메뉴 건너뛰기




Volumn 93, Issue 2, 2011, Pages 331-338

Mapping the eosinophil cationic protein antimicrobial activity by chemical and enzymatic cleavage

Author keywords

Antimicrobial peptides; Chemical cleavage; Eosinophil cationic protein; Host defense; Proteolysis

Indexed keywords

EOSINOPHIL CATIONIC PROTEIN;

EID: 78651308063     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.10.005     Document Type: Article
Times cited : (18)

References (61)
  • 2
    • 0028931427 scopus 로고
    • Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity
    • H.F. Rosenberg Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity J. Biol. Chem. 270 1995 7876 7881
    • (1995) J. Biol. Chem. , vol.270 , pp. 7876-7881
    • Rosenberg, H.F.1
  • 3
    • 0038661343 scopus 로고    scopus 로고
    • Both aromatic and cationic residues contribute to the membrane-lytic and bactericidal activity of eosinophil cationic protein
    • E. Carreras, E. Boix, H.F. Rosenberg, C.M. Cuchillo, and M.V. Nogues Both aromatic and cationic residues contribute to the membrane-lytic and bactericidal activity of eosinophil cationic protein Biochemistry 42 2003 6636 6644
    • (2003) Biochemistry , vol.42 , pp. 6636-6644
    • Carreras, E.1    Boix, E.2    Rosenberg, H.F.3    Cuchillo, C.M.4    Nogues, M.V.5
  • 5
    • 40849124076 scopus 로고    scopus 로고
    • Eosinophil cationic protein high-affinity binding to bacteria-wall lipopolysaccharides and peptidoglycans
    • M. Torrent, S. Navarro, M. Moussaoui, M.V. Nogues, and E. Boix Eosinophil cationic protein high-affinity binding to bacteria-wall lipopolysaccharides and peptidoglycans Biochemistry 47 2008 3544 3555
    • (2008) Biochemistry , vol.47 , pp. 3544-3555
    • Torrent, M.1    Navarro, S.2    Moussaoui, M.3    Nogues, M.V.4    Boix, E.5
  • 6
    • 65249140613 scopus 로고    scopus 로고
    • Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7
    • M. Torrent, D. Sánchez, V. Buzón, M.V. Nogués, J. Cladera, and E. Boix Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7 Biochim. Biophys. Acta 1788 2009 1116 1125
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1116-1125
    • Torrent, M.1    Sánchez, D.2    Buzón, V.3    Nogués, M.V.4    Cladera, J.5    Boix, E.6
  • 7
    • 77949586101 scopus 로고    scopus 로고
    • Comparison of human RNase 3 and RNase 7 bactericidal action at the Gram-negative and Gram-positive bacterial cell wall
    • M. Torrent, M. Badia, M. Moussaoui, D. Sanchez, M.V. Nogues, and E. Boix Comparison of human RNase 3 and RNase 7 bactericidal action at the Gram-negative and Gram-positive bacterial cell wall Febs J. 277 2010 1713 1725
    • (2010) Febs J. , vol.277 , pp. 1713-1725
    • Torrent, M.1    Badia, M.2    Moussaoui, M.3    Sanchez, D.4    Nogues, M.V.5    Boix, E.6
  • 8
    • 77649237880 scopus 로고    scopus 로고
    • Antimicrobial peptides: General overview and clinical implications in human health and disease
    • E. Guani-Guerra, T. Santos-Mendoza, S.O. Lugo-Reyes, and L.M. Teran Antimicrobial peptides: general overview and clinical implications in human health and disease Clin. Immunol. 135 2010 1 11
    • (2010) Clin. Immunol. , vol.135 , pp. 1-11
    • Guani-Guerra, E.1    Santos-Mendoza, T.2    Lugo-Reyes, S.O.3    Teran, L.M.4
  • 10
    • 28044443162 scopus 로고    scopus 로고
    • Antibacterial peptides and proteins with multiple cellular targets
    • L. Otvos Jr. Antibacterial peptides and proteins with multiple cellular targets J. Pept. Sci. 11 2005 697 706
    • (2005) J. Pept. Sci. , vol.11 , pp. 697-706
