메뉴 건너뛰기




Volumn 183, Issue 2, 1996, Pages 621-629

Lipoprotein e(P4) is essential for hemin uptake by Haemophilus influenzae

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BETA LACTAMASE; BINDING PROTEIN; CYTOCHROME C3; EDETIC ACID; HEMIN; HEMOGLOBIN; LIPOPROTEIN; LIPOPROTEIN E(P4); NICOTINAMIDE ADENINE DINUCLEOTIDE; OUTER MEMBRANE PROTEIN; PROTOPORPHYRIN; UNCLASSIFIED DRUG;

EID: 0030046924     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.183.2.621     Document Type: Article
Times cited : (59)

References (50)
  • 1
    • 0025860730 scopus 로고
    • Haemophilus influenzae disease and immunization in developing countries
    • Funkhouser, A., M.C. Steinhoff, and J. Ward. 1991. Haemophilus influenzae disease and immunization in developing countries. Rev. Infect. Dis. 13:542-554.
    • (1991) Rev. Infect. Dis. , vol.13 , pp. 542-554
    • Funkhouser, A.1    Steinhoff, M.C.2    Ward, J.3
  • 2
    • 0021235776 scopus 로고
    • The pathogenicity of Haemophilus influenzae
    • Turk, D.C. 1984. The pathogenicity of Haemophilus influenzae. J. Med. Microbiol. 18:1-16.
    • (1984) J. Med. Microbiol. , vol.18 , pp. 1-16
    • Turk, D.C.1
  • 3
    • 0016162606 scopus 로고
    • Hemin and nicotinamide adenine dinucleotide requirements of Haemophilus influenzae
    • Evans, N.M., D.D. Smith, and A.J. Wicken. 1974. Hemin and nicotinamide adenine dinucleotide requirements of Haemophilus influenzae. J. Med. Microbiol. 7:359-365.
    • (1974) J. Med. Microbiol. , vol.7 , pp. 359-365
    • Evans, N.M.1    Smith, D.D.2    Wicken, A.J.3
  • 4
    • 0001897732 scopus 로고
    • The porphyrin requirements of Haemophilus influenzae and some functions of the vinyl and propionic acid chains of heme
    • Granick, S., and H. Gilder. 1946. The porphyrin requirements of Haemophilus influenzae and some functions of the vinyl and propionic acid chains of heme. J. Gen. Physiol 30:1-13.
    • (1946) J. Gen. Physiol , vol.30 , pp. 1-13
    • Granick, S.1    Gilder, H.2
  • 5
    • 0001307325 scopus 로고
    • Hemin biosynthesis in Haemophilus
    • White, D.C., and S. Granick. 1963. Hemin biosynthesis in Haemophilus. J. Bacteriol. 85:842-850.
    • (1963) J. Bacteriol. , vol.85 , pp. 842-850
    • White, D.C.1    Granick, S.2
  • 6
    • 0027998545 scopus 로고
    • Identification of a locus involved in the utilization of iron by Haemophilus influenzae
    • Sanders, J.D., L.D. Cope, and E.J. Hansen. 1994. Identification of a locus involved in the utilization of iron by Haemophilus influenzae. Infect. Immun. 62:4515-4525.
    • (1994) Infect. Immun. , vol.62 , pp. 4515-4525
    • Sanders, J.D.1    Cope, L.D.2    Hansen, E.J.3
  • 7
    • 0026716387 scopus 로고
    • Iron acquisition in Haemophilus influenzae: Receptor for human transferrin
    • Schryvers, A.B., and S. Gray-Owen. 1992. Iron acquisition in Haemophilus influenzae: receptor for human transferrin. J. Infect. Dis. 165:103-104.
    • (1992) J. Infect. Dis. , vol.165 , pp. 103-104
    • Schryvers, A.B.1    Gray-Owen, S.2
  • 8
    • 0028958297 scopus 로고
    • Identification and characterization of genes encoding the human transferrin-binding proteins from Haemophilus influenzae
    • Gray-Owen, S.D., S. Loosmore, and A.B. Schryvers. 1995. Identification and characterization of genes encoding the human transferrin-binding proteins from Haemophilus influenzae. Infect. Immun. 63:1201-1210.
