (1998) Mol. Microbiol. , vol.28 , pp. 103-117
    • Celli, J.1    Trieu-Cuot, P.2
  • 6
    • 0029042013 scopus 로고
    • Peptide permeases from Streptococcus pneumoniae affect adherence to eucaryotic cells
    • Cundell, D. R., B. J. Pearce, J. Sandros, A. M. Naughton, and H. R. Masure. 1995. Peptide permeases from Streptococcus pneumoniae affect adherence to eucaryotic cells. Infect. Immun. 63:2493-2498.
    • (1995) Infect. Immun. , vol.63 , pp. 2493-2498
    • Cundell, D.R.1    Pearce, B.J.2    Sandros, J.3    Naughton, A.M.4    Masure, H.R.5
  • 7
    • 0033982985 scopus 로고    scopus 로고
    • Role of group A streptococcal virulence factors in adherence to keratinocytes
    • Darmstadt, G. L., L. Mentele, A. Podbielski, and C. E. Rubens. 2000. Role of group A streptococcal virulence factors in adherence to keratinocytes. Infect. Immun. 68:1215-1221.
    • (2000) Infect. Immun. , vol.68 , pp. 1215-1221
    • Darmstadt, G.L.1    Mentele, L.2    Podbielski, A.3    Rubens, C.E.4
  • 8
    • 0028008788 scopus 로고
    • Fate of Listeria monocytogenes in murine macrophages: Evidence for simultaneous killing and survival of intracellular bacteria
    • de Chastellier, C., and P. Berche. 1994. Fate of Listeria monocytogenes in murine macrophages: evidence for simultaneous killing and survival of intracellular bacteria. Infect. Immun. 62:543-553.
    • (1994) Infect. Immun. , vol.62 , pp. 543-553
    • De Chastellier, C.1    Berche, P.2
  • 9
    • 0032564324 scopus 로고    scopus 로고
    • Kinetics and specificity of peptide uptake by the oligopeptide transport system of Lactococcus lactis
    • Detmers, F. J., E. R. Kunji. F. C. Lanfermeijer, B. Poolman, and W. N. Konings. 1998. Kinetics and specificity of peptide uptake by the oligopeptide transport system of Lactococcus lactis. Biochemistry 37:16671-16679.
    • (1998) Biochemistry , vol.37 , pp. 16671-16679
    • Detmers, F.J.1    Kunji, E.R.2    Lanfermeijer, F.C.3    Poolman, B.4    Konings, W.N.5
  • 10
    • 0025951915 scopus 로고
    • Listeria monocytogenes, a food-borne pathogen
    • Erratum, 55:752
    • Farber, J. M., and P. I. Peterkin. 1991. Listeria monocytogenes, a food-borne pathogen. Microbiol. Rev. 55:476-511. (Erratum, 55:752.)
    • (1991) Microbiol. Rev. , vol.55 , pp. 476-511
    • Farber, J.M.1    Peterkin, P.I.2
  • 11
    • 0011542909 scopus 로고
    • Indigenous enzymes in milk-proteinases
    • P. F. Fox (ed.). Elsevier, London, United Kingdom
    • Fox, P. F. 1992. Indigenous enzymes in milk-proteinases, p. 310-321. In P. F. Fox (ed.). Advanced dairy chemistry, vol. 1. Proteins. Elsevier, London, United Kingdom.
    • (1992) Advanced Dairy Chemistry, Vol. 1. Proteins , vol.1 , pp. 310-321
    • Fox, P.F.1
  • 12
    • 0034103357 scopus 로고    scopus 로고
    • The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes
    • Gaillot, O., E. Pellegrini, S. Bregenholt, S. Nair, and P. Berche. 2000. The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes. Mol. Microbiol. 35:1286-1294.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1286-1294
    • Gaillot, O.1    Pellegrini, E.2    Bregenholt, S.3    Nair, S.4    Berche, P.5
  • 13
    • 0029858776 scopus 로고    scopus 로고
    • Sodium-driven, osmotically activated glycine betaine transport in Listeria monocytogenes membrane vesicles
    • Gerhardt, P. N., L. T. Smith, and G. M. Smith. 1996. Sodium-driven, osmotically activated glycine betaine transport in Listeria monocytogenes membrane vesicles. J. Bacteriol. 178:6105-6109.
    • (1996) J. Bacteriol. , vol.178 , pp. 6105-6109
    • Gerhardt, P.N.1    Smith, L.T.2    Smith, G.M.3
  • 14
    • 0034004726 scopus 로고    scopus 로고
    • Osmotic and chill activation of glycine betaine porter II in Listeria monocytogenes membrane vesicles
    • Gerhardt, P. N., L. Tombras Smith, and G. M. Smith. 2000. Osmotic and chill activation of glycine betaine porter II in Listeria monocytogenes membrane vesicles. J. Bacteriol. 182:2544-2550.
