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Volumn 35, Issue 2, 2013, Pages 106-114

Broad activity against porcine bacterial pathogens displayed by two insect antimicrobial peptides moricin and cecropin B

Author keywords

antimicrobial peptide; cecropin B; Haemophilus parasuis SH 0165; moricin; transmission electron microscopy

Indexed keywords

CECROPIN B; MORICIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 84879675951     PISSN: 10168478     EISSN: 02191032     Source Type: Journal    
DOI: 10.1007/s10059-013-2132-0     Document Type: Article
Times cited : (46)

References (36)
  • 1
    • 0037362455 scopus 로고    scopus 로고
    • Ascaris nematodes from pig and human make three antibacterial peptides: Isolation of cecropin P1 and two ASABF peptides
    • 12737319 10.1007/s000180300051 1:CAS:528:DC%2BD3sXjsFGitLY%3D
    • Andersson, M., Boman, A., and Boman, H. (2003). Ascaris nematodes from pig and human make three antibacterial peptides: isolation of cecropin P1 and two ASABF peptides. Cell. Mol. Life Sci. 60, 599-606.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 599-606
    • Andersson, M.1    Boman, A.2    Boman, H.3
  • 2
    • 0001564983 scopus 로고
    • Cell-free immunity in insects
    • 10.1016/0968-0004(81)90109-2 1:CAS:528:DyaL38XltVCqtg%3D%3D
    • Boman, H.G., and Hultmark, D. (1981). Cell-free immunity in insects. Trends Biochem. Sci. 6, 306-309.
    • (1981) Trends Biochem. Sci. , vol.6 , pp. 306-309
    • Boman, H.G.1    Hultmark, D.2
  • 3
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • 15703760 10.1038/nrmicro1098 1:CAS:528:DC%2BD2MXhslGjtbo%3D
    • Brogden, K.A. (2005). Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3, 238-250.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 4
    • 79955944259 scopus 로고    scopus 로고
    • Zinc resistance of Staphylococcus aureus of animal origin is strongly associated with methicillin resistance
    • 21411247 10.1016/j.vetmic.2011.02.014 1:CAS:528:DC%2BC3MXmtFyrs70%3D
    • Cavaco, L.M., Hasman, H., and Aarestrup, F.M. (2011). Zinc resistance of Staphylococcus aureus of animal origin is strongly associated with methicillin resistance. Vet. Microbiol. 150, 344-348.
    • (2011) Vet. Microbiol. , vol.150 , pp. 344-348
    • Cavaco, L.M.1    Hasman, H.2    Aarestrup, F.M.3
  • 5
    • 0242665328 scopus 로고    scopus 로고
    • Transmission electron microscopic observations of membrane effects of antibiotic cecropin B on Escherichia coli
    • 14601148 10.1002/jemt.10406 1:CAS:528:DC%2BD3sXhtVSjsbbF
    • Chen, H.M., Chan, S.C., Lee, J.C., Chang, C.C., Murugan, M., and Jack, R.W. (2003). Transmission electron microscopic observations of membrane effects of antibiotic cecropin B on Escherichia coli. Microsc. Res. Tech. 62, 423-430.
    • (2003) Microsc. Res. Tech. , vol.62 , pp. 423-430
    • Chen, H.M.1    Chan, S.C.2    Lee, J.C.3    Chang, C.C.4    Murugan, M.5    Jack, R.W.6
  • 6
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • 2455891 10.1073/pnas.85.14.5072 1:CAS:528:DyaL1cXls1Grs7Y%3D
    • Christensen, B., Fink, J., Merrifield, R., and Mauzerall, D. (1988). Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Nat. Acad. Sci. USA 85, 5072-5076.
    • (1988) Proc. Nat. Acad. Sci. USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.3    Mauzerall, D.4
  • 7
    • 0027101951 scopus 로고
    • Modeling the ion channel structure of cecropin
    • 1283347 10.1016/S0006-3495(92)81730-7 1:CAS:528:DyaK3sXhs1Smtrw%3D
    • Durell, S.R., Raghunathan, G., and Guy, H.R. (1992). Modeling the ion channel structure of cecropin. Biophys. J. 63, 1623-1631.