    • (1995) Infect. Immun. , vol.63 , pp. 1201-1210
    • Gray-Owen, S.D.1    Loosmore, S.2    Schryvers, A.B.3
  • 9
    • 0029044848 scopus 로고
    • A gene cluster involved in the utilization of both free heme and heme:hemopexin by Haemophilus influenzae type b
    • Cope, L.D., R. Yogev, U. Muller-Eberhard, and E.J. Hansen. 1995. A gene cluster involved in the utilization of both free heme and heme:hemopexin by Haemophilus influenzae type b. J. Bacteriol. 377:2644-2653.
    • (1995) J. Bacteriol. , vol.377 , pp. 2644-2653
    • Cope, L.D.1    Yogev, R.2    Muller-Eberhard, U.3    Hansen, E.J.4
  • 10
    • 0026599032 scopus 로고
    • Identification of a genetic locus of Haemophilus influenzae type b necessary for the binding and utilization of heme bound to human hemopexin
    • Hanson, M.S., S.E. Pelzel, J. Larimer, U. Muller-Eberhard, and E.J. Hansen. 1992. Identification of a genetic locus of Haemophilus influenzae type b necessary for the binding and utilization of heme bound to human hemopexin. Proc. Natl. Acad. Sci. USA. 89:1973-1977.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1973-1977
    • Hanson, M.S.1    Pelzel, S.E.2    Larimer, J.3    Muller-Eberhard, U.4    Hansen, E.J.5
  • 11
    • 0029005376 scopus 로고
    • Affinity, conservation, and surface exposure of hemopexin-binding proteins in Haemophilus influenzae
    • Wong, J.C.Y., R. Patel, D. Kendall, P.W. Whitby, A. Smith, J. Holland, and P. Williams. 1995. Affinity, conservation, and surface exposure of hemopexin-binding proteins in Haemophilus influenzae Infect. Immun. 63:2327-2333
    • (1995) Infect. Immun. , vol.63 , pp. 2327-2333
    • Wong, J.C.Y.1    Patel, R.2    Kendall, D.3    Whitby, P.W.4    Smith, A.5    Holland, J.6    Williams, P.7
  • 13
    • 0028905674 scopus 로고
    • Identification and purification of a conserved heme-regulated hemoglobin-binding outer membrane protein from Haemophilus ducreyi
    • Elkins, C. 1995. Identification and purification of a conserved heme-regulated hemoglobin-binding outer membrane protein from Haemophilus ducreyi. Infect. Immun. 63:1241-1245.
    • (1995) Infect. Immun. , vol.63 , pp. 1241-1245
    • Elkins, C.1
  • 14
    • 0029061591 scopus 로고
    • Characterization of the hgbA locus encoding a hemoglobin receptor from Haemophilus ducreyi
    • Elkins, C., C.J. Chen, and C.E. Thomas. 1995. Characterization of the hgbA locus encoding a hemoglobin receptor from Haemophilus ducreyi. Infect. Immun. 63:2194-2200.
    • (1995) Infect. Immun. , vol.63 , pp. 2194-2200
    • Elkins, C.1    Chen, C.J.2    Thomas, C.E.3
  • 15
    • 0026535997 scopus 로고
    • Isolation of an outer membrane hemin-binding protein of Haemophilus influenzae type b
    • Lee, B.C. 1992. Isolation of an outer membrane hemin-binding protein of Haemophilus influenzae type b. Infect. Immun. 60:810-816.
    • (1992) Infect. Immun. , vol.60 , pp. 810-816
    • Lee, B.C.1
  • 16
    • 0026629422 scopus 로고
    • The hbpA gene of Haemophilus influenzae type b encodes a hemebinding lipoprotein conserved among heme-dependent Haemophilus species
    • Hanson, M.S., C. Slaughter, and E.J. Hansen. 1992. The hbpA gene of Haemophilus influenzae type b encodes a hemebinding lipoprotein conserved among heme-dependent Haemophilus species. Infect. Immun. 60:2257-2266.
