메뉴 건너뛰기




Volumn 65, Issue 7-8, 2008, Pages 1202-1219

The Sushi peptides: Structural characterization and mode of action against Gram-negative bacteria

Author keywords

LPS binding and disruption; Membrane phospholipids; Sushi peptides; Synthetic antimicrobial peptides

Indexed keywords

ALAMETHICIN; FACTOR C; GLYCEROL DERIVATIVE; LACTOFERRICIN B; LIPID A; LIPOPOLYSACCHARIDE; LIPOPOLYSACCHARIDE BINDING PROTEIN; MEMBRANE PHOSPHOLIPID; PALMITOYLOLEOYLPHOSPHATIDYLGLYCEROL; POLYMYXIN B; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEGRIN; SERINE PROTEINASE; SERUM AMYLOID P; SUSHI 1 PEPTIDE; SUSHI 3 PEPTIDE; SYNTHETIC PEPTIDE; TACHYPLESIN; UNCLASSIFIED DRUG;

EID: 42449113387     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-7456-0     Document Type: Review
Times cited : (36)

References (156)
  • 1
    • 0033257746 scopus 로고    scopus 로고
    • The new antibiotics
    • Breithaupt, H. (1999) The new antibiotics. Nat. Biotechnol. 17, 1165-1169.
    • (1999) Nat. Biotechnol , vol.17 , pp. 1165-1169
    • Breithaupt, H.1
  • 2
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 3
    • 13444266131 scopus 로고    scopus 로고
    • The role of peptidoglycan in pathogenesis
    • Boneca, I. G. (2005) The role of peptidoglycan in pathogenesis. Curr. Opin. Microbiol. 8, 46-53.
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 46-53
    • Boneca, I.G.1
  • 4
    • 0035654561 scopus 로고    scopus 로고
    • Systemic toxins: Signs, symptoms and management of patients in septic shock
    • quiz 66-67
    • Lent, M., Hirshberg, A. and Margolis, G. (2001) Systemic toxins: signs, symptoms and management of patients in septic shock. JEMS 26, 54-65; quiz 66-67.
    • (2001) JEMS , vol.26 , pp. 54-65
    • Lent, M.1    Hirshberg, A.2    Margolis, G.3
  • 7
    • 0029941532 scopus 로고    scopus 로고
    • The sepsis syndrome: Definition and general approach to management
    • Bone, R. C. (1996) The sepsis syndrome: definition and general approach to management, Clin. Chest Med. 17, 175-181.
    • (1996) Clin. Chest Med , vol.17 , pp. 175-181
    • Bone, R.C.1
  • 8
    • 0034780632 scopus 로고    scopus 로고
    • Toxic shock syndrome and bacterial superantigens: An update
    • McCormick, J. K., Yarwood, J. M. and Schlievert, P. M. (2001) Toxic shock syndrome and bacterial superantigens: an update. Annu. Rev. Microbiol. 55, 77-104.
    • (2001) Annu. Rev. Microbiol , vol.55 , pp. 77-104
    • McCormick, J.K.1    Yarwood, J.M.2    Schlievert, P.M.3
  • 10
    • 0028844387 scopus 로고    scopus 로고
    • Gradishar, W. J., Vogelzang, N. J., Kilton, L. J., Leibach, S. J., Rademaker, A. W., French, S. and Benson, A. B., 3rd. (1995) A phase II clinical trial of echinomycin in metastatic soft tissue sarcoma. An Illinois Cancer Center Study, Invest. New Drugs 13, 171-174.
    • Gradishar, W. J., Vogelzang, N. J., Kilton, L. J., Leibach, S. J., Rademaker, A. W., French, S. and Benson, A. B., 3rd. (1995) A phase II clinical trial of echinomycin in metastatic soft tissue sarcoma. An Illinois Cancer Center Study, Invest. New Drugs 13, 171-174.
  • 11
    • 0035192670 scopus 로고    scopus 로고
    • Systemic inflammatory response syndrome, sepsis, and multiple organ dysfunction
    • v-vi
    • Brady, C. A. and Otto, C. M. (2001) Systemic inflammatory response syndrome, sepsis, and multiple organ dysfunction. Vet. Clin. North Am. Small Anim. Pract. 31, 1147-1162, v-vi.
    • (2001) Vet. Clin. North Am. Small Anim. Pract , vol.31 , pp. 1147-1162
    • Brady, C.A.1    Otto, C.M.2
  • 13
    • 0034924156 scopus 로고    scopus 로고
    • Epidemiology of sepsis: An update
    • Angus, D. C. and Wax, R. S. (2001) Epidemiology of sepsis: an update. Crit. Care Med. 29, S109-116.
    • (2001) Crit. Care Med , vol.29
    • Angus, D.C.1    Wax, R.S.2
  • 16
    • 0036015489 scopus 로고    scopus 로고
    • Lipopolysaccharide: Structure, bioactivity, receptors, and signal transduction. Trends Glycosci
    • Ulmer, A. J., Rietschel, E. T., Zahringer, U. and Heine, H. (2002) Lipopolysaccharide: structure, bioactivity, receptors, and signal transduction. Trends Glycosci. Glycotechnol., 14, 53-88.
    • (2002) Glycotechnol , vol.14 , pp. 53-88
    • Ulmer, A.J.1    Rietschel, E.T.2    Zahringer, U.3    Heine, H.4
  • 17
    • 78651235479 scopus 로고    scopus 로고
    • Molecular dynamics study on lipid A from Escherichia coli: Insights into its mechanism of biological action
    • Frecer, V., Ho, B. and Ding, J. L. (2000) Molecular dynamics study on lipid A from Escherichia coli: insights into its mechanism of biological action. Biochim Biophys Acta 1466, 87-104.
    • (2000) Biochim Biophys Acta , vol.1466 , pp. 87-104
    • Frecer, V.1    Ho, B.2    Ding, J.L.3
  • 18
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • Hancock, R. E. 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.1    Rozek, A.2
  • 20
    • 0037031254 scopus 로고    scopus 로고
    • Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin
    • Yamaguchi, S., Hong, T., Waring, A., Lehrer, R. I. and Hong, M. (2002) Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin. Biochemistry 41, 9852-9862.
    • (2002) Biochemistry , vol.41 , pp. 9852-9862
    • Yamaguchi, S.1    Hong, T.2    Waring, A.3    Lehrer, R.I.4    Hong, M.5
  • 23
    • 0019515401 scopus 로고
    • Neisseria gonorrhoeae cell envelope: Permeability to hydrophobic molecules
    • Lysko, P. G. and Morse, S. A. (1981) Neisseria gonorrhoeae cell envelope: permeability to hydrophobic molecules. J. Bacteriol. 145, 946-952.
    • (1981) J. Bacteriol , vol.145 , pp. 946-952
    • Lysko, P.G.1    Morse, S.A.2
  • 24
    • 0242414731 scopus 로고    scopus 로고
    • Treponemal phospholipids inhibit innate immune responses induced by pathogen-associated molecular patterns
    • Hashimