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Volumn 9, Issue 2, 2014, Pages 405-413

An insect defensin-derived β-hairpin peptide with enhanced antibacterial activity

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BETA HAIRPIN PEPTIDE; CYSTEINE; DEFENSIN; INSECT PROTEIN; NAVIDEFENSIN2 2; PHENYLALANINE; PROPIDIUM IODIDE; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; VANCOMYCIN;

EID: 84896735396     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb400591d     Document Type: Article
Times cited : (26)

References (44)
  • 1
    • 0032411402 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides in invertebrates
    • Dimarcq, J. L., Bulet, P., Hetru, C., and Hoffmann, J. (1998) Cysteine-rich antimicrobial peptides in invertebrates Biopolymers 47, 465-477
    • (1998) Biopolymers , vol.47 , pp. 465-477
    • Dimarcq, J.L.1    Bulet, P.2    Hetru, C.3    Hoffmann, J.4
  • 2
    • 0036747342 scopus 로고    scopus 로고
    • Reverse genetics in the mosquito Anopheles gambiae: Targeted disruption of the defensin gene
    • Blandin, S., Moita, L. F., Köcher, T., Wilm, M., Kafatos, F., and Levashina, E. A. (2002) Reverse genetics in the mosquito Anopheles gambiae: targeted disruption of the defensin gene EMBO Rep. 3, 852-856
    • (2002) EMBO Rep. , vol.3 , pp. 852-856
    • Blandin, S.1    Moita, L.F.2    Köcher, T.3    Wilm, M.4    Kafatos, F.5    Levashina, E.A.6
  • 3
    • 0023692422 scopus 로고
    • Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina
    • Matsuyama, K. and Natori, S. (1988) Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina J. Biol. Chem. 263, 17112-17116
    • (1988) J. Biol. Chem. , vol.263 , pp. 17112-17116
    • Matsuyama, K.1    Natori, S.2
  • 5
    • 33845673319 scopus 로고    scopus 로고
    • Evolutionary selective trends of insect/mosquito antimicrobial defensin peptides containing cysteine-stabilized alpha/beta motifs
    • Dassanayake, R. S., Silva Gunawardene, Y. I., and Tobe, S. S. (2007) Evolutionary selective trends of insect/mosquito antimicrobial defensin peptides containing cysteine-stabilized alpha/beta motifs Peptides 28, 62-75
    • (2007) Peptides , vol.28 , pp. 62-75
    • Dassanayake, R.S.1    Silva Gunawardene, Y.I.2    Tobe, S.S.3
  • 7
    • 77953618671 scopus 로고    scopus 로고
    • Defensin of the zebra mussel (Dreissena polymorpha): Molecular structure, in vitro expression, antimicrobial activity, and potential functions
    • Xu, W. and Faisal, M. (2010) Defensin of the zebra mussel (Dreissena polymorpha): molecular structure, in vitro expression, antimicrobial activity, and potential functions Mol. Immunol. 47, 2138-2147
    • (2010) Mol. Immunol. , vol.47 , pp. 2138-2147
    • Xu, W.1    Faisal, M.2
  • 8
    • 34848836028 scopus 로고    scopus 로고
    • Discovery of six families of fungal defensin-like peptides provides insights into origin and evolution of the CSαβ defensins
    • Zhu, S. (2008) Discovery of six families of fungal defensin-like peptides provides insights into origin and evolution of the CSαβ defensins Mol. Immunol. 45, 828-838
    • (2008) Mol. Immunol. , vol.45 , pp. 828-838
    • Zhu, S.1
  • 10
    • 27144432006 scopus 로고    scopus 로고
    • Phylogenetic distribution, functional epitopes and evolution of the CSαβ superfamily
    • Zhu, S., Gao, B., and Tytgat, J. (2005) Phylogenetic distribution, functional epitopes and evolution of the CSαβ superfamily Cell. Mol. Life Sci. 62, 2257-2269
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2257-2269
    • Zhu, S.1    Gao, B.2    Tytgat, J.3
  • 11
    • 1642545489 scopus 로고    scopus 로고
    • Antimicrobial peptides: From invertebrates to vertebrates
