메뉴 건너뛰기




Volumn 47, Issue 9, 2003, Pages 2804-2809

Antimicrobial characterization of human β-defensin 3 derivatives

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID; BETA DEFENSIN 3; CYSTEINE; HUMAN BETA DEFENSIN 3; HUMAN BETA DEFENSIN 3 ALPHA AMINOBUTYRIC ACID; HUMAN BETA DEFENSIN 3 DELTA10; HUMAN BETA DEFENSIN 3 DELTA8; PEPTIDE CHRG01; PEPTIDE CHRG02; PEPTIDE CHRG04; PEPTIDE CHRG06; PEPTIDE CHRG07; PEPTIDE DERIVATIVE; PEPTIDE STRC06; UNCLASSIFIED DRUG;

EID: 0041923585     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.47.9.2804-2809.2003     Document Type: Article
Times cited : (229)

References (39)
  • 2
    • 0033863173 scopus 로고    scopus 로고
    • Combinatorial libraries: A tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies
    • Blondelle, S. E., and K. Lohner. 2000. Combinatorial libraries: a tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies. Biopolymers 55:74-87.
    • (2000) Biopolymers , vol.55 , pp. 74-87
    • Blondelle, S.E.1    Lohner, K.2
  • 3
    • 0036086590 scopus 로고    scopus 로고
    • Treponema denticola is resistant to human β-defensins
    • Brissette, C. A., and S. A. Lukehart. 2002. Treponema denticola is resistant to human β-defensins. Infect. Immun. 70:3982-3984.
    • (2002) Infect. Immun. , vol.70 , pp. 3982-3984
    • Brissette, C.A.1    Lukehart, S.A.2
  • 4
    • 0027249384 scopus 로고
    • Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus
    • Cociancich, S., A. Ghazi, C. Hetru, J. A. Hoffmann, and L. Letellier. 1993. Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus. J. Biol. Chem. 268:19239-19245.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19239-19245
    • Cociancich, S.1    Ghazi, A.2    Hetru, C.3    Hoffmann, J.A.4    Letellier, L.5
  • 5
    • 0027218376 scopus 로고
    • Defensins promote fusion and lysis of negatively charged membranes
    • Fujii, G., M. E. Selsted, and D. Eisenberg. 1993. Defensins promote fusion and lysis of negatively charged membranes. Protein Sci. 2:1301-1312.
    • (1993) Protein Sci. , vol.2 , pp. 1301-1312
    • Fujii, G.1    Selsted, M.E.2    Eisenberg, D.3
  • 6
    • 0033569682 scopus 로고    scopus 로고
    • Defensins and host defense
    • Ganz, T. 1999. Defensins and host defense. Science 286:420-421.
    • (1999) Science , vol.286 , pp. 420-421
    • Ganz, T.1
  • 8
    • 0001475281 scopus 로고    scopus 로고
    • Identification of a novel, multifunctional beta-defensin (human beta-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction
    • García, J. R., F. Jaumann, S. Schulz, A. Krause, J. Rodríguez-Jiménez, U. Forssmann, K. Adermann, E. Kluver, C. Vogelmeier, D. Becker, R. Hedrich, W. G. Forssmann, and R. Bals. 2001. Identification of a novel, multifunctional beta-defensin (human beta-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction. Cell Tissue Res. 306:257-264.
    • (2001) Cell Tissue Res. , vol.306 , pp. 257-264
    • García, J.R.1    Jaumann, F.2    Schulz, S.3    Krause, A.4    Rodríguez-Jiménez, J.5    Forssmann, U.6    Adermann, K.7    Kluver, E.8    Vogelmeier, C.9    Becker, D.10    Hedrich, R.11    Forssmann, W.G.12    Bals, R.13
  • 10
    • 0026009980 scopus 로고
    • Human neutrophil peptide defensins induce single strand DNA breaks in target cells
    • Gera, J. F., and A. Lichtenstein. 1991. Human neutrophil peptide defensins induce single strand DNA breaks in target cells. Cell. Immunol. 138:108-120.
    • (1991) Cell. Immunol. , vol.138 , pp. 108-120
    • Gera, J.F.1    Lichtenstein, A.2
  • 11
    • 0033541516 scopus 로고    scopus 로고
    • Epithelial defensins impair adenoviral infection: Implication for adenovirus-mediated gene therapy
    • Gropp, R., M. Frye, T. O. Wagner, and J. Bargon. 1999. Epithelial defensins impair adenoviral infection: implication for adenovirus-mediated gene therapy. Hum. Gene Ther. 10:957-964.
    • (1999) Hum. Gene Ther. , vol.10 , pp. 957-964
    • Gropp, R.1    Frye, M.2    Wagner, T.O.3    Bargon, J.4
  • 13
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic
    • Harder, J., J. Bartels, E. Christophers, and J. M. Schröder. 2001. Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic. J. Biol. Chem. 276:5707-5713.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schröder, J.M.4
  • 14
    • 0027980251 scopus 로고
    • Neutrophil defensins: Purification, characterization, and antimicrobial testing
    • Harwig, S. S., T. Ganz, and R. I. Lehrer. 1994. Neutrophil defensins: purification, characterization, and antimicrobial testing. Methods Enzymol. 236:160-172.
