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Volumn 65, Issue 7, 1997, Pages 2898-2903

Effects of pH and salinity on the antimicrobial properties of clavanins

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; CLAVANIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 1842373858     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.65.7.2898-2903.1997     Document Type: Article
Times cited : (210)

References (43)
  • 1
    • 0015888330 scopus 로고
    • Properties of salivary basic proteins showing polymorphism
    • Azen, A. E. 1973. Properties of salivary basic proteins showing polymorphism. Biochem. Genet. 9:69-86.
    • (1973) Biochem. Genet. , vol.9 , pp. 69-86
    • Azen, A.E.1
  • 2
    • 0028834275 scopus 로고
    • CDNA sequences of three sheep mycloid cathelicidins
    • Bagella, L., M. Scocchi, and M. Zanetti. 1995. cDNA sequences of three sheep mycloid cathelicidins. FEBS Lett. 376:225-228.
    • (1995) FEBS Lett. , vol.376 , pp. 225-228
    • Bagella, L.1    Scocchi, M.2    Zanetti, M.3
  • 3
    • 0017699712 scopus 로고
    • Polyacrylamide gel elcctrophoresis of human salivary histidine-rich polypeptides
    • Baum, B. J., J. L. Bird, and R. W. Longton. 1977. Polyacrylamide gel elcctrophoresis of human salivary histidine-rich polypeptides. J. Dent. Res. 56: :1115-1118.
    • (1977) J. Dent. Res. , vol.56 , pp. 1115-1118
    • Baum, B.J.1    Bird, J.L.2    Longton, R.W.3
  • 4
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman, H. G. 1995. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol, 13:61-92.
    • (1995) Annu. Rev. Immunol , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 5
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • Rockville
    • Broekaert, W. F., F. R. Terras, B. P. Cam mue, and R. W. Osborn. 1995. Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol. (Rockville) 108:1353-1358.
    • (1995) Plant Physiol , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.2    Cam Mue, B.P.3    Osborn, R.W.4
  • 6
    • 0024438756 scopus 로고
    • Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers
    • Duclohier, H., G. Molle, and G. Spach. 1989. Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers. Biophys. J. 56:1017-1021.
    • (1989) Biophys. J. , vol.56 , pp. 1017-1021
    • Duclohier, H.1    Molle, G.2    Spach, G.3
  • 8
    • 0029111532 scopus 로고
    • Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles
    • Gazit, E., A. Boman, H. G. Boman, and Y. Shai. 1995. Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles. Biochemistry 34:11479-11488.
    • (1995) Biochemistry , vol.34 , pp. 11479-11488
    • Gazit, E.1    Boman, A.2    Boman, H.G.3    Shai, Y.4
  • 9
    • 0023100945 scopus 로고
    • Biosynthesis and degradation of peptides derived from Xenopus laevis prohormones
    • Giovannini, M. G., L. Poulter, B. W. Gibson, and D. H. Williams. 1987. Biosynthesis and degradation of peptides derived from Xenopus laevis prohormones. Biochem. J. 243:113-120.
    • (1987) Biochem. J. , vol.243 , pp. 113-120
    • Giovannini, M.G.1    Poulter, L.2    Gibson, B.W.3    Williams, D.H.4
  • 10
    • 0020366780 scopus 로고
    • Insect immunity: Isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae
    • Hultmark, D., A. Engstrom, H. Bennich, R. Kapur, and H. G. Boman. 1982. Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae. Eur. J. Biochem. 127:207-217.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 207-217
    • Hultmark, D.1    Engstrom, A.2    Bennich, H.3    Kapur, R.4    Boman, H.G.5
  • 12
    • 0026731832 scopus 로고
    • Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy
    • Jackson, M., H. H. Mantsch, and J. H. Spencer. 1992. Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy. Biochemistry 31:7289-7293.
    • (1992) Biochemistry , vol.31 , pp. 7289-7293
    • Jackson, M.1    Mantsch, H.H.2    Spencer, J.H.3
  • 16
    • 0025165288 scopus 로고
    • The intraccllular pH of tunicate blood cells: Ascidia ceratodes whole blood, morula cells, vacuoles and cytoplasm
    • Lee, S., K. Nakanishi, and K. Kustin. 1990. The intraccllular pH of tunicate blood cells: Ascidia ceratodes whole blood, morula cells, vacuoles and cytoplasm. Biochim. Biophys. Acta 1033:311-317,
    • (1990) Biochim. Biophys. Acta , vol.1033 , pp. 311-317
    • Lee, S.1    Nakanishi, K.2    Kustin, K.3
  • 17
    • 0023920225 scopus 로고
    • Concurrent assessment of inner and ouicr membrane permeabilizution and bacteriolysis in E. coli by multiple-wavelength spectrophotometry
    • Lehrer, R. I., A. Barton, and T. Ganz. 1988. Concurrent assessment of inner and ouicr membrane permeabilizution and bacteriolysis in E. coli by multiple-wavelength spectrophotometry. J. Immunol. Methods 108:153-158.
