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Volumn 1788, Issue 11, 2009, Pages 2411-2420

Structure-function study of cathelicidin-derived bovine antimicrobial peptide BMAP-28: Design of its cell-selective analogs by amino acid substitutions in the heptad repeat sequences

Author keywords

Antimicrobial and toxic activity; Antimicrobial peptide; Leucine zipper motif; Localization of antimicrobial peptides onto bacterial and mammalian cells; Peptide membrane interaction

Indexed keywords

CATHELICIDIN; ISOLEUCINE; LEUCINE; MELITTIN; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN BMAP 28; UNCLASSIFIED DRUG;

EID: 71149113168     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.08.021     Document Type: Article
Times cited : (40)

References (43)
  • 1
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman H.G. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13 (1995) 61-92
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 2
    • 0036218636 scopus 로고    scopus 로고
    • Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity
    • Ramanathan B., Davis E.G., Ross C.R., and Blecha F. Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity. Microbes Infect. 4 (2002) 361-372
    • (2002) Microbes Infect. , vol.4 , pp. 361-372
    • Ramanathan, B.1    Davis, E.G.2    Ross, C.R.3    Blecha, F.4
  • 3
    • 0027474382 scopus 로고
    • Defensins: antimicrobial and cytotoxic peptides of mammalian cells
    • Lehrer R.I., Lichtenstein A.K., and Ganz T. Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11 (1993) 105-128
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 4
    • 0028844134 scopus 로고
    • Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M., Gennaro R., and Romeo D. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374 (1995) 1-5
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 5
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: effectors in innate immunity and novel antimicrobials
    • Hancock R.E. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 1 (2001) 156-164
    • (2001) Lancet Infect. Dis. , vol.1 , pp. 156-164
    • Hancock, R.E.1
  • 6
    • 0025066842 scopus 로고
    • Rapid membrane permeabilization and inhibition of vital functions of Gram-negative bacteria by bactenecins
    • Skerlavaj B., Romeo D., and Gennaro R. Rapid membrane permeabilization and inhibition of vital functions of Gram-negative bacteria by bactenecins. Infect. Immun. 58 (1990) 3724-3730
    • (1990) Infect. Immun. , vol.58 , pp. 3724-3730
    • Skerlavaj, B.1    Romeo, D.2    Gennaro, R.3
  • 7
    • 0033664277 scopus 로고    scopus 로고
    • Leukocyte antimicrobial peptides: multifunctional effector molecules of innate immunity
    • Risso A. Leukocyte antimicrobial peptides: multifunctional effector molecules of innate immunity. J. Leukoc. Biol. 68 (2000) 785-792
    • (2000) J. Leukoc. Biol. , vol.68 , pp. 785-792
    • Risso, A.1
  • 8
    • 0023746603 scopus 로고
    • Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils
    • Romeo D., Skerlavaj B.M., Bolognesi M., and Gennaro R.J. Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J. Biol. Chem. 263 (1988) 9573-9575
    • (1988) J. Biol. Chem. , vol.263 , pp. 9573-9575
    • Romeo, D.1    Skerlavaj, B.M.2    Bolognesi, M.3    Gennaro, R.J.4
  • 9
    • 0024460671 scopus 로고
    • Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils
    • Gennaro R., Skerlavaj B., and Romeo D. Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils. Infect. Immun. 57 (1989) 3142-3146
    • (1989) Infect. Immun. , vol.57 , pp. 3142-3146
    • Gennaro, R.1    Skerlavaj, B.2    Romeo, D.3
  • 10
    • 0027472180 scopus 로고
    • The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics
    • Zanetti M., Del Sal G., Storici P., Schneider C., and Romeo D. The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics. J. Biol. Chem. 268 (1993) 522-526
    • (1993) J. Biol. Chem. , Issue.268 , pp. 522-526
    • Zanetti, M.1    Del Sal, G.2    Storici, P.3    Schneider, C.4    Romeo, D.5
  • 11
    • 0036135697 scopus 로고    scopus 로고
    • Cathelicidins: a family of endogenous antimicrobial peptides
    • Lehrer R.I., and Ganz T. Cathelicidins: a family of endogenous antimicrobial peptides. Curr. Opin. Hematol. 9 (2002) 18-22
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 18-22