    • (1994) Methods Enzymol. , vol.236 , pp. 160-172
    • Harwig, S.S.1    Ganz, T.2    Lehrer, R.I.3
  • 15
    • 0025903814 scopus 로고
    • Crystal structure of defensin HNP-3, an amphiphilic dimer: Mechanisms of membrane permeabilization
    • Hill, C. P., J. Yee, M. E. Selsted, and D. Eisenberg. 1991. Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization. Science 251:1481-1485.
    • (1991) Science , vol.251 , pp. 1481-1485
    • Hill, C.P.1    Yee, J.2    Selsted, M.E.3    Eisenberg, D.4
  • 17
    • 0029811094 scopus 로고    scopus 로고
    • Interactions of monomeric rabbit neutrophil defensins with bilayers: Comparison with dimeric human defensin HNP-2
    • Hristova, K., M. E. Selsted, and S. H. White. 1996. Interactions of monomeric rabbit neutrophil defensins with bilayers: comparison with dimeric human defensin HNP-2. Biochemistry 35:11888-11894.
    • (1996) Biochemistry , vol.35 , pp. 11888-11894
    • Hristova, K.1    Selsted, M.E.2    White, S.H.3
  • 18
    • 0030827974 scopus 로고    scopus 로고
    • Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins
    • Hristova, K., M. E. Selsted, and S. H. White. 1997. Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins. J. Biol. Chem. 272:24224-24233.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24224-24233
    • Hristova, K.1    Selsted, M.E.2    White, S.H.3
  • 20
    • 0025021992 scopus 로고
    • Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes
    • Kagan, B. L., M. E. Selsted, T. Ganz, and R. I. Lehrer. 1990. Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes. Proc. Natl. Acad. Sci. USA 87:210-214.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 210-214
    • Kagan, B.L.1    Selsted, M.E.2    Ganz, T.3    Lehrer, R.I.4
  • 21
    • 0030734903 scopus 로고    scopus 로고
    • Penetration of the insect defensin A into phospholipid monolayers and formation of defensin A-lipid complexes
    • Maget-Dana, R., and M. Ptak. 1997. Penetration of the insect defensin A into phospholipid monolayers and formation of defensin A-lipid complexes. Biophys. J. 73:2527-2533.
    • (1997) Biophys. J. , vol.73 , pp. 2527-2533
    • Maget-Dana, R.1    Ptak, M.2
  • 22
    • 0036171208 scopus 로고    scopus 로고
    • Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs: Structural and disulfide bridge requirements for activity
    • Mandal, M., M. V. Jagannadham, and R. Nagaraj. 2002. Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs: structural and disulfide bridge requirements for activity. Peptides 23:413-418.
    • (2002) Peptides , vol.23 , pp. 413-418
    • Mandal, M.1    Jagannadham, M.V.2    Nagaraj, R.3
  • 23
    • 0035000423 scopus 로고    scopus 로고
    • Cryptdin-3 induces novel apical conductance(s) in Cl- secretory, including cystic fibrosis, epithelia
    • Merlin, D., G. Yue, W. I. Lencer, M. E. Selsted, and J. L. Madara. 2001. Cryptdin-3 induces novel apical conductance(s) in Cl- secretory, including cystic fibrosis, epithelia. Am. J. Physiol. Cell Physiol. 280:C296-C302.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280
    • Merlin, D.1    Yue, G.2    Lencer, W.I.3    Selsted, M.E.4    Madara, J.L.5
  • 24
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • Peschel, A., M. Otto, R. W. Jack, H. Kalbacher, G. Jung, and F. Gotz. 1999. Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. J. Biol. Chem. 274:8405-8410.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5    Gotz, F.6
  • 25
    • 0030913746 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial activity of human intestinal defensin 5
    • Porter, E. M., E. van Dam, E. V. Valore, and T. Ganz. 1997. Broad-spectrum antimicrobial activity of human intestinal defensin 5. Infect. Immun. 65:2396-2401.
    • (1997) Infect. Immun. , vol.65 , pp. 2396-2401
    • Porter, E.M.1    Van Dam, E.2    Valore, E.V.3    Ganz, T.4
  • 26
    • 0037005996 scopus 로고    scopus 로고
    • Current status of defensins and their role in innate and adaptive immunity
    • Raj, P. A., and A. R. Dentino. 2002. Current status of defensins and their role in innate and adaptive immunity. FEMS Microbiol. Lett. 206:9-18.
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 9-18
    • Raj, P.A.1    Dentino, A.R.2
  • 27
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus
    • Schibli, D. J., H. N. Hunter, V. Aseyev, T. D. Starner, J. M. Wiencek, P. B. McCray, Jr., B. F. Tack, and H. J. Vogel. 2002. The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. J. Biol. Chem. 277:8279-8289.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8279-8289