    • Bulet, P., Stöcklin, R., and Menin, L. (2004) Antimicrobial peptides: from invertebrates to vertebrates Immunol. Rev. 198, 169-184
    • (2004) Immunol. Rev. , vol.198 , pp. 169-184
    • Bulet, P.1    Stöcklin, R.2    Menin, L.3
  • 14
    • 44949252130 scopus 로고    scopus 로고
    • Rational design of peptides active against the gram positive bacteria Staphylococcus aureus
    • Landon, C., Barbault, F., Legrain, M., Guenneugues, M., and Vovelle, F. (2008) Rational design of peptides active against the gram positive bacteria Staphylococcus aureus Proteins 72, 229-239
    • (2008) Proteins , vol.72 , pp. 229-239
    • Landon, C.1    Barbault, F.2    Legrain, M.3    Guenneugues, M.4    Vovelle, F.5
  • 15
    • 2442515355 scopus 로고    scopus 로고
    • Multidimensional signatures in antimicrobial peptides
    • Yount, N. Y. and Yeaman, M. R. (2004) Multidimensional signatures in antimicrobial peptides Proc. Natl. Acad. Sci. U.S.A. 101, 7363-7368
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 7363-7368
    • Yount, N.Y.1    Yeaman, M.R.2
  • 17
    • 0032738363 scopus 로고    scopus 로고
    • Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: Solution structure and molecular dynamics simulations in the presence of a lipid monolayer
    • Mandard, N., Sy, D., Maufrais, C., Bonmatin, J. M., Bulet, P., Hetru, C., and Vovelle, F. (1999) Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: solution structure and molecular dynamics simulations in the presence of a lipid monolayer J. Biomol. Struct. Dyn. 17, 367-380
    • (1999) J. Biomol. Struct. Dyn. , vol.17 , pp. 367-380
    • Mandard, N.1    Sy, D.2    Maufrais, C.3    Bonmatin, J.M.4    Bulet, P.5    Hetru, C.6    Vovelle, F.7
  • 18
    • 0036178451 scopus 로고    scopus 로고
    • The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider
    • Mandard, N., Bulet, P., Caille, A., Daffre, S., and Vovelle, F. (2002) The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider Eur. J. Biochem. 269, 1190-1198
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1190-1198
    • Mandard, N.1    Bulet, P.2    Caille, A.3    Daffre, S.4    Vovelle, F.5
  • 19
    • 0037108278 scopus 로고    scopus 로고
    • Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives
    • Laederach, A., Andreotti, A. H., and Fulton, D. B. (2002) Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives Biochemistry 41, 12359-12368
    • (2002) Biochemistry , vol.41 , pp. 12359-12368
    • Laederach, A.1    Andreotti, A.H.2    Fulton, D.B.3
  • 20
    • 77649339897 scopus 로고    scopus 로고
    • Identification and characterization of the parasitic wasp Nasonia defensins: Positive selection targeting the functional region?
    • Gao, B. and Zhu, S. (2010) Identification and characterization of the parasitic wasp Nasonia defensins: positive selection targeting the functional region? Dev. Comp. Immunol. 34, 659-668
    • (2010) Dev. Comp. Immunol. , vol.34 , pp. 659-668
    • Gao, B.1    Zhu, S.2
  • 22
    • 0032528858 scopus 로고    scopus 로고
    • Identification and characterization of the antimicrobial peptide corresponding to C-terminal β-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor
    • Lee, K. H., Hong, S. Y., Oh, J. E., Kwon, M., Yoon, J. H., Lee, J., Lee, B. L., and Moon, H. M. (1998) Identification and characterization of the antimicrobial peptide corresponding to C-terminal β-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor Biochem. J. 334, 99-105
    • (1998) Biochem. J. , vol.334 , pp. 99-105
    • Lee, K.H.1    Hong, S.Y.2    Oh, J.E.3    Kwon, M.4    Yoon, J.H.5    Lee, J.6    Lee, B.L.7    Moon, H.M.8
  • 23
    • 0030178188 scopus 로고    scopus 로고