    • (1992) Infect. Immun. , vol.60 , pp. 2257-2266
    • Hanson, M.S.1    Slaughter, C.2    Hansen, E.J.3
  • 17
    • 0025866724 scopus 로고
    • The e (P4) outer membrane protein of Haemophilus influenzae: Biologic activity of anti-e serum and cloning and sequencing of the structural gene
    • Green, B.A., J.E. Farley, T. Quinn-Dey, R.A. Deich, and G.W. Zlotnick. 1991. The e (P4) outer membrane protein of Haemophilus influenzae: biologic activity of anti-e serum and cloning and sequencing of the structural gene. Infect. Immun. 59:3191-3198.
    • (1991) Infect. Immun. , vol.59 , pp. 3191-3198
    • Green, B.A.1    Farley, J.E.2    Quinn-Dey, T.3    Deich, R.A.4    Zlotnick, G.W.5
  • 18
    • 0021930401 scopus 로고
    • Decreased protective efficacy of reduced and alkylated human immune serum globulin in experimental infection with Haemaphilus influenzae type b
    • Schreiber, J.R., V.A. Barrus, and G.R. Siber. 1985. Decreased protective efficacy of reduced and alkylated human immune serum globulin in experimental infection with Haemaphilus influenzae type b. Infect. Immun. 47:142-148.
    • (1985) Infect. Immun. , vol.47 , pp. 142-148
    • Schreiber, J.R.1    Barrus, V.A.2    Siber, G.R.3
  • 19
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to select promoters in Escherichia coli using bacterio-phage lambda and mu
    • Casadaban, M.J. 1976. Transposition and fusion of the lac genes to select promoters in Escherichia coli using bacterio-phage lambda and mu. J. Mol. Biol. 104:541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 21
    • 0004136246 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • Maniatis, T., E.F. Frisch, and J. Sambrook. 1982. Molecular Cloning. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY. pp. 97-148.
    • (1982) Molecular Cloning , pp. 97-148
    • Maniatis, T.1    Frisch, E.F.2    Sambrook, J.3
  • 22
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A.C.Y., and S.N. Cohen. 1978. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol. 134:1141-1156.
    • (1978) J. Bacteriol. , vol.134 , pp. 1141-1156
    • Chang, A.C.Y.1    Cohen, S.N.2
  • 23
    • 0024283925 scopus 로고
    • The nucleotide sequence of pACYC184
    • Rose, R.E. 1988. The nucleotide sequence of pACYC184. Nucleic Acids Res. 16:355.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 355
    • Rose, R.E.1
  • 24
    • 0024283935 scopus 로고
    • The nucleotide sequence of pACYC177
    • Rose, R.E. 1988. The nucleotide sequence of pACYC177. Nucleic Acids Res. 16:356.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 356
    • Rose, R.E.1
  • 25
    • 0023461268 scopus 로고
    • Specific synthesis of DNA in vitro via a polymerase chain reaction
    • Mullis, K.B., and F. Faloona. 1987. Specific synthesis of DNA in vitro via a polymerase chain reaction. Methods Enzymol. 155:335-340.
    • (1987) Methods Enzymol. , vol.155 , pp. 335-340
    • Mullis, K.B.1    Faloona, F.2
  • 26
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E.M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 51:503-517.
    • (1975) J. Mol. Biol. , vol.51 , pp. 503-517
    • Southern, E.M.1
  • 27
    • 0025874161 scopus 로고
    • Electroporation of Haemophilus influenzae is effective for transformation of plasmid but not chromosomal DNA
    • Mitchell, M.A., K. Skowronek, L. Kauc, and S.H. Goodgal. 1991. Electroporation of Haemophilus influenzae is effective for transformation of plasmid but not chromosomal DNA. Nucleic Acids Res. 19:3625-3628.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3625-3628
    • Mitchell, M.A.1    Skowronek, K.2    Kauc, L.3    Goodgal, S.H.4
  • 28
    • 0024401347 scopus 로고
    • Transposon mutagenesis, characterization, and cloning of transformation genes of Haemophilus influenzac Rd
    • Tomb, J.F., G.J. Barack, M.S. Chandler, R.J. Redfield and H.O. Smith. 1989. Transposon mutagenesis, characterization, and cloning of transformation genes of Haemophilus influenzac Rd. J. Bacteriol. 171:3796-3802.
