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Volumn 197, Issue 8, 2008, Pages 1124-1132

Identification of 2 hypothetical genes involved in Neisseria meningitidis cathelicidin resistance

Author keywords

[No Author keywords available]

Indexed keywords

CATHELICIDIN; CATHELIN RELATED ANTIMICROBIAL PEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 42549116264     PISSN: 00221899     EISSN: None     Source Type: Journal    
DOI: 10.1086/533456     Document Type: Article
Times cited : (15)

References (35)
  • 1
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • Peschel A. How do bacteria resist human antimicrobial peptides? Trends Microbiol 2002; 10:179-86.
    • (2002) Trends Microbiol , vol.10 , pp. 179-186
    • Peschel, A.1
  • 2
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: Effectors in innate immunity and novel antimicrobials
    • Hancock RE. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect Dis 2001; 1:156-64.
    • (2001) Lancet Infect Dis , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 3
    • 0036252092 scopus 로고    scopus 로고
    • Cationic peptides: Distribution and mechanisms of resistance
    • Devine DA, Hancock RE. Cationic peptides: distribution and mechanisms of resistance. Curr Pharm Des 2002; 8:703-14.
    • (2002) Curr Pharm Des , vol.8 , pp. 703-714
    • Devine, D.A.1    Hancock, R.E.2
  • 4
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown KL, Hancock RE. Cationic host defense (antimicrobial) peptides. Curr Opin Immunol 2006; 18:24-30.
    • (2006) Curr Opin Immunol , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 5
    • 0035936156 scopus 로고    scopus 로고
    • Innate antimicrobial peptide protects the skin from invasive bacterial infection
    • Nizet V, Ohtake T, Lauth X, et al. Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature 2001; 414:454-7.
    • (2001) Nature , vol.414 , pp. 454-457
    • Nizet, V.1    Ohtake, T.2    Lauth, X.3
  • 6
    • 0001216086 scopus 로고    scopus 로고
    • Epithelial antimicrobial peptides in host defense against infection
    • Bals R. Epithelial antimicrobial peptides in host defense against infection. Respir Res 2000; 1:141-50.
    • (2000) Respir Res , vol.1 , pp. 141-150
    • Bals, R.1
  • 7
    • 0034998629 scopus 로고    scopus 로고
    • Participation of mammalian defensins and cathelicidins in anti-microbial immunity: Receptors and activities of human defensins and cathelicidin (LL-37)
    • Yang D, Chertov O, Oppenheim JJ. Participation of mammalian defensins and cathelicidins in anti-microbial immunity: receptors and activities of human defensins and cathelicidin (LL-37). J Leukoc Biol 2001; 69:691-7.
    • (2001) J Leukoc Biol , vol.69 , pp. 691-697
    • Yang, D.1    Chertov, O.2    Oppenheim, J.J.3
  • 8
    • 0036379140 scopus 로고    scopus 로고
    • Cathelicidins, essential gene-encoded mammalian antibiotics
    • Zaiou M, Gallo RL. Cathelicidins, essential gene-encoded mammalian antibiotics. J Mol Med 2002; 80:549-61.
    • (2002) J Mol Med , vol.80 , pp. 549-561
    • Zaiou, M.1    Gallo, R.L.2
  • 9
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity
    • Oren Z, Lerman JC, Gudmundsson GH, Agerberth B, Shai Y. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem J 1999; 341:501-13.
    • (1999) Biochem J , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 10
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipatic alpha-helical antimicrobial peptides
    • Oren Z, Shai Y. Mode of action of linear amphipatic alpha-helical antimicrobial peptides. Biopolymers 1998; 47:451-63.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 11
    • 0025811874 scopus 로고
    • Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: Peptide isolation and cloning of a cDNA
    • Diamond G, Zasloff M, Eck H, Brasseur M, Maloy WL, Bevins CL. Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA. Proc Natl Acad Sci USA 1991; 88:3952-6.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3952-3956