    • Schibli, D.J.1    Hunter, H.N.2    Aseyev, V.3    Starner, T.D.4    Wiencek, J.M.5    McCray P.B., Jr.6    Tack, B.F.7    Vogel, H.J.8
  • 29
    • 0034967230 scopus 로고    scopus 로고
    • DNA as the intracellular secondary target for antibacterial action of human neutrophil peptide-I against Mycobacterium tuberculosis H37Ra
    • Sharma, S., and G. Khuller. 2001. DNA as the intracellular secondary target for antibacterial action of human neutrophil peptide-I against Mycobacterium tuberculosis H37Ra. Curr. Microbiol. 43:74-76.
    • (2001) Curr. Microbiol. , vol.43 , pp. 74-76
    • Sharma, S.1    Khuller, G.2
  • 30
    • 0036717730 scopus 로고    scopus 로고
    • Susceptibility of nontypeable Haemophilus influenzae to human β-defensins is influenced by lipooligosaccharide acylation
    • Starner, T. D., W. E. Swords, M. A. Apicella, and P. B. McCray, Jr. 2002. Susceptibility of nontypeable Haemophilus influenzae to human β-defensins is influenced by lipooligosaccharide acylation. Infect. Immun. 70:5287-5289.
    • (2002) Infect. Immun. , vol.70 , pp. 5287-5289
    • Starner, T.D.1    Swords, W.E.2    Apicella, M.A.3    McCray P.B., Jr.4
  • 31
    • 0033549108 scopus 로고    scopus 로고
    • Thia Zip reaction for synthesis of large cyclic peptides: Mechanisms and applications
    • Tam, J. P., Y. A. Lu, and Q. Yu. 1999. Thia Zip reaction for synthesis of large cyclic peptides: mechanisms and applications. J. Am. Chem. Soc. 121:4316-4324.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4316-4324
    • Tam, J.P.1    Lu, Y.A.2    Yu, Q.3
  • 32
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins
    • Tang, Y. Q., J. Yuan, G. Osapay, K. Osapay, D. Tran, C. J. Miller, A. J. Ouellette, and M. E. Selsted. 1999. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated α-defensins. Science 286:498-502.
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3    Osapay, K.4    Tran, D.5    Miller, C.J.6    Ouellette, A.J.7    Selsted, M.E.8
  • 33
    • 0033981958 scopus 로고    scopus 로고
    • Specific binding sites for an antifungal plant defensin from dahlia (Dahlia merckii) on fungal cells are required for antifungal activity
    • Thevissen, K., R. W. Osborn, D. P. Acland, and W. F. Broekaert. 2000. Specific binding sites for an antifungal plant defensin from dahlia (Dahlia merckii) on fungal cells are required for antifungal activity. Mol. Plant-Microbe Interact. 13:54-61.
    • (2000) Mol. Plant-Microbe Interact. , vol.13 , pp. 54-61
    • Thevissen, K.1    Osborn, R.W.2    Acland, D.P.3    Broekaert, W.F.4
  • 34
    • 0029097115 scopus 로고
    • Structure, function, and membrane integration of defensins
    • White, S. H., W. C. Wimley, and M. E. Selsted. 1995. Structure, function, and membrane integration of defensins. Curr. Opin. Struct. Biol. 5:521-527.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 521-527
    • White, S.H.1    Wimley, W.C.2    Selsted, M.E.3
  • 35
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores
    • Wimley, W. C., M. E. Selsted, and S. H. White. 1994. Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores. Protein Sci. 3:1362-1373.
    • (1994) Protein Sci. , vol.3 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 37
    • 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., O. Chertov, and J. J. Oppenheim. 2001. Participation of mammalian defensins and cathelicidins in anti-microbial immunity: receptors and activities of human defensins and cathelicidin (LL-37). J. Leukoc. Biol. 69:691-697.
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 691-697
    • Yang, D.1    Chertov, O.2    Oppenheim, J.J.3
  • 38
    • 0031984629 scopus 로고    scopus 로고
    • Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action
    • Yeaman, M. R., A. S. Bayer, S. P. Koo, W. Foss, and P. M. Sullam. 1998. Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action. J. Clin. Investig. 101:178-187.
    • (1998) J. Clin. Investig. , vol.101 , pp. 178-187
    • Yeaman, M.R.1    Bayer, A.S.2    Koo, S.P.3    Foss, W.4    Sullam, P.M.5
  • 39
    • 0034635459 scopus 로고    scopus 로고
    • Engineered salt-insensitive alphadefensins with end-to-end circularized structures
    • Yu, Q., R. I. Lehrer, and J. P. Tam. 2000. Engineered salt-insensitive alphadefensins with end-to-end circularized structures. J. Biol. Chem. 275:3943-3949.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3943-3949
    • Yu, Q.1    Lehrer, R.I.2    Tam, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.