    • (1989) J. Bacteriol. , vol.171 , pp. 3796-3802
    • Tomb, J.F.1    Barack, G.J.2    Chandler, M.S.3    Redfield, R.J.4    Smith, H.O.5
  • 29
    • 0029562634 scopus 로고
    • Characterization of Vibrio cholerae bacteriophage K139 and use of a novel mini transposon to identify a phage-encoded virulence factor
    • Reidl, J., and J.J. Mekalanos. 1995. Characterization of Vibrio cholerae bacteriophage K139 and use of a novel mini transposon to identify a phage-encoded virulence factor. Mol. Microbiol. 18:685-701.
    • (1995) Mol. Microbiol. , vol.18 , pp. 685-701
    • Reidl, J.1    Mekalanos, J.J.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0026686195 scopus 로고
    • Glutamyl-transfer RNA: A precursor of heme and chlorophyll biosynthesis
    • Jahn, D., E. Verkamp, and D. Söil. 1992. Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis Trends Biochem. Sci. 17:215-218.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 215-218
    • Jahn, D.1    Verkamp, E.2    Söil, D.3
  • 34
    • 0015767767 scopus 로고
    • Mutations affecting porphyrin biosynthesis in Eschenchia coli
    • Powell, K.A., R. Cox, M. McConville, and H.P. Charles. 1973. Mutations affecting porphyrin biosynthesis in Eschenchia coli. Enzyme. 16:65-73.
    • (1973) Enzyme , vol.16 , pp. 65-73
    • Powell, K.A.1    Cox, R.2    McConville, M.3    Charles, H.P.4
  • 35
    • 0024724030 scopus 로고
    • Isolation, nucleotide sequence, and preliminary characterization of the Escherichia coli K-12 hemA gene
    • Verkamp, E., and B.K. Chelm. 1989. Isolation, nucleotide sequence, and preliminary characterization of the Escherichia coli K-12 hemA gene. J Bacteriol. 171:4728-4735.
    • (1989) J Bacteriol. , vol.171 , pp. 4728-4735
    • Verkamp, E.1    Chelm, B.K.2
  • 36
    • 0018287635 scopus 로고
    • Mutants of Escherichia coli K-12 permeable to haemin
    • McConville, M.L., and H.P. Charles. 1979. Mutants of Escherichia coli K-12 permeable to haemin. J Gen. Microbiol. 113: 165-168
    • (1979) J Gen. Microbiol. , vol.113 , pp. 165-168
    • McConville, M.L.1    Charles, H.P.2
  • 37
    • 0026445951 scopus 로고
    • Hemin uptake system of Yersinia enterocolitica: Similarities with other TonB-dependent systems in gram-negative bacteria
    • Stojiljkovic, I., and K. Hantke. 1992. Hemin uptake system of Yersinia enterocolitica: similarities with other TonB-dependent systems in gram-negative bacteria. EMBO (Eur. Mol. Biol. Organ.) J. 11:4359-4367.
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 4359-4367
    • Stojiljkovic, I.1    Hantke, K.2
  • 38
    • 0025893685 scopus 로고
    • Structure and organization of E. coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes
    • Reuter, K., R. Slany, F. Ullnch, and H. Kersten. 1991. Structure and organization of E. coli genes involved in biosynthesis of the deazaguanine derivative queuine, a nutrient factor for eukaryotes. J. Bacteriol. 173:2256-2264.