    • Lehrer, R.I.1    Ganz, T.2
  • 12
    • 0033863168 scopus 로고    scopus 로고
    • Structural features and biological activities of the cathelicidin-derived antimicrobial peptides
    • Gennaro R., and Zanetti M. Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers 55 (2000) 31-49
    • (2000) Biopolymers , Issue.55 , pp. 31-49
    • Gennaro, R.1    Zanetti, M.2
  • 13
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 75 (2004) 39-48
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 14
    • 0029129210 scopus 로고
    • Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39
    • Gudmundsson G.H., Magnusson K.P., Chowdhary B.P., Johansson M., Andersson L., and Boman H.G. Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 7085-7089
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , Issue.92 , pp. 7085-7089
    • Gudmundsson, G.H.1    Magnusson, K.P.2    Chowdhary, B.P.3    Johansson, M.4    Andersson, L.5    Boman, H.G.6
  • 15
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 393-395
    • (2002) Nature , vol.415 , pp. 393-395
    • Zasloff, M.1
  • 16
    • 2542480000 scopus 로고    scopus 로고
    • Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense
    • Yang D., Biragyn A., Hoover D.M., Lubkowski J., and Oppenheim J.J. Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annu. Rev. Immunol. 22 (2004) 181-215
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 181-215
    • Yang, D.1    Biragyn, A.2    Hoover, D.M.3    Lubkowski, J.4    Oppenheim, J.J.5
  • 18
    • 0031574103 scopus 로고    scopus 로고
    • The cathelicidin family of antimicrobial peptide precursors: a component of the oxygen-independent defense mechanisms of neutrophils
    • Zanetti M., Gennaro R., and Romeo D. The cathelicidin family of antimicrobial peptide precursors: a component of the oxygen-independent defense mechanisms of neutrophils. Ann. N. Y. Acad. Sci. 883 (1997) 147-162
    • (1997) Ann. N. Y. Acad. Sci. , vol.883 , pp. 147-162
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 19
    • 0036929153 scopus 로고    scopus 로고
    • Comparative in vitro activity of five cathelicidin-derived synthetic peptides against Leptospira, Borrelia and Treponema pallidum
    • Sambri V., Marangon A., Giacani L., Gennaro R., Murgia R., Cevenini R., and Cinco M. Comparative in vitro activity of five cathelicidin-derived synthetic peptides against Leptospira, Borrelia and Treponema pallidum. J. Antimicrob. Chemother. 50 (2002) 895-902
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 895-902
    • Sambri, V.1    Marangon, A.2    Giacani, L.3    Gennaro, R.4    Murgia, R.5    Cevenini, R.6    Cinco, M.7
  • 20
    • 0029961492 scopus 로고    scopus 로고
    • Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities
    • Skerlavaj B., Gennaro R., Bagella L., Merluzzi L., Risso A., and Zanetti M. Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities. J. Biol. Chem. 271 (1996) 28375-28381
    • (1996) J. Biol. Chem. , vol.271 , pp. 28375-28381
    • Skerlavaj, B.1    Gennaro, R.2    Bagella, L.3    Merluzzi, L.4    Risso, A.5    Zanetti, M.6
  • 21
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study
    • Oren Z., and Shai Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry 36 (1997) 1826-1835
    • (1997) Biochemistry , vol.36 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 22
    • 0024841875 scopus 로고
    • Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids
    • Boman H.G., Wade D., Boman I.A., Wåhlin B., and Merrifield R.B. Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids. FEBS Lett. 259 (1989) 103-106
    • (1989) FEBS Lett. , vol.259 , pp. 103-106
    • Boman, H.G.1    Wade, D.2    Boman, I.A.3    Wåhlin, B.4    Merrifield, R.B.5
  • 23
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen Y., Mant C.T., Farmer S.W., Hancock R.E., Vasil M.L., and Hodges R.S. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J. Biol. Chem. 280 (2005) 12316-12329
    • (2005) J. Biol. Chem. , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 24
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • Hilpert K., Volkmer-Engert R., Walter T., and Hancock R.E. High-throughput generation of small antibacterial peptides with improved activity. Nat. Biotechnol. 23 (2005) 1008-1012
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.4
  • 25
    • 0033616105 scopus 로고    scopus 로고
    • De novo design of antibacterial β-peptides
    • Hamuro Y., Schneider J.P., and DeGrado W.F. De novo design of antibacterial β-peptides. J. Am. Chem. Soc 121 (1999) 12200-12201
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 12200-12201
    • Hamuro, Y.1    Schneider, J.P.2    DeGrado, W.F.3
  • 26
    • 33750446295 scopus 로고    scopus 로고
    • Ultrashort antibacterial and antifungal lipopeptides
    • Makovitzki, Avrahami D., and Shai Y. Ultrashort antibacterial and antifungal lipopeptides. PNAS 103 (2006) 15997-16002
    • (2006) PNAS , vol.103 , pp. 15997-16002
    • Makovitzki1    Avrahami, D.2    Shai, Y.3
  • 28
    • 11244272784 scopus 로고    scopus 로고
    • Dissection of antibacterial and toxic activity of melittin: a leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity
    • Asthana N., Yadav S.P., and Ghosh J.K. Dissection of antibacterial and toxic activity of melittin: a leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity. J. Biol. Chem. 279 (2004) 55042-55050
    • (2004) J. Biol. Chem. , vol.279 , pp. 55042-55050
    • Asthana, N.1    Yadav, S.P.2    Ghosh, J.K.3
  • 29
    • 0347065360 scopus 로고    scopus 로고
    • Identification and characterization of an amphipathic leucine zipper-like motif in Escherichia coli toxin hemolysin E. Plausible role in the assembly and membrane destabilization
    • Yadav S.P., Kundu B., and Ghosh J.K. Identification and characterization of an amphipathic leucine zipper-like motif in Escherichia coli toxin hemolysin E. Plausible role in the assembly and membrane destabilization. J. Biol. Chem. 278 (2003) 51023-51034
    • (2003) J. Biol. Chem. , vol.278 , pp. 51023-51034
    • Yadav, S.P.1    Kundu, B.2    Ghosh, J.K.3
  • 30
    • 33746807690 scopus 로고    scopus 로고
    • Utilization of an amphipathic leucine zipper sequence to design antibacterial peptides with simultaneous modulation of toxic activity against human red blood cells
    • Ahmad A., Yadav S.P., Asthana N., Mitra K., Srivastava S.P., and Ghosh J.K. Utilization of an amphipathic leucine zipper sequence to design antibacterial peptides with simultaneous modulation of toxic activity against human red blood cells. J. Biol. Chem. 281 (2006) 22029-22038
    • (2006) J. Biol. Chem. , vol.281 , pp. 22029-22038
    • Ahmad, A.1    Yadav, S.P.2    Asthana, N.3    Mitra, K.4    Srivastava, S.P.5    Ghosh, J.K.6
  • 31
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields G.B., and Noble R.L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pep. Prot. Res. 35 (1990) 161-214
    • (1990) Int. J. Pep. Prot. Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 33
    • 4143110396 scopus 로고    scopus 로고
    • Suppression of human prostate tumor growth in mice by a cytolytic d-, l-amino acid peptide: membrane lysis, increased necrosis, and inhibition of prostate-specific antigen secretion
    • Papo N., Braunstein A., Eshhar Z., and Shai Y. Suppression of human prostate tumor growth in mice by a cytolytic d-, l-amino acid peptide: membrane lysis, increased necrosis, and inhibition of prostate-specific antigen secretion. Cancer Res. 64 (2004) 5779-5786
    • (2004) Cancer Res. , vol.64 , pp. 5779-5786
    • Papo, N.1    Braunstein, A.2    Eshhar, Z.3    Shai, Y.4
  • 34
    • 39649103630 scopus 로고    scopus 로고
    • Inhibition of lytic activity of E. coli toxin hemolysin E against human red blood cells by a leucine zipper peptide and understanding the underlying mechanism
    • Yadav S.P., Ahmad A., Pandey B.K., Verma R., and Ghosh J.K. Inhibition of lytic activity of E. coli toxin hemolysin E against human red blood cells by a leucine zipper peptide and understanding the underlying mechanism. Biochemistry 47 (2008) 2134-2142
    • (2008) Biochemistry , vol.47 , pp. 2134-2142
    • Yadav, S.P.1    Ahmad, A.2    Pandey, B.K.3    Verma, R.4    Ghosh, J.K.5
  • 35
    • 0030020463 scopus 로고    scopus 로고
    • Detection of altered membrane phospholipid asymmetry in subpopulations of human red blood cells using fluorescently labeled annexin V
    • Kuypers F.A., Lewis R.A., Hua M., Schott M.A., Discher D., Ernst J.D., and Lubin B.H. Detection of altered membrane phospholipid asymmetry in subpopulations of human red blood cells using fluorescently labeled annexin V. Blood 87 (1996) 1179-1187
    • (1996) Blood , vol.87 , pp. 1179-1187
    • Kuypers, F.A.1    Lewis, R.A.2    Hua, M.3    Schott, M.A.4    Discher, D.5    Ernst, J.D.6    Lubin, B.H.7
  • 36
    • 34249042323 scopus 로고    scopus 로고
    • Addition of a small hydrophobic segment from the head region to an amphipathic leucine zipper like motif of E. coli toxin hemolysin E enhances the peptide-induced permeability of zwitterionic lipid vesicles
    • Yadav S.P., Ahmad A., and Ghosh J.K. Addition of a small hydrophobic segment from the head region to an amphipathic leucine zipper like motif of E. coli toxin hemolysin E enhances the peptide-induced permeability of zwitterionic lipid vesicles. Biochim. Biophys. Acta 1768 (2007) 1574-1582
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1574-1582
    • Yadav, S.P.1    Ahmad, A.2    Ghosh, J.K.3
  • 37
    • 0141706347 scopus 로고    scopus 로고
    • Redefining cholesterol's role in the mechanism of the cholesterol dependent cytolysins
    • Giddings K.S., Johnson A.E., and Tweten R.K. Redefining cholesterol's role in the mechanism of the cholesterol dependent cytolysins. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 11315-11320
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 11315-11320
    • Giddings, K.S.1    Johnson, A.E.2    Tweten, R.K.3
  • 38
    • 33845461993 scopus 로고    scopus 로고
    • Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures
    • Schibli D.J., Nguyen L.T., Kernaghan S.D., Rekdal Ø., and Vogel H.J. Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures. Biophys. J. 91 (2006) 4413-4426
    • (2006) Biophys. J. , vol.91 , pp. 4413-4426
    • Schibli, D.J.1    Nguyen, L.T.2    Kernaghan, S.D.3    Rekdal, Ø.4    Vogel, H.J.5
  • 39
    • 0036389644 scopus 로고    scopus 로고
    • Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide
    • Yang S.T., Shin S.Y., Kim Y.C., Kim Y., Hahm K.S., and Kim J.I. Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide. Biochem. Biophys. Res. Commun. 296 (2002) 1044-1050
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 1044-1050
    • Yang, S.T.1    Shin, S.Y.2    Kim, Y.C.3    Kim, Y.4    Hahm, K.S.5    Kim, J.I.6
  • 40
    • 0030583546 scopus 로고    scopus 로고
    • Requirements for antibacterial and hemolytic activities in the bovine neutrophil derived 13-residue peptide indolicidin
    • Subbalakshmi C., Krishnakumari V., Nagaraj R., and Sitaram N. Requirements for antibacterial and hemolytic activities in the bovine neutrophil derived 13-residue peptide indolicidin. FEBS Lett. 395 (1996) 48-52
    • (1996) FEBS Lett. , vol.395 , pp. 48-52
    • Subbalakshmi, C.1    Krishnakumari, V.2    Nagaraj, R.3    Sitaram, N.4
  • 41
    • 0035968224 scopus 로고    scopus 로고
    • Structure and mechanism of action of an indolicidin peptide derivative with improved activity against Gram-positive bacteria
    • Friedrich C.L., Rozek A., Patrzykat A., and Hancock R.E.W. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against Gram-positive bacteria. J. Biol. Chem. 276 (2001) 24015-24022
    • (2001) J. Biol. Chem. , vol.276 , pp. 24015-24022
    • Friedrich, C.L.1    Rozek, A.2    Patrzykat, A.3    Hancock, R.E.W.4
  • 42
    • 49649110753 scopus 로고    scopus 로고
    • Probing structure-activity relationships in bactericidal peptide betapep-25
    • Dings R.P., Haseman J.R., and Mayo K.H. Probing structure-activity relationships in bactericidal peptide betapep-25. Biochem. J. 414 (2008) 143-150
    • (2008) Biochem. J. , vol.414 , pp. 143-150
    • Dings, R.P.1    Haseman, J.R.2    Mayo, K.H.3
  • 43
    • 34249070808 scopus 로고    scopus 로고
    • Substitution of the leucine zipper sequence in melittin with peptoid residues affects self-association, cell selectivity, and mode of action
    • Zhu W.L., Song Y.M., Park Y., Park K.H., Yang S.T., Kim J.I., Park I.S., Hahm K.S., and Shin S.Y. Substitution of the leucine zipper sequence in melittin with peptoid residues affects self-association, cell selectivity, and mode of action. Biochim. Biophys. Acta 1768 (2007) 1506-1517
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1506-1517
    • Zhu, W.L.1    Song, Y.M.2    Park, Y.3    Park, K.H.4    Yang, S.T.5    Kim, J.I.6    Park, I.S.7    Hahm, K.S.8    Shin, S.Y.9


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