    • (2000) J. Bacteriol. , vol.182 , pp. 2544-2550
    • Gerhardt, P.N.1    Tombras Smith, L.2    Smith, G.M.3
  • 15
    • 0023636673 scopus 로고
    • Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli
    • Goodell, E. W., and C. F. Higgins. 1987. Uptake of cell wall peptides by Salmonella typhimurium and Escherichia coli. J. Bacteriol. 169:3861-3865.
    • (1987) J. Bacteriol. , vol.169 , pp. 3861-3865
    • Goodell, E.W.1    Higgins, C.F.2
  • 16
    • 0013922015 scopus 로고
    • Listeria monocytogenes and listeric infections
    • Gray, M. L., and A. H. Killinger. 1966. Listeria monocytogenes and listeric infections. Bacteriol. Rev. 30:309-382.
    • (1966) Bacteriol. Rev. , vol.30 , pp. 309-382
    • Gray, M.L.1    Killinger, A.H.2
  • 17
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. 1992. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 18
    • 0022558554 scopus 로고
    • Peptide transport in bacteria
    • Higgins, C. F., and M. M. Gibson. 1986. Peptide transport in bacteria. Methods Enzymol. 125:365-377.
    • (1986) Methods Enzymol. , vol.125 , pp. 365-377
    • Higgins, C.F.1    Gibson, M.M.2
  • 19
    • 0023644827 scopus 로고
    • Molecular characterization of the oligopeptide permease of Salmonella typhimurium
    • Hiles, I. D., M. P. Gallagher, D. J. Jamieson, and C. F. Higgins. 1987 Molecular characterization of the oligopeptide permease of Salmonella typhimurium. J. Mol. Biol. 195:125-142.
    • (1987) J. Mol. Biol. , vol.195 , pp. 125-142
    • Hiles, I.D.1    Gallagher, M.P.2    Jamieson, D.J.3    Higgins, C.F.4
  • 20
    • 0023152853 scopus 로고
    • Peptide transport in Salmonella typhimurium: Molecular cloning and characterization of the oligopeptide permease genes
    • Hiles, I. D., L. M. Powell, and C. F. Higgins. 1987. Peptide transport in Salmonella typhimurium: molecular cloning and characterization of the oligopeptide permease genes. Mol. Gen. Genet. 206:101-109.
    • (1987) Mol. Gen. Genet. , vol.206 , pp. 101-109
    • Hiles, I.D.1    Powell, L.M.2    Higgins, C.F.3
  • 21
    • 0032828415 scopus 로고    scopus 로고
    • Identification of an ATP-driven, osmoregulated glycine betaine transport system in Listeria monocytogenes
    • Ko, R., and L. T. Smith. 1999. Identification of an ATP-driven, osmoregulated glycine betaine transport system in Listeria monocytogenes. Appl. Environ. Microbiol. 65:4040-4048.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4040-4048
    • Ko, R.1    Smith, L.T.2
  • 22
    • 0028157327 scopus 로고
    • Glycine hetaine confers enhanced osmotolerance and cryotolerance on Listeria monocytogenes
    • Ko, R., L. T. Smith, and G. M. Smith. 1994. Glycine hetaine confers enhanced osmotolerance and cryotolerance on Listeria monocytogenes. J. Bacteriol. 176:426-431.
    • (1994) J. Bacteriol. , vol.176 , pp. 426-431
    • Ko, R.1    Smith, L.T.2    Smith, G.M.3
  • 23
    • 0026515440 scopus 로고
    • L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein
    • Kocks, C., E. Gouin, M. Tabouret, P. Berche, H. Ohayon, and P. Cossart. 1992. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68:521-531.
    • (1992) Cell , vol.68 , pp. 521-531
    • Kocks, C.1    Gouin, E.2    Tabouret, M.3    Berche, P.4    Ohayon, H.5    Cossart, P.6
  • 25
    • 0030044159 scopus 로고    scopus 로고
    • Enterococcus faecalis pheromone binding protein, PrgZ, recruits a chromosomal oligopeptide permease system to import sex pheromone cCF10 for induction of conjugation
    • Leonard, B. A., A. Podbielski, P. J. Hedberg, and G. M. Dunny. 1996 Enterococcus faecalis pheromone binding protein, PrgZ, recruits a chromosomal oligopeptide permease system to import sex pheromone cCF10 for induction of conjugation. Proc. Natl. Acad. Sci. USA 93:260-264.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 260-264
    • Leonard, B.A.1    Podbielski, A.2    Hedberg, P.J.3    Dunny, G.M.4
  • 26
    • 0022474926 scopus 로고
    • Peptide chemotaxis in E. coli involves the Tap signal transducer and the dipeptide permease
    • Manson, M. D., V. Blank, G. Brade, and C. F. Higgins. 1986. Peptide chemotaxis in E. coli involves the Tap signal transducer and the dipeptide permease. Nature 321:253-256.