    • (1992) Biophys. J. , vol.63 , pp. 1623-1631
    • Durell, S.R.1    Raghunathan, G.2    Guy, H.R.3
  • 8
    • 0000249015 scopus 로고
    • Insect immunity: Inducible antibacterial activity in Drosophila
    • 10.1016/0020-1790(87)90155-7 1:CAS:528:DyaL2sXjtFaktA%3D%3D
    • Flyg, C., Dalhammar, G., Rasmuson, B., and Boman, H.G. (1987). Insect immunity: inducible antibacterial activity in Drosophila. Insect Biochem. 17, 153-160.
    • (1987) Insect Biochem. , vol.17 , pp. 153-160
    • Flyg, C.1    Dalhammar, G.2    Rasmuson, B.3    Boman, H.G.4
  • 9
    • 34250892580 scopus 로고    scopus 로고
    • Prevalence, distribution and characterisation of ceftiofur resistance in Salmonella enterica isolated from animals in the USA from 1999 to 2003
    • 17531447 10.1016/j.ijantimicag.2007.03.013 1:CAS:528:DC%2BD2sXntFart7w%3D
    • Frye, J.G., and Fedorka-Cray, P.J. (2007). Prevalence, distribution and characterisation of ceftiofur resistance in Salmonella enterica isolated from animals in the USA from 1999 to 2003. Int. J. Antimicrob. Agents 30, 134-142.
    • (2007) Int. J. Antimicrob. Agents , vol.30 , pp. 134-142
    • Frye, J.G.1    Fedorka-Cray, P.J.2
  • 10
    • 0029111532 scopus 로고
    • Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipids vesicles
    • 7547876 10.1021/bi00036a021 1:CAS:528:DyaK2MXns1Cisro%3D
    • Gazit, E., Boman, A., Boman, H.G., and Shai, Y. (1995). Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipids 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
  • 11
    • 77951212665 scopus 로고    scopus 로고
    • Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis
    • 20187872 10.1042/BJ20091607 1:CAS:528:DC%2BC3cXkvFemu7w%3D
    • Hammer, M.U., Brauser, A., Olak, C., Brezesinski, G., Goldmann, T., Gutsmann, T., and Andrä, J. (2010). Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis. Biochem. J. 427, 477-488.
    • (2010) Biochem. J. , vol.427 , pp. 477-488
    • Hammer, M.U.1    Brauser, A.2    Olak, C.3    Brezesinski, G.4    Goldmann, T.5    Gutsmann, T.6    Andrä, J.7
  • 12
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • 11814654 10.1111/j.1574-6968.2002.tb11000.x 1:CAS:528: DC%2BD38Xos1Ontg%3D%3D
    • Hancock, R.E.W., and Rozek, A. (2002). Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 206, 143-149.
    • (2002) FEMS Microbiol. Lett. , vol.206 , pp. 143-149
    • Hancock, R.E.W.1    Rozek, A.2
  • 13
    • 0029051008 scopus 로고
    • A novel antibacterial peptide family isolated from the silkworm, Bombyx mori
    • 7654207 1:CAS:528:DyaK2MXnvVKit74%3D
    • Hara, S., and Yamakawa, M. (1995a). A novel antibacterial peptide family isolated from the silkworm, Bombyx mori. Biochem. J. 310 651-656.
    • (1995) Biochem. J. , vol.310 , pp. 651-656
    • Hara, S.1    Yamakawa, M.2
  • 14
    • 0029609285 scopus 로고
    • Moricin, a novel type of antibacterial peptide isolated from the silkworm, Bombyx mori
    • 8530391 10.1074/jbc.270.50.29923 1:CAS:528:DyaK2MXhtVSitbjO
    • Hara, S., and Yamakawa, M. (1995b). Moricin, a novel type of antibacterial peptide isolated from the silkworm, Bombyx mori. J. Biol. Chem. 270, 29923-29927.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29923-29927
    • Hara, S.1    Yamakawa, M.2
  • 15
    • 77955377305 scopus 로고    scopus 로고
    • Damage of bacterial cell envelope by antimicrobial peptides Gramicidin S and PGLa as revealed by transmission and scanning electron microscopy
    • 10.1128/AAC.00124-10 1:CAS:528:DC%2BC3cXhtVOms7nL
    • Hartmann, M., Berditsch, M., Hawecker, J., Ardakani, M.F., Gerthsen, D., and Ulrich, A.S. (2010). Damage of bacterial cell envelope by antimicrobial peptides Gramicidin S and PGLa as revealed by transmission and scanning electron microscopy. Antimicro. Agents Chemother. 54, 3132-3142.