    • Otvos Jr., L.1
  • 11
    • 70350435548 scopus 로고    scopus 로고
    • Multifunctional host defense peptides: Intracellular-targeting antimicrobial peptides
    • P. Nicolas Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides Febs J. 276 2009 6483 6496
    • (2009) Febs J. , vol.276 , pp. 6483-6496
    • Nicolas, P.1
  • 12
    • 37349104237 scopus 로고    scopus 로고
    • Alternative mechanisms of action of cationic antimicrobial peptides on bacteria
    • J.D. Hale, and R.E. Hancock Alternative mechanisms of action of cationic antimicrobial peptides on bacteria Expert Rev. Anti Infect. Ther. 5 2007 951 959
    • (2007) Expert Rev. Anti Infect. Ther. , vol.5 , pp. 951-959
    • Hale, J.D.1    Hancock, R.E.2
  • 13
    • 27644434075 scopus 로고    scopus 로고
    • Peptidoglycan recognition in innate immunity
    • R. Dziarski, and D. Gupta Peptidoglycan recognition in innate immunity J. Endotoxin Res. 11 2005 304 310
    • (2005) J. Endotoxin Res. , vol.11 , pp. 304-310
    • Dziarski, R.1    Gupta, D.2
  • 14
    • 33748949579 scopus 로고    scopus 로고
    • Lipopolysaccharide (Endotoxin)-host defense antibacterial peptides interactions: Role in bacterial resistance and prevention of sepsis
    • Y. Rosenfeld, and Y. Shai Lipopolysaccharide (Endotoxin)-host defense antibacterial peptides interactions: role in bacterial resistance and prevention of sepsis Biochim. Biophys. Acta 1758 2006 1513 1522
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1513-1522
    • Rosenfeld, Y.1    Shai, Y.2
  • 15
    • 67650957816 scopus 로고    scopus 로고
    • New strategies for novel antibiotics: Peptides targeting bacterial cell membranes
    • K. Lohner New strategies for novel antibiotics: peptides targeting bacterial cell membranes Gen. Physiol. Biophys. 28 2009 105 116
    • (2009) Gen. Physiol. Biophys. , vol.28 , pp. 105-116
    • Lohner, K.1
  • 16
    • 0021929428 scopus 로고
    • Lysozyme-mediated aggregation and lysis of the periodontal microorganism Capnocytophaga gingivalis 2010
    • V.J. Iacono, S.M. Zove, B.L. Grossbard, J.J. Pollock, D.H. Fine, and L.S. Greene Lysozyme-mediated aggregation and lysis of the periodontal microorganism Capnocytophaga gingivalis 2010 Infect. Immun. 47 1985 457 464
    • (1985) Infect. Immun. , vol.47 , pp. 457-464
    • Iacono, V.J.1    Zove, S.M.2    Grossbard, B.L.3    Pollock, J.J.4    Fine, D.H.5    Greene, L.S.6
  • 17
    • 0032401651 scopus 로고    scopus 로고
    • Biophysical characterisation of lysozyme binding to LPS Re and lipid A
    • K. Brandenburg, M.H. Koch, and U. Seydel Biophysical characterisation of lysozyme binding to LPS Re and lipid A Eur. J. Biochem. 258 1998 686 695
    • (1998) Eur. J. Biochem. , vol.258 , pp. 686-695
    • Brandenburg, K.1    Koch, M.H.2    Seydel, U.3
  • 18
    • 0026560481 scopus 로고
    • Bactericidal activities of lysozyme and aprotinin against gram-negative and gram-positive bacteria related to their basic character
    • A. Pellegrini, U. Thomas, R. von Fellenberg, and P. Wild Bactericidal activities of lysozyme and aprotinin against gram-negative and gram-positive bacteria related to their basic character J. Appl. Bacteriol. 72 1992 180 187
    • (1992) J. Appl. Bacteriol. , vol.72 , pp. 180-187
    • Pellegrini, A.1    Thomas, U.2    Von Fellenberg, R.3    Wild, P.4
  • 19
    • 0021183247 scopus 로고
    • Cationic antimicrobial proteins isolated from human neutrophil granulocytes in the presence of diisopropyl fluorophosphate