    • (1991) J. Bacteriol. , vol.173 , pp. 2256-2264
    • Reuter, K.1    Slany, R.2    Ullnch, F.3    Kersten, H.4
  • 40
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara, M. 1992. Agents that increase the permeability of the outer membrane. Microbiol. Rev. 56:395-411.
    • (1992) Microbiol. Rev. , vol.56 , pp. 395-411
    • Vaara, M.1
  • 41
    • 0027417443 scopus 로고
    • Cloning and characterization of the Vibrio cholerae genes encoding the utilization of iron from haemin and haemoglobin
    • Henderson, D.P., and S.M. Payne. 1993. Cloning and characterization of the Vibrio cholerae genes encoding the utilization of iron from haemin and haemoglobin. Mol. Microbiol. 7: 461-469.
    • (1993) Mol. Microbiol. , vol.7 , pp. 461-469
    • Henderson, D.P.1    Payne, S.M.2
  • 42
    • 0028086537 scopus 로고
    • Transport of haemin across the cytoplasmic membrane through a haemin-specific periplasmic binding-protein-dependent transport system in Yersinia enterocolitica
    • Stojiljkovic, I., and K. Hantke. 1994. Transport of haemin across the cytoplasmic membrane through a haemin-specific periplasmic binding-protein-dependent transport system in Yersinia enterocolitica. Mol. Microbiol. 13:719-732.
    • (1994) Mol. Microbiol. , vol.13 , pp. 719-732
    • Stojiljkovic, I.1    Hantke, K.2
  • 44
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R., and D.J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 45
    • 0026084296 scopus 로고
    • Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein
    • Olson, E.R., D.S. Dunyak, L.M. Jurrs, and R.A. Poorman. 1991. Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein. J. Bacteriol. 173:234-244.
    • (1991) J. Bacteriol. , vol.173 , pp. 234-244
    • Olson, E.R.1    Dunyak, D.S.2    Jurrs, L.M.3    Poorman, R.A.4
  • 46
    • 0027532660 scopus 로고
    • The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli
    • Verkamp, E., V.M. Backman, J.M. Bjoernsson, and D. Soell. 1993. The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli. J. Bacteriol. 175:1452-1456.
    • (1993) J. Bacteriol. , vol.175 , pp. 1452-1456
    • Verkamp, E.1    Backman, V.M.2    Bjoernsson, J.M.3    Soell, D.4
  • 47
    • 0025924816 scopus 로고
    • Close tetrapod relationships of the coelacanth Latimeria indicated by haemoglobin sequences
    • Gorr, T., T. Kleinschmidt, and H. Fricke. 1991. Close tetrapod relationships of the coelacanth Latimeria indicated by haemoglobin sequences. Nature (Lond.). 351:394-397.
    • (1991) Nature (Lond.) , vol.351 , pp. 394-397
    • Gorr, T.1    Kleinschmidt, T.2    Fricke, H.3
  • 48
    • 0026084295 scopus 로고
    • Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough
    • Pollock, W.B., M. Loufti, M. Bruschi, J. Rapp-Giles, J.D. Wall, and G. Voordouw. 1991. Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough. J. Bacteriol. 173:220-228.
    • (1991) J. Bacteriol. , vol.173 , pp. 220-228
    • Pollock, W.B.1    Loufti, M.2    Bruschi, M.3    Rapp-Giles, J.4    Wall, J.D.5    Voordouw, G.6
  • 49
    • 0028821439 scopus 로고
    • Heme binds to a short sequence that serves a regulatory function in diverse proteins
    • Zhang, L., and L. Guarente. 1995. Heme binds to a short sequence that serves a regulatory function in diverse proteins. EMBO (Eur. Mol. Biol. Organ.) J. 14:313-320.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 313-320
    • Zhang, L.1    Guarente, L.2
  • 50
    • 0027171383 scopus 로고
    • Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 a resolution
    • Hoess, A., S. Watson, G.R. Siber, and R. Liddington. 1993. Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 A resolution. EMBO (Eur. Mol. Biol. Organ.) J. 12:3351-3356.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 3351-3356
    • Hoess, A.1    Watson, S.2    Siber, G.R.3    Liddington, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.