    • Hydrophobic effects on antibacterial and channel-forming properties of cecropin A-melittin hybrids
    • Juvvadi, P., Vunnam, S., Merrifield, E. L., Boman, H. G., and Merrifield, R. B. (1996) Hydrophobic effects on antibacterial and channel-forming properties of cecropin A-melittin hybrids J. Pept. Sci. 2, 223-232
    • (1996) J. Pept. Sci. , vol.2 , pp. 223-232
    • Juvvadi, P.1    Vunnam, S.2    Merrifield, E.L.3    Boman, H.G.4    Merrifield, R.B.5
  • 24
    • 0030198873 scopus 로고    scopus 로고
    • Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes
    • Fahrner, R. L., Dieckmann, T., Harwig, S. S., Lehrer, R. I., Eisenberg, D., and Feigon, J. (1996) Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes Chem. Biol. 3, 543-550
    • (1996) Chem. Biol. , vol.3 , pp. 543-550
    • Fahrner, R.L.1    Dieckmann, T.2    Harwig, S.S.3    Lehrer, R.I.4    Eisenberg, D.5    Feigon, J.6
  • 25
    • 84873328552 scopus 로고    scopus 로고
    • Membrane interactions and pore formation by the antimicrobial peptide protegrin
    • Lazaridis, T., He, Y., and Prieto, L. (2013) Membrane interactions and pore formation by the antimicrobial peptide protegrin Biophys. J. 104, 633-642
    • (2013) Biophys. J. , vol.104 , pp. 633-642
    • Lazaridis, T.1    He, Y.2    Prieto, L.3
  • 26
    • 34248377855 scopus 로고    scopus 로고
    • Biological and structural characterization of new linear gomesin analogues with improved therapeutic indices
    • Fázio, M. A., Jouvensal, L., Vovelle, F., Bulet, P., Miranda, M. T., Daffre, S., and Miranda, A. (2007) Biological and structural characterization of new linear gomesin analogues with improved therapeutic indices Biopolymers 88, 386-400
    • (2007) Biopolymers , vol.88 , pp. 386-400
    • Fázio, M.A.1    Jouvensal, L.2    Vovelle, F.3    Bulet, P.4    Miranda, M.T.5    Daffre, S.6    Miranda, A.7
  • 27
    • 2342593248 scopus 로고    scopus 로고
    • Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I
    • Powers, J. P., Rozek, A., and Hancock, R. E. (2004) Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I Biochim. Biophys. Acta 1698, 239-250
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 239-250
    • Powers, J.P.1    Rozek, A.2    Hancock, R.E.3
  • 28
    • 0037159195 scopus 로고    scopus 로고
    • Design of non-cysteine-containing antimicrobial beta-hairpins: Structure-activity relationship studies with linear protegrin-1 analogues
    • Lai, J. R., Huck, B. R., Weisblum, B., and Gellman, S. H. (2002) Design of non-cysteine-containing antimicrobial beta-hairpins: structure-activity relationship studies with linear protegrin-1 analogues Biochemistry 41, 12835-12842
    • (2002) Biochemistry , vol.41 , pp. 12835-12842
    • Lai, J.R.1    Huck, B.R.2    Weisblum, B.3    Gellman, S.H.4
  • 29
    • 0003621201 scopus 로고    scopus 로고
    • Chemical synthesis and characterization of small proteins: Example of scorpion toxins
    • (Rochat, H. and Martin-Eauclaire, M. F. Eds.), Birkhauser Verlag, Basel
    • Sabatier, J. M. (1999) Chemical synthesis and characterization of small proteins: example of scorpion toxins, in Animal Toxins (Rochat, H. and Martin-Eauclaire, M. F., Eds.), pp 196-216, Birkhauser Verlag, Basel.
    • (1999) Animal Toxins , pp. 196-216
    • Sabatier, J.M.1
  • 31
    • 0002672374 scopus 로고
    • Salmonella species (including typhoid fever)
    • (Mandell, G. L. Douglas, R. G. and Bennett, J. E. Eds.) 2 nd ed. p, Churchill Livingstone, London.
    • Hook, E. W. (1988) Salmonella species (including typhoid fever), in Principles and Practice of Infectious Diseases (Mandell, G. L., Douglas, R. G., and Bennett, J. E., Eds.) 2 nd ed., p 1256, Churchill Livingstone, London.