    • W.M. Shafer, L.E. Martin, and J.K. Spitznagel Cationic antimicrobial proteins isolated from human neutrophil granulocytes in the presence of diisopropyl fluorophosphate Infect. Immun. 45 1984 29 35
    • (1984) Infect. Immun. , vol.45 , pp. 29-35
    • Shafer, W.M.1    Martin, L.E.2    Spitznagel, J.K.3
  • 21
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • K.L. Brown, and R.E. Hancock Cationic host defense (antimicrobial) peptides Curr. Opin. Immunol. 18 2006 24 30
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 22
    • 70450158469 scopus 로고    scopus 로고
    • The chemistry and biology of LL-37
    • M.F. Burton, and P.G. Steel The chemistry and biology of LL-37 Nat. Prod. Rep. 26 2009 1572 1584
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 1572-1584
    • Burton, M.F.1    Steel, P.G.2
  • 23
    • 0033377813 scopus 로고    scopus 로고
    • Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system
    • G.H. Gudmundsson, and B. Agerberth Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system J. Immunol. Methods 232 1999 45 54
    • (1999) J. Immunol. Methods , vol.232 , pp. 45-54
    • Gudmundsson, G.H.1    Agerberth, B.2
  • 24
    • 0032437146 scopus 로고    scopus 로고
    • Direct evidence of the generation in human stomach of an antimicrobial peptide domain (lactoferricin) from ingested lactoferrin
    • H. Kuwata, T.T. Yip, M. Tomita, and T.W. Hutchens Direct evidence of the generation in human stomach of an antimicrobial peptide domain (lactoferricin) from ingested lactoferrin Biochim. Biophys. Acta 1429 1998 129 141
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 129-141
    • Kuwata, H.1    Yip, T.T.2    Tomita, M.3    Hutchens, T.W.4
  • 25
  • 26
    • 0034667551 scopus 로고    scopus 로고
    • Antimicrobial proteins and peptides of blood: Templates for novel antimicrobial agents
    • O. Levy Antimicrobial proteins and peptides of blood: templates for novel antimicrobial agents Blood 96 2000 2664 2672
    • (2000) Blood , vol.96 , pp. 2664-2672
    • Levy, O.1
  • 27
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • M. Zanetti, R. Gennaro, and D. Romeo 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
  • 29
    • 44649149642 scopus 로고    scopus 로고
    • RNase A ribonucleases and host defense: An evolving story
    • H.F. Rosenberg RNase A ribonucleases and host defense: an evolving story J. Leukoc. Biol. 83 2008 1079 1087
    • (2008) J. Leukoc. Biol. , vol.83 , pp. 1079-1087
    • Rosenberg, H.F.1
  • 30
    • 33748742183 scopus 로고    scopus 로고
    • Evolution and function of leukocyte RNase A ribonucleases of the avian species, Gallus gallus
    • T. Nitto, K.D. Dyer, M. Czapiga, and H.F. Rosenberg Evolution and function of leukocyte RNase A ribonucleases of the avian species, Gallus gallus J. Biol. Chem. 281 2006 25622 25634
    • (2006) J. Biol. Chem. , vol.281 , pp. 25622-25634
    • Nitto, T.1    Dyer, K.D.2    Czapiga, M.3    Rosenberg, H.F.4
  • 31
    • 36749100831 scopus 로고    scopus 로고
    • The success of the RNase scaffold in the advance of biosciences and in evolution
    • E. Pizzo, and G. D'Alessio The success of the RNase scaffold in the advance of biosciences and in evolution Gene 406 2007 8 12
    • (2007) Gene , vol.406 , pp. 8-12
    • Pizzo, E.1    D'Alessio, G.2
  • 32
    • 69249227505 scopus 로고    scopus 로고
    • Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment
    • M. Torrent, B.G. de la Torre, V.M. Nogues, D. Andreu, and E. Boix Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment Biochem. J. 421 2009 425 434
    • (2009) Biochem. J. , vol.421 , pp. 425-434