    • (1988) J. Immunol. Methods , vol.108 , pp. 153-158
    • Lehrer, R.I.1    Barton, A.2    Ganz, T.3
  • 18
    • 0024391711 scopus 로고
    • Interaction of human defcnsins with Escherichia coli. Mechanism of bactericidal activity
    • Lehrer, R. I., A. Bartun, K. A. Daher, S. S. Harwig, T. Ganz, and M. E. Selsted. 1989. Interaction of human defcnsins with Escherichia coli. Mechanism of bactericidal activity. J. Clin. Invest. 84:553-561.
    • (1989) J. Clin. Invest. , vol.84 , pp. 553-561
    • Lehrer, R.I.1    Bartun, A.2    Daher, K.A.3    Harwig, S.S.4    Ganz, T.5    Selsted, M.E.6
  • 20
    • 0021280786 scopus 로고
    • Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans
    • MacKay, B. J., L. Denapitaya, V. J. laconn, S. B. Krost, and J. J. Pollock. 1984. Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans. Infect. Immun. 44:695-701.
    • (1984) Infect. Immun. , vol.44 , pp. 695-701
    • MacKay, B.J.1    Denapitaya, L.2    Laconn, V.J.3    Krost, S.B.4    Pollock, J.J.5
  • 21
    • 0021239238 scopus 로고
    • Isolation of milligram quantities of a group of histidine-rich polypeptides from human parotid saliva
    • MacKay, B. J., J. J. Pollock, V. J. Iacono, and B. J. Baum. 1984. Isolation of milligram quantities of a group of histidine-rich polypeptides from human parotid saliva. Infect. Immun. 44:688-694.
    • (1984) Infect. Immun. , vol.44 , pp. 688-694
    • MacKay, B.J.1    Pollock, J.J.2    Iacono, V.J.3    Baum, B.J.4
  • 23
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host defense peptides
    • Maloy, W. L., and U. P. Kari. 1995. Structure-activity studies on magainins and other host defense peptides. Biopolymers 37:105-22.
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 25
  • 26
    • 0028818140 scopus 로고
    • Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers
    • Matsuzaki, K., O. Murase, and K. Miyajima. 1995. Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers. Biochemistry 34:12553-12559.
    • (1995) Biochemistry , vol.34 , pp. 12553-12559
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 28
    • 0027158358 scopus 로고
    • Synthetic bactericidal peptide based on CAP37; a 37-kDa human neutrophil granuleassociated cationic antimicrobial protein chemotactic for monocytes
    • Pereira, H. A., I. Erdem, J. Pohl, and J. K. Spitznagel. 1993. Synthetic bactericidal peptide based on CAP37; a 37-kDa human neutrophil granuleassociated cationic antimicrobial protein chemotactic for monocytes. Proc. Natl. Acad. Sci. USA 90:4733-4737.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4733-4737
    • Pereira, H.A.1    Erdem, I.2    Pohl, J.3    Spitznagel, J.K.4
  • 29
    • 0029000671 scopus 로고
    • The dorsalrelated immunity factor, Dif, is a sequence-specific trans-activator of Drosophila Cecropin gene expression
    • Petersen, U. M., G. Bjurklund, Y. T. Ip, and Y. Engstrom. 1995. The dorsalrelated immunity factor, Dif, is a sequence-specific trans-activator of Drosophila Cecropin gene expression. EMBO J. 14:3146-3158.