    • (1986) Nature , vol.321 , pp. 253-256
    • Manson, M.D.1    Blank, V.2    Brade, G.3    Higgins, C.F.4
  • 27
    • 0027214122 scopus 로고
    • Intracytoplasmic growth and virulence of Listeria monocytogenes auxotrophic mutants
    • Marquis, H., H. G. Bouwer, D. J. Hinrichs, and D. A. Portnoy. 1993. Intracytoplasmic growth and virulence of Listeria monocytogenes auxotrophic mutants. Infect. Immun. 61:3756-3760.
    • (1993) Infect. Immun. , vol.61 , pp. 3756-3760
    • Marquis, H.1    Bouwer, H.G.2    Hinrichs, D.J.3    Portnoy, D.A.4
  • 28
    • 0027244956 scopus 로고
    • Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells
    • Menard, R., P. J. Sansonetti, and C. Parsot. 1993. Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells. J. Bacteriol. 175:5899-5906.
    • (1993) J. Bacteriol. , vol.175 , pp. 5899-5906
    • Menard, R.1    Sansonetti, P.J.2    Parsot, C.3
  • 29
    • 0032920682 scopus 로고    scopus 로고
    • ClpE, a novel member of the HSP100 family, is involved in cell division and virulence of Listeria monocytogenes
    • Nair, S., C. Frehel, L. Nguyen, V. Escuyer, and P. Berche. 1999. ClpE, a novel member of the HSP100 family, is involved in cell division and virulence of Listeria monocytogenes. Mol. Microbiol. 31:185-196.
    • (1999) Mol. Microbiol. , vol.31 , pp. 185-196
    • Nair, S.1    Frehel, C.2    Nguyen, L.3    Escuyer, V.4    Berche, P.5
  • 30
    • 0028294944 scopus 로고
    • Peptide transport by micro-organisms
    • Payne, J. W., and M. W. Smith. 1994. Peptide transport by micro-organisms. Adv. Microb. Physiol. 36:1-80.
    • (1994) Adv. Microb. Physiol. , vol.36 , pp. 1-80
    • Payne, J.W.1    Smith, M.W.2
  • 31
    • 0026031219 scopus 로고
    • The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation
    • Perego, M., C. F. Higgins, S. R. Pearce, M. P. Gallagher, and J. A. Hoch. 1991. The oligopeptide transport system of Bacillus subtilis plays a role in the initiation of sporulation. Mol. Microbiol. 5:173-185.
    • (1991) Mol. Microbiol. , vol.5 , pp. 173-185
    • Perego, M.1    Higgins, C.F.2    Pearce, S.R.3    Gallagher, M.P.4    Hoch, J.A.5
  • 32
    • 0029798285 scopus 로고    scopus 로고
    • Molecular characterization of group A streptococcal (GAS) oligopeptide permease (opp) and its effect on cysteine protease production
    • Podbielski, A., B. Pohl, M. Woischnik, C. Korner, K. H. Schmidt, E. Rozdzinski, and B. A. Leonard. 1996. Molecular characterization of group A streptococcal (GAS) oligopeptide permease (opp) and its effect on cysteine protease production. Mol. Microbiol. 21:1087-1099.
    • (1996) Mol. Microbiol. , vol.21 , pp. 1087-1099
    • Podbielski, A.1    Pohl, B.2    Woischnik, M.3    Korner, C.4    Schmidt, K.H.5    Rozdzinski, E.6    Leonard, B.A.7
  • 33
    • 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., E. Abachin, I. Razafimanantsoa, and P. Berche. 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
  • 34
    • 0025953961 scopus 로고
    • Development of an improved chemically defined minimal medium for Listeria monocytogenes
    • Premaratne, R. J., W. J. Lin, and E. A. Johnson. 1991. Development of an improved chemically defined minimal medium for Listeria monocytogenes. Appl. Environ. Microbiol. 57:3046-3048.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 3046-3048
    • Premaratne, R.J.1    Lin, W.J.2    Johnson, E.A.3
  • 36
    • 0025971265 scopus 로고
    • The spoOK locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence
    • Rudner, D. Z., J. R. LeDeaux, K. Ireton, and A. D. Grossman. 1991. The spoOK locus of Bacillus subtilis is homologous to the oligopeptide permease locus and is required for sporulation and competence. J. Bacteriol. 173:1388-1398.