    • (1988) Principles and Practice of Infectious Diseases , pp. 1256
    • Hook, E.W.1
  • 33
    • 65349154518 scopus 로고    scopus 로고
    • Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides
    • Gao, B., Sherman, P., Luo, L., Bowie, J., and Zhu, S. (2009) Structural and functional characterization of two genetically related meucin peptides highlights evolutionary divergence and convergence in antimicrobial peptides FASEB J. 23, 1230-1245
    • (2009) FASEB J. , vol.23 , pp. 1230-1245
    • Gao, B.1    Sherman, P.2    Luo, L.3    Bowie, J.4    Zhu, S.5
  • 35
    • 32344448382 scopus 로고    scopus 로고
    • Screening for peptide drugs from the natural repertoire of biodiverse protein folds
    • Watt, P. M. (2006) Screening for peptide drugs from the natural repertoire of biodiverse protein folds Nat. Biotechnol. 24, 177-183
    • (2006) Nat. Biotechnol. , vol.24 , pp. 177-183
    • Watt, P.M.1
  • 36
    • 78249235317 scopus 로고    scopus 로고
    • Disulphide bonds of the peptide protegrin-1 are not essential for antimicrobial activity and haemolytic activity
    • Dawson, R. M. and Liu, C. Q. (2010) Disulphide bonds of the peptide protegrin-1 are not essential for antimicrobial activity and haemolytic activity Int. J. Antimicrob. Agents 36, 579-580
    • (2010) Int. J. Antimicrob. Agents , vol.36 , pp. 579-580
    • Dawson, R.M.1    Liu, C.Q.2
  • 38
    • 77950498316 scopus 로고    scopus 로고
    • Fluorescence and electron microscopy methods for exploring antimicrobial peptides mode(s) of action
    • Marcellini, L., Giammatteo, M., Aimola, P., and Mangoni, M. L. (2010) Fluorescence and electron microscopy methods for exploring antimicrobial peptides mode(s) of action Methods Mol. Biol. 618, 249-266
    • (2010) Methods Mol. Biol. , vol.618 , pp. 249-266
    • Marcellini, L.1    Giammatteo, M.2    Aimola, P.3    Mangoni, M.L.4
  • 39
    • 84867198418 scopus 로고    scopus 로고
    • Alteration of the mode of antibacterial action of a defensin by the amino-terminal loop substitution
    • Gao, B. and Zhu, S. (2012) Alteration of the mode of antibacterial action of a defensin by the amino-terminal loop substitution Biochem. Biophys. Res. Commun. 426, 630-635
    • (2012) Biochem. Biophys. Res. Commun. , vol.426 , pp. 630-635
    • Gao, B.1    Zhu, S.2
  • 40
    • 0001582678 scopus 로고    scopus 로고
    • Quantification of antimicrobial activity, using the inhibition-zone assay
    • (Wiesner, A. Dumphy, A. G. Marmaras, V. J. Morishima, I. Sugumaran, M. and Yamakawa, M. Eds.) pp, SOS Publications, Fair Haven
    • Hultmark, D. (1998) Quantification of antimicrobial activity, using the inhibition-zone assay, in Techniques in Insect Immunology (Wiesner, A., Dumphy, A. G., Marmaras, V. J., Morishima, I., Sugumaran, M., and Yamakawa, M., Eds.) pp 103-107, SOS Publications, Fair Haven.
    • (1998) Techniques in Insect Immunology , pp. 103-107
    • Hultmark, D.1
  • 41
    • 0038045648 scopus 로고    scopus 로고
    • Key role of the loop connecting the two beta strands of mussel defensin in its antimicrobial activity
    • Romestand, B., Molina, F., Richard, V., Roch, P., and Granier, C. (2003) Key role of the loop connecting the two beta strands of mussel defensin in its antimicrobial activity Eur. J. Biochem. 270, 2805-2813
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2805-2813
    • Romestand, B.1    Molina, F.2    Richard, V.3    Roch, P.4    Granier, C.5
  • 42
    • 80053319541 scopus 로고    scopus 로고
    • The defensin gene family expansion in the tick Ixodes scapularis
    • Wang, Y. and Zhu, S. (2011) The defensin gene family expansion in the tick Ixodes scapularis Dev. Comp. Immunol. 35, 1128-1134
    • (2011) Dev. Comp. Immunol. , vol.35 , pp. 1128-1134
    • Wang, Y.1    Zhu, S.2
  • 44


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