    • (1995) EMBO J. , vol.14 , pp. 3146-3158
    • Petersen, U.M.1    Bjurklund, G.2    Ip, Y.T.3    Engstrom, Y.4
  • 30
    • 0028321505 scopus 로고
    • Membrane-induced conformation of an active candidacidal fragment of salivary hisiatins
    • Raj, P. A., S. D. Soni, and M. J. Le vine. 1994. Membrane-induced conformation of an active candidacidal fragment of salivary hisiatins. J. Biol. Chem. 269:9610-9619.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9610-9619
    • Raj, P.A.1    Soni, S.D.2    Le Vine, M.J.3
  • 31
    • 0030570839 scopus 로고    scopus 로고
    • Stabilization of helix by side-chain interactions in histatin-derived peptides: Role in candidacidal activity
    • Ramalingam, K., T. L. Gururaja, N. Ramasubbu, and M. J. Levlne. 1996. Stabilization of helix by side-chain interactions in histatin-derived peptides: role in candidacidal activity. Biochem. Biophys. Res. Commun. 225:47-53.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 47-53
    • Ramalingam, K.1    Gururaja, T.L.2    Ramasubbu, N.3    Levlne, M.J.4
  • 32
    • 0024980013 scopus 로고
    • Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (His1 and His2)
    • Sabatini, L. M., and E. A. Azen. 1989. Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (His1 and His2). Biochem. Biophys. Res. Commun. 160:495-502.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 495-502
    • Sabatini, L.M.1    Azen, E.A.2
  • 33
    • 0029870085 scopus 로고    scopus 로고
    • Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid
    • Smith, J. J., S. M. Travis, E. P. Greenberg, and M. J. Welsh. 1996. Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid. Cell 85:229-236.
    • (1996) Cell , vol.85 , pp. 229-236
    • Smith, J.J.1    Travis, S.M.2    Greenberg, E.P.3    Welsh, M.J.4
  • 34
    • 0023903695 scopus 로고
    • The cDNA sequence coding for prepro-PGS prepro-magainins and aspects of the processing pf this prepropolypeptide
    • Terry, A. S., L. Poulter, D. H. Williams, J. C. Nutkins, M. G. Glovannini, C. H. Moore, and B. W. Gibson. 1988. The cDNA sequence coding for prepro-PGS prepro-magainins and aspects of the processing pf this prepropolypeptide. J. Biol. Chcm. 263:5745-5751.
    • (1988) J. Biol. Chcm. , vol.263 , pp. 5745-5751
    • Terry, A.S.1    Poulter, L.2    Williams, D.H.3    Nutkins, J.C.4    Glovannini, M.G.5    Moore, C.H.6    Gibson, B.W.7
  • 36
    • 0030307267 scopus 로고    scopus 로고
    • The final pH of bacteria comprising the predominant flora on sound and carious human root and enamel surfaces
    • van Houte, J., J. Lopman, and R. Kent, 1996. The final pH of bacteria comprising the predominant flora on sound and carious human root and enamel surfaces. J. Dent. Res. 75:1008-1014.
    • (1996) J. Dent. Res. , vol.75 , pp. 1008-1014
    • Van Houte, J.1    Lopman, J.2    Kent, R.3
  • 38
    • 0027584861 scopus 로고
    • Salivary proteolysis of histidine-rich polypeptides and the antifungal activity of peptide degradation products
    • Xu, L., K. Lal, R. P. Santarpia III, and J. J. Pollock. 1993. Salivary proteolysis of histidine-rich polypeptides and the antifungal activity of peptide degradation products. Arch. Oral Biol. 38:277-283.
    • (1993) Arch. Oral Biol. , vol.38 , pp. 277-283
    • Xu, L.1    Lal, K.2    Santarpia III, R.P.3    Pollock, J.J.4
  • 39
    • 0025733707 scopus 로고
    • Anticandidal activity of major human salivary histatins
    • Xu, T., S. M. Levitz, R. D. Diamond, and F. G. Oppenheim. 1991. Anticandidal activity of major human salivary histatins. Infect. Immun. 59:2549-2554.
    • (1991) Infect. Immun. , vol.59 , pp. 2549-2554
    • Xu, T.1    Levitz, S.M.2    Diamond, R.D.3    Oppenheim, F.G.4
  • 40
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti, M., R. Gennaro, and D. Romeo. 1995. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374:1-5.
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 41
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. 1988. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 84:5449-5453.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 42
    • 0023854883 scopus 로고
    • Antimicrobial activity of synthetic magainin peptides and several analogues
    • Zasloff, M., B. Martin, and H. C. Chen. 1988. Antimicrobial activity of synthetic magainin peptides and several analogues, Proc. Nail. Acad. Sci. USA 85:910-913.
    • (1988) Proc. Nail. Acad. Sci. USA , vol.85 , pp. 910-913
    • Zasloff, M.1    Martin, B.2    Chen, H.C.3
  • 43
    • 0029101209 scopus 로고
    • Recombinant histatins: Functional domain duplication enhances candidacidal activity
    • Zuo, Y., T. Xu, R. F. Troxler, J. Li, J. Driscoll, and F. G. Oppenheim. 1995. Recombinant histatins: functional domain duplication enhances candidacidal activity. Gene 161:87-91.
    • (1995) Gene , vol.161 , pp. 87-91
    • Zuo, Y.1    Xu, T.2    Troxler, R.F.3    Li, J.4    Driscoll, J.5    Oppenheim, F.G.6


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