    • (1991) J. Bacteriol. , vol.173 , pp. 1388-1398
    • Rudner, D.Z.1    LeDeaux, J.R.2    Ireton, K.3    Grossman, A.D.4
  • 38
    • 0029830022 scopus 로고    scopus 로고
    • Role of osmolytes in adaptation of osmotically stressed and chill-stressed Listeria monocytogenes grown in liquid media and on processed meat surfaces
    • Smith, L. T. 1996. Role of osmolytes in adaptation of osmotically stressed and chill-stressed Listeria monocytogenes grown in liquid media and on processed meat surfaces. Appl. Environ. Microbiol. 62:3088-3093.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3088-3093
    • Smith, L.T.1
  • 39
    • 0028951976 scopus 로고
    • Convergent sensing pathways mediate response to two extracellular competence factors in Bacillus subtilis
    • Solomon, J. M., R. Magnuson, A. Srivastava, and A. D. Grossman. 1995. Convergent sensing pathways mediate response to two extracellular competence factors in Bacillus subtilis. Genes Dev. 9:547-558.
    • (1995) Genes Dev. , vol.9 , pp. 547-558
    • Solomon, J.M.1    Magnuson, R.2    Srivastava, A.3    Grossman, A.D.4
  • 40
    • 0000601778 scopus 로고
    • Proteolytic enzymes of starter bacteria
    • Thomas, T. D., and O. E. Mills. 1981. Proteolytic enzymes of starter bacteria. Neth. Milk Dairy J. 35:255-273.
    • (1981) Neth. Milk Dairy J. , vol.35 , pp. 255-273
    • Thomas, T.D.1    Mills, O.E.2
  • 41
    • 0025861975 scopus 로고
    • Shuttle vectors containing a multiple cloning site and a lacZ alpha gene for conjugal transfer of DNA from Escherichia coli to gram-positive bacteria
    • Trieu-Cuot, P., C. Carlier, C. Poyart-Salmeron, and P. Courvalin. 1991. Shuttle vectors containing a multiple cloning site and a lacZ alpha gene for conjugal transfer of DNA from Escherichia coli to gram-positive bacteria. Gene 102:99-104.
    • (1991) Gene , vol.102 , pp. 99-104
    • Trieu-Cuot, P.1    Carlier, C.2    Poyart-Salmeron, C.3    Courvalin, P.4
  • 42
    • 0028872386 scopus 로고
    • A di-and tripeptide transport system can supply Listeria monocytogenes Scott A with amino acids essential for growth
    • Verheul, A., A. Hagting, M. R. Amezaga, I. R. Booth, F. M. Rombouts, and T. Abee. 1995. A di-and tripeptide transport system can supply Listeria monocytogenes Scott A with amino acids essential for growth. Appl. Environ. Microhiol. 61:225-233.
    • (1995) Appl. Environ. Microhiol. , vol.61 , pp. 225-233
    • Verheul, A.1    Hagting, A.2    Amezaga, M.R.3    Booth, I.R.4    Rombouts, F.M.5    Abee, T.6
  • 43
    • 0031932856 scopus 로고    scopus 로고
    • Utilization of oligopeptides by Listeria monocytogenes Scott A
    • Verheul, A., F. M. Rombouts, and T. Abee. 1998. Utilization of oligopeptides by Listeria monocytogenes Scott A. Appl. Environ. Microbiol. 64:1059-1065.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1059-1065
    • Verheul, A.1    Rombouts, F.M.2    Abee, T.3
  • 44
    • 0022343971 scopus 로고
    • Cloning and expression of the Listeria monocytogenes haemolysin in E. coli
    • Vicente, M. F., F. Baquero, and J. C. Perez-Diaz. 1985. Cloning and expression of the Listeria monocytogenes haemolysin in E. coli. FEMS Microhiol. Lett. 30:77-79.
    • (1985) FEMS Microhiol. Lett. , vol.30 , pp. 77-79
    • Vicente, M.F.1    Baquero, F.2    Perez-Diaz, J.C.3
  • 45
    • 0025349411 scopus 로고
    • Growth of Listeria monocytogenes at refrigeration temperatures
    • Walker, S. J., P. Archer, and J. G. Banks. 1990. Growth of Listeria monocytogenes at refrigeration temperatures. J. Appl. Bacteriol. 68:157-162.
    • (1990) J. Appl. Bacteriol. , vol.68 , pp. 157-162
    • Walker, S.J.1    Archer, P.2    Banks, J.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.