    • Diamond, G.1    Zasloff, M.2    Eck, H.3    Brasseur, M.4    Maloy, W.L.5    Bevins, C.L.6
  • 12
    • 0028902757 scopus 로고
    • Epithelial antibiotics induced at sites of inflammation
    • Schonwetter BS, Stolzenberg ED, Zasloff MA. Epithelial antibiotics induced at sites of inflammation. Science 1995; 267:1645-8.
    • (1995) Science , vol.267 , pp. 1645-1648
    • Schonwetter, B.S.1    Stolzenberg, E.D.2    Zasloff, M.A.3
  • 13
    • 0029007198 scopus 로고
    • hCAP-18, a cathelin/probactenecin- like protein of human neutrophil specific granules
    • Cowland JB, Johnsen AH, Borregaard N. hCAP-18, a cathelin/probactenecin- like protein of human neutrophil specific granules. FEBS Lett 1995; 368:173-6.
    • (1995) FEBS Lett , vol.368 , pp. 173-176
    • Cowland, J.B.1    Johnsen, A.H.2    Borregaard, N.3
  • 14
    • 0034332193 scopus 로고    scopus 로고
    • The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations
    • Agerberth B, Charo J, Werr J, et al. The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations. Blood 2000; 96:3086-93.
    • (2000) Blood , vol.96 , pp. 3086-3093
    • Agerberth, B.1    Charo, J.2    Werr, J.3
  • 15
    • 0034946907 scopus 로고    scopus 로고
    • Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus
    • Dorschner RA, Pestonjamasp VK, Tamakuwala S, et al. Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus. J Invest Dermatol 2001; 117:91-7.
    • (2001) J Invest Dermatol , vol.117 , pp. 91-97
    • Dorschner, R.A.1    Pestonjamasp, V.K.2    Tamakuwala, S.3
  • 17
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415:389-95.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 18
    • 0036714329 scopus 로고    scopus 로고
    • Previously unrecognized vaccine candidates against group B meningococcus identified by DNA microarrays
    • Grifantini R, Bartolini E, Muzzi A, et al. Previously unrecognized vaccine candidates against group B meningococcus identified by DNA microarrays. Nat Biotechnol 2002; 20:914-21.
    • (2002) Nat Biotechnol , vol.20 , pp. 914-921
    • Grifantini, R.1    Bartolini, E.2    Muzzi, A.3
  • 19
    • 0025297769 scopus 로고
    • Nucleotide sequence of the erythromycin resistance gene of the conjugative transposon Tn1545
    • Trieu-Cuot P, Poyart-Salmeron C, Carlier C, Courvalin P. Nucleotide sequence of the erythromycin resistance gene of the conjugative transposon Tn1545. Nucleic Acids Res 1990; 18:3660.
    • (1990) Nucleic Acids Res , vol.18 , pp. 3660
    • Trieu-Cuot, P.1    Poyart-Salmeron, C.2    Carlier, C.3    Courvalin, P.4
  • 20
    • 8544233512 scopus 로고    scopus 로고
    • Characterization of a novel Neisseria meningitidis Fur and iron-regulated operon required for protection from oxidative stress: Utility of DNA microarray in the assignment of the biological role of hypothetical genes
    • Grifantini R, Frigimelica E, Delany I, Bartolini E, Giovinazzi S, Balloni S. Characterization of a novel Neisseria meningitidis Fur and iron-regulated operon required for protection from oxidative stress: utility of DNA microarray in the assignment of the biological role of hypothetical genes. Mol Microbiol 2004; 54:962-79.
    • (2004) Mol Microbiol , vol.54 , pp. 962-979
    • Grifantini, R.1    Frigimelica, E.2    Delany, I.3    Bartolini, E.4    Giovinazzi, S.5    Balloni, S.6
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 33845487301 scopus 로고    scopus 로고
    • Induction of the antimicrobial peptide CRAMP in the blood-brain barrier and meninges after meningococcal infection
    • Bergman P, Johansson L, Wan H, et al. Induction of the antimicrobial peptide CRAMP in the blood-brain barrier and meninges after meningococcal infection. Infect Immun 2006; 74:6982-91.
    • (2006) Infect Immun , vol.74 , pp. 6982-6991
    • Bergman, P.1    Johansson, L.2    Wan, H.3
  • 24
    • 0000207681 scopus 로고
    • TMbase - a database of membrane spanning proteins segments
    • Hofmann K, Stoffel W. TMbase - a database of membrane spanning proteins segments. Biol Chem Hoppe Seyler 1993; 374:166.