    • Torrent, M.1    De La Torre, B.G.2    Nogues, V.M.3    Andreu, D.4    Boix, E.5
  • 33
    • 0033022636 scopus 로고    scopus 로고
    • Kinetic and product distribution analysis of human eosinophil cationic protein indicates a subsite arrangement that favors exonuclease-type activity
    • E. Boix, Z. Nikolovski, G.P. Moiseyev, H.F. Rosenberg, C.M. Cuchillo, and M.V. Nogues Kinetic and product distribution analysis of human eosinophil cationic protein indicates a subsite arrangement that favors exonuclease-type activity J. Biol. Chem. 274 1999 15605 15614
    • (1999) J. Biol. Chem. , vol.274 , pp. 15605-15614
    • Boix, E.1    Nikolovski, Z.2    Moiseyev, G.P.3    Rosenberg, H.F.4    Cuchillo, C.M.5    Nogues, M.V.6
  • 35
    • 0021105027 scopus 로고
    • Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis
    • P.A. Jekel, W.J. Weijer, and J.J. Beintema Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis Anal. Biochem. 134 1983 347 354
    • (1983) Anal. Biochem. , vol.134 , pp. 347-354
    • Jekel, P.A.1    Weijer, W.J.2    Beintema, J.J.3
  • 36
    • 73049160443 scopus 로고
    • Nonenzymatic cleavage of peptide bonds: The methionine residues in bovine pancreatic ribonuclease
    • E. Gross, and B. Witkop Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease J. Biol. Chem. 237 1962 1856 1860
    • (1962) J. Biol. Chem. , vol.237 , pp. 1856-1860
    • Gross, E.1    Witkop, B.2
  • 37
    • 0029871341 scopus 로고    scopus 로고
    • Role of the N terminus in RNase A homologues: Differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity
    • E. Boix, Y. Wu, V.M. Vasandani, S.K. Saxena, W. Ardelt, J. Ladner, and R.J. Youle Role of the N terminus in RNase A homologues: differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity J. Mol. Biol. 257 1996 992 1007
    • (1996) J. Mol. Biol. , vol.257 , pp. 992-1007
    • Boix, E.1    Wu, Y.2    Vasandani, V.M.3    Saxena, S.K.4    Ardelt, W.5    Ladner, J.6    Youle, R.J.7
  • 38
    • 0022445505 scopus 로고
    • Modification of bovine pancreatic ribonuclease A with 6-chloropurine riboside
    • J. Alonso, M.V. Nogues, and C.M. Cuchillo Modification of bovine pancreatic ribonuclease A with 6-chloropurine riboside Arch. Biochem. Biophys. 246 1986 681 689
    • (1986) Arch. Biochem. Biophys. , vol.246 , pp. 681-689
    • Alonso, J.1    Nogues, M.V.2    Cuchillo, C.M.3
  • 40
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • K. Hilpert, R. Volkmer-Engert, T. Walter, and R.E. Hancock 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
  • 41
    • 0018270640 scopus 로고
    • Spin-labeled ribonuclease A. Effects of chemical, enzymatic, and physical modifications on enzyme conformation
    • M.R. Gregory, W.E. Daniel Jr., and R.G. Hiskey Spin-labeled ribonuclease A. Effects of chemical, enzymatic, and physical modifications on enzyme conformation Biochemistry 17 1978 2025 2030
    • (1978) Biochemistry , vol.17 , pp. 2025-2030
    • Gregory, M.R.1    Daniel Jr., W.E.2    Hiskey, R.G.3
  • 42
    • 0014675276 scopus 로고
    • The total synthesis of an enzyme with ribonuclease A activity
    • B. Gutte, and R.B. Merrifield The total synthesis of an enzyme with ribonuclease A activity J. Am. Chem. Soc. 91 1969 501 502
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 501-502
    • Gutte, B.1    Merrifield, R.B.2
  • 43
    • 0022017388 scopus 로고
    • Renaturation of soluble and immobilized ribonuclease: Are the polypeptide folding pathways for structure formation the same for soluble proteins and for proteins associated with a surface?
    • V.G. Janolino, H.E. Swaisgood, and H.R. Horton Renaturation of soluble and immobilized ribonuclease: are the polypeptide folding pathways for structure formation the same for soluble proteins and for proteins associated with a surface? J. Appl. Biochem. 7 1985 33 37
    • (1985) J. Appl. Biochem. , vol.7 , pp. 33-37
    • Janolino, V.G.1    Swaisgood, H.E.2    Horton, H.R.3
  • 45
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action
    • H.R. Ibrahim, U. Thomas, and A. Pellegrini A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action J. Biol. Chem. 276 2001 43767 43774
    • (2001) J. Biol. Chem. , vol.276 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 48
    • 71049173766 scopus 로고    scopus 로고
    • A theoretical approach to spot active regions in antimicrobial proteins
    • M. Torrent, V.M. Nogues, and E. Boix A theoretical approach to spot active regions in antimicrobial proteins BMC Bioinformatics 10 2009 373 382
    • (2009) BMC Bioinformatics , vol.10 , pp. 373-382
    • Torrent, M.1    Nogues, V.M.2    Boix, E.3
  • 49
    • 0032584099 scopus 로고    scopus 로고
    • Positive Darwinian selection after gene duplication in primate ribonuclease genes
    • J. Zhang, H.F. Rosenberg, and M. Nei Positive Darwinian selection after gene duplication in primate ribonuclease genes Proc. Natl. Acad. Sci. USA 95 1998 3708 3713
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3708-3713
    • Zhang, J.1    Rosenberg, H.F.2    Nei, M.3
  • 50
    • 0019888485 scopus 로고
    • Primary structure of 3-phosphoglycerate kinase from horse muscle. II. Amino acid sequence of cyanogen bromide peptides CB1-CB4 and CB6-CB14, sequence of methionine-containing regions, and complete sequence of the enzyme
    • M. Merrett Primary structure of 3-phosphoglycerate kinase from horse muscle. II. Amino acid sequence of cyanogen bromide peptides CB1-CB4 and CB6-CB14, sequence of methionine-containing regions, and complete sequence of the enzyme J. Biol. Chem. 256 1981 10293 10305
    • (1981) J. Biol. Chem. , vol.256 , pp. 10293-10305
    • Merrett, M.1
  • 51
    • 0020669308 scopus 로고
    • Cleavage at tryptophanyl residues with dimethyl sulfoxide-hydrochloric acid and cyanogen bromide
    • H.V. Huang, M.W. Bond, M.W. Hunkapiller, and L.E. Hood Cleavage at tryptophanyl residues with dimethyl sulfoxide-hydrochloric acid and cyanogen bromide Meth. Enzymol. 91 1983 318 324
    • (1983) Meth. Enzymol. , vol.91 , pp. 318-324
    • Huang, H.V.1    Bond, M.W.2    Hunkapiller, M.W.3    Hood, L.E.4
  • 52
    • 0022374759 scopus 로고
    • Cyanogen bromide cleaves Fc fragments of pooled human IgG at both methionine and tryptophan residues
    • D.W. Boulware, P.D. Goldsworthy, F.A. Nardella, and M. Mannik Cyanogen bromide cleaves Fc fragments of pooled human IgG at both methionine and tryptophan residues Mol. Immunol. 22 1985 1317 1322
    • (1985) Mol. Immunol. , vol.22 , pp. 1317-1322
    • Boulware, D.W.1    Goldsworthy, P.D.2    Nardella, F.A.3    Mannik, M.4
  • 54
    • 20944447573 scopus 로고    scopus 로고
    • Surface-exposed amino acids of eosinophil cationic protein play a critical role in the inhibition of mammalian cell proliferation
    • E. Carreras, E. Boix, S. Navarro, H.F. Rosenberg, C.M. Cuchillo, and M.V. Nogues Surface-exposed amino acids of eosinophil cationic protein play a critical role in the inhibition of mammalian cell proliferation Mol. Cell. Biochem. 272 2005 1 7
    • (2005) Mol. Cell. Biochem. , vol.272 , pp. 1-7
    • Carreras, E.1    Boix, E.2    Navarro, S.3    Rosenberg, H.F.4    Cuchillo, C.M.5    Nogues, M.V.6
  • 55
  • 56
    • 85031337947 scopus 로고    scopus 로고
    • Eosinophil cationic protein (ECP) can bind heparin and other glycosaminoglycans through its RNase active site
    • M. Torrent, M.V. Nogues, and E. Boix Eosinophil cationic protein (ECP) can bind heparin and other glycosaminoglycans through its RNase active site J. Mol. Recognit. 2010
    • (2010) J. Mol. Recognit.
    • Torrent, M.1    Nogues, M.V.2    Boix, E.3
  • 57
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 58
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • D. Andreu, and L. Rivas Animal antimicrobial peptides: an overview Biopolymers 47 1998 415 433
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 60
    • 77955578891 scopus 로고    scopus 로고
    • Eosinophil cationic protein (ECP) aggregation. Identification of an N-terminus amyloid prone region
    • M. Torrent, F. Odorizzi, M.V. Nogués, and E. Boix Eosinophil cationic protein (ECP) aggregation. Identification of an N-terminus amyloid prone region Biomacromolecules 11 2010 1983 1990
    • (2010) Biomacromolecules , vol.11 , pp. 1983-1990
    • Torrent, M.1    Odorizzi, F.2    Nogués, M.V.3    Boix, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.