    • (2010) Antimicro. Agents Chemother. , vol.54 , pp. 3132-3142
    • Hartmann, M.1    Berditsch, M.2    Hawecker, J.3    Ardakani, M.F.4    Gerthsen, D.5    Ulrich, A.S.6
  • 16
    • 0037042209 scopus 로고    scopus 로고
    • Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori
    • 11997013 10.1016/S0014-5793(02)02637-6 1:CAS:528:DC%2BD38XjsVSku7c%3D
    • Hemmi, H., Ishibashi, J., Hara, S., and Yamakawa, M. (2002). Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori. FEBS Lett. 518, 33-38.
    • (2002) FEBS Lett. , vol.518 , pp. 33-38
    • Hemmi, H.1    Ishibashi, J.2    Hara, S.3    Yamakawa, M.4
  • 17
    • 0018820115 scopus 로고
    • Insect immunity: Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • 7341234 10.1111/j.1432-1033.1980.tb05991.x 1:CAS:528:DyaL3cXktVGrt7w%3D
    • Hultmark, D., Steiner, H., Rasmuson, T., and Boman, H.G. (1980). Insect immunity: purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur. J. Biochem. 106, 7-16.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 18
    • 0020366780 scopus 로고
    • Insect immunity: Isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae
    • 7140755 10.1111/j.1432-1033.1982.tb06857.x 1:CAS:528:DyaL38XmtFCjtr0%3D
    • Hultmark, D., Engström, Å., Bennich, H., Kapur, R., and Boman, H.G. (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    Engström2    Bennich, H.3    Kapur, R.4    Boman, H.G.5
  • 19
    • 33748948410 scopus 로고    scopus 로고
    • Insertion selectivity of antimicrobial peptide protegrin-1 into lipid monolayers: Effect of head group electrostatics and tail group packing
    • 10.1016/j.bbamem.2006.08.001 1:CAS:528:DC%2BD28XhtVanu7fN
    • Ishitsuka, Y., Pham, D.S., Waring, A.J., Lehrer, R.I., and Lee, K.Y.C. (2006). Insertion selectivity of antimicrobial peptide protegrin-1 into lipid monolayers: effect of head group electrostatics and tail group packing. Biochim. Biophys. Acta (BBA)-Biomembranes 1758, 1450-1460.
    • (2006) Biochim. Biophys. Acta (BBA)-Biomembranes , vol.1758 , pp. 1450-1460
    • Ishitsuka, Y.1    Pham, D.S.2    Waring, A.J.3    Lehrer, R.I.4    Lee, K.Y.C.5
  • 20
    • 75749101436 scopus 로고    scopus 로고
    • Expression of a synthesized gene encoding cationic peptide cecropin B in transgenic tomato plants protects against bacterial diseases
    • 10.1128/AEM.00698-09 1:CAS:528:DC%2BC3cXisVCjsL4%3D
    • Jan, P.S., Huang, H.Y., and Chen, H.M. (2010). Expression of a synthesized gene encoding cationic peptide cecropin B in transgenic tomato plants protects against bacterial diseases. Appl. Environ. Microb. 76, 769-775.
    • (2010) Appl. Environ. Microb. , vol.76 , pp. 769-775
    • Jan, P.S.1    Huang, H.Y.2    Chen, H.M.3
  • 21
    • 33746532309 scopus 로고    scopus 로고
    • Peptide antimicrobial agents
    • 16847082 10.1128/CMR.00056-05 1:CAS:528:DC%2BD28XosVaqsrk%3D
    • Jenssen, H., Hamill, P., and Hancock, R.E.W. (2006). Peptide antimicrobial agents. Clin. Microbiol. Rev. 19, 491-511.
    • (2006) Clin. Microbiol. Rev. , vol.19 , pp. 491-511
    • Jenssen, H.1    Hamill, P.2    Hancock, R.E.W.3
  • 22
    • 77956036047 scopus 로고    scopus 로고
    • Characterization and cDNA cloning of a cecropin-like antimicrobial peptide, papiliocin, from the swallowtail butterfly, Papilio xuthus
    • 20213310 10.1007/s10059-010-0050-y 1:CAS:528:DC%2BC3cXlsVCrtbw%3D
    • Kim, S.R., Hong, M.Y., Park, S.W., Choi, K.H., Yun, E.Y., Goo, T.W., Kang, S.W., Suh, H.J., Kim, I., and Hwang, J.S. (2010). Characterization and cDNA cloning of a cecropin-like antimicrobial peptide, papiliocin, from the swallowtail butterfly, Papilio xuthus. Mol. Cells 29, 419-423.
    • (2010) Mol. Cells , vol.29 , pp. 419-423
    • Kim, S.R.1    Hong, M.Y.2    Park, S.W.3    Choi, K.H.4    Yun, E.Y.5    Goo, T.W.6    Kang, S.W.7    Suh, H.J.8    Kim, I.9    Hwang, J.S.10
  • 23
    • 84894904956 scopus 로고    scopus 로고
    • Prevalence and antimicrobial resistance of Salmonella spp. and Escherichia coli isolated from pigs at slaughterhouses in Korea
    • Kim, H.B., Baek, H., Lee, S.J., Jang, Y.H., Jung, S.C., Kim, A., and Choe, N.H. (2011). Prevalence and antimicrobial resistance of Salmonella spp. and Escherichia coli isolated from pigs at slaughterhouses in Korea. Afr. J. Microbiol. Res. 5, 823-830.
    • (2011) Afr. J. Microbiol. Res. , vol.5 , pp. 823-830
    • Kim, H.B.1    Baek, H.2    Lee, S.J.3    Jang, Y.H.4    Jung, S.C.5    Kim, A.6    Choe, N.H.7
  • 24
    • 22244480342 scopus 로고    scopus 로고
    • Structure-activity relation of human β-defensin 3: Influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity
    • 16008365 10.1021/bi050272k
    • Klüver, E., Schulz-Maronde, S., Scheid, S., Meyer, B., Forssmann, W.G., and Adermann, K. (2005). Structure-activity relation of human β-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity. Biochemistry 44, 9804-9816.
    • (2005) Biochemistry , vol.44 , pp. 9804-9816
    • Klüver, E.1    Schulz-Maronde, S.2    Scheid, S.3    Meyer, B.4    Forssmann, W.G.5    Adermann, K.6
  • 25
    • 0028695274 scopus 로고
    • Antimicrobial peptides from amphibian skin: An overview
    • 7768159 1:CAS:528:DyaK28XmtFGgtQ%3D%3D
    • Kreil, G. (1994). Antimicrobial peptides from amphibian skin: an overview. Ciba Found. Symp. 186, 77-85.
    • (1994) Ciba Found. Symp. , vol.186 , pp. 77-85
    • Kreil, G.1
  • 26
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis. l. The synthesis of a tetrapeptide
    • 10.1021/ja00897a025 1:CAS:528:DyaF3sXksVajsLg%3D
    • Merrifield, R.B. (1963). Solid phase peptide synthesis. l. The synthesis of a tetrapeptide. J. Am. Chem. Soc. 85, 2149-2154.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 2149-2154
    • Merrifield, R.B.1
  • 27
    • 23944464883 scopus 로고    scopus 로고
    • Isolation, gene expression and solution structure of a novel moricin analogue, antibacterial peptide from a lepidop-teran insect, Spodoptera litura
    • 16115804 10.1016/j.bbapap.2005.07.013 1:CAS:528:DC%2BD2MXptVWnu7s%3D
    • Oizumi, Y., Hemmi, H., Minami, M., Asaoka, A., and Yamakawa, M. (2005). Isolation, gene expression and solution structure of a novel moricin analogue, antibacterial peptide from a lepidop-teran insect, Spodoptera litura. Biochim. Biophys. Acta 1752, 83-92.