    • (1993) Biol Chem Hoppe Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 25
    • 0031985455 scopus 로고    scopus 로고
    • Periplasmic superoxide dismutase in meningococcal pathogenicity
    • Wilks KE, Dunn KL, Farrant JL, et al. Periplasmic superoxide dismutase in meningococcal pathogenicity. Infect Immun 1998; 66:213-7.
    • (1998) Infect Immun , vol.66 , pp. 213-217
    • Wilks, K.E.1    Dunn, K.L.2    Farrant, J.L.3
  • 27
    • 1642581491 scopus 로고    scopus 로고
    • A mutant form of the Neisseria gonorrhoeae pilus secretin protein PilQ allows increased entry of heme and antimicrobial compounds
    • Chen CJ, Tobiason DM, Thomas CE, Shafer WM, Seifert HS, Sparling PF. A mutant form of the Neisseria gonorrhoeae pilus secretin protein PilQ allows increased entry of heme and antimicrobial compounds. J Bacteriol 2004; 186:730-9.
    • (2004) J Bacteriol , vol.186 , pp. 730-739
    • Chen, C.J.1    Tobiason, D.M.2    Thomas, C.E.3    Shafer, W.M.4    Seifert, H.S.5    Sparling, P.F.6
  • 28
    • 22544486843 scopus 로고    scopus 로고
    • Cationic antimicrobial peptide resistance in Neisseria meningitidis
    • Tzeng YL, Ambrose KD, Zughaier S, et al. Cationic antimicrobial peptide resistance in Neisseria meningitidis. J Bacteriol 2005; 187:5387-96.
    • (2005) J Bacteriol , vol.187 , pp. 5387-5396
    • Tzeng, Y.L.1    Ambrose, K.D.2    Zughaier, S.3
  • 30
    • 0033377813 scopus 로고    scopus 로고
    • Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system
    • Gudmundsson GH, Agerberth B. Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system. J Immunol Methods 1999; 232:45-54.
    • (1999) J Immunol Methods , vol.232 , pp. 45-54
    • Gudmundsson, G.H.1    Agerberth, B.2
  • 31
    • 1442330405 scopus 로고    scopus 로고
    • Interplay between antibacterial effectors: A macrophage antimicrobial peptide impairs intracellular Salmonella replication
    • Rosenberger CM, Gallo RL, Finlay BB. Interplay between antibacterial effectors: a macrophage antimicrobial peptide impairs intracellular Salmonella replication. Proc Natl Acad Sci USA 2004; 101:2422-7.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2422-2427
    • Rosenberger, C.M.1    Gallo, R.L.2    Finlay, B.B.3
  • 32
    • 13444259757 scopus 로고    scopus 로고
    • Mig-14 is an inner membrane-associated protein that promotes Salmonella typhimurium resistance to CRAMP, survival within activated macrophages and persistent infection
    • Brodsky IE, Ghori N, Falkow S, Monack D. Mig-14 is an inner membrane-associated protein that promotes Salmonella typhimurium resistance to CRAMP, survival within activated macrophages and persistent infection. Mol Microbiol 2005; 55:954-72.
    • (2005) Mol Microbiol , vol.55 , pp. 954-972
    • Brodsky, I.E.1    Ghori, N.2    Falkow, S.3    Monack, D.4
  • 33
    • 0035821289 scopus 로고    scopus 로고
    • Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with l-lysine
    • Peschel A, Jack RW, Otto M, et al. Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with l-lysine. J Exp Med 2001; 193:1067-76.
    • (2001) J Exp Med , vol.193 , pp. 1067-1076
    • Peschel, A.1    Jack, R.W.2    Otto, M.3
  • 34
    • 0033020793 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa fur overlaps with a gene encoding a novel outer membrane lipoprotein, OmlA
    • Ochsner UA, Vasil AI, Johnson Z, Vasil ML. Pseudomonas aeruginosa fur overlaps with a gene encoding a novel outer membrane lipoprotein, OmlA. J Bacteriol 1999; 181:1099-109.
    • (1999) J Bacteriol , vol.181 , pp. 1099-1109
    • Ochsner, U.A.1    Vasil, A.I.2    Johnson, Z.3    Vasil, M.L.4
  • 35
    • 20544432535 scopus 로고    scopus 로고
    • Ramos JL, Martinez-Bueno M, Molina-Henares AJ, et al R. The TetR family of transcriptional repressors. Microbiol Mol Biol Rev 2005; 69:326-56.
    • Ramos JL, Martinez-Bueno M, Molina-Henares AJ, et al R. The TetR family of transcriptional repressors. Microbiol Mol Biol Rev 2005; 69:326-56.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.