    • (2005) Biochim. Biophys. Acta , vol.1752 , pp. 83-92
    • Oizumi, Y.1    Hemmi, H.2    Minami, M.3    Asaoka, A.4    Yamakawa, M.5
  • 28
    • 0037437054 scopus 로고    scopus 로고
    • Bactericidal activity of cecro pin B and cecropin P 1 expressed in fish cells (CHSE-214): Application in controlling fish bacterial pathogens
    • 10.1016/S0044-8486(02)00634-8 1:CAS:528:DC%2BD3sXitFagurk%3D
    • Sarmasik, A., and Chen, T.T. (2003). Bactericidal activity of cecro pin B and cecropin P 1 expressed in fish cells (CHSE-214): application in controlling fish bacterial pathogens. Aquaculture 220, 183-194.
    • (2003) Aquaculture , vol.220 , pp. 183-194
    • Sarmasik, A.1    Chen, T.T.2
  • 29
    • 33749012269 scopus 로고    scopus 로고
    • Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic α-helical antimicrobial peptides
    • 16697975 10.1016/j.bbamem.2006.02.021 1:CAS:528:DC%2BD28XhtVanu7vI
    • Sato, H., and Feix, J.B. (2006). Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic α-helical antimicrobial peptides. Biochim. Biophys. Acta 1758, 1245-1256.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1245-1256
    • Sato, H.1    Feix, J.B.2
  • 31
    • 0020039463 scopus 로고
    • Secondary structure of the cecropins: Antibacterial peptides from the moth Hyalophora cecropia
    • 15768483 10.1016/0014-5793(82)80368-2 1:CAS:528:DyaL38XhslKnsL4%3D
    • Steiner, H. (1982). Secondary structure of the cecropins: antibacterial peptides from the moth Hyalophora cecropia. FEBS Lett. 137, 283-287.
    • (1982) FEBS Lett. , vol.137 , pp. 283-287
    • Steiner, H.1
  • 32
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects
    • 3128324 10.1016/0005-2736(88)90069-7 1:CAS:528:DyaL1cXktVGju7Y%3D
    • Steiner, H., Andreu, D., and Merrifield, R.B. (1988). Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim. Biophys. Acta 939, 260-266.
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 34
    • 84857646338 scopus 로고    scopus 로고
    • Antimicrobial Resistance of Actinobacillus Pleuropneumoniae Isolated from Swine
    • 22104584 10.1016/j.vetmic.2011.10.022
    • Vanni, M., Merenda, M., Barigazzi, G., Garbarino, C., Luppi, A., Tognetti, R., and Intorre, L. (2011). Antimicrobial Resistance of Actinobacillus Pleuropneumoniae Isolated from Swine. Vet. Microbiol. 156, 172-177.
    • (2011) Vet. Microbiol. , vol.156 , pp. 172-177
    • Vanni, M.1    Merenda, M.2    Barigazzi, G.3    Garbarino, C.4    Luppi, A.5    Tognetti, R.6    Intorre, L.7
  • 35
    • 34548290744 scopus 로고    scopus 로고
    • Porcine β-defensin 2 displays broad antimicrobial activity against pathogenic intestinal bacteria
    • 17658606 10.1016/j.molimm.2007.06.001 1:CAS:528:DC%2BD2sXpslOltLY%3D
    • Veldhuizen, E.J.A., Rijnders, M., Claassen, E.A., Van Dijk, A., and Haagsman, H.P. (2008). Porcine β-defensin 2 displays broad antimicrobial activity against pathogenic intestinal bacteria. Mol. Immunol. 45, 386-394.
    • (2008) Mol. Immunol. , vol.45 , pp. 386-394
    • Veldhuizen, E.J.A.1    Rijnders, M.2    Claassen, E.A.3    Van Dijk, A.4    Haagsman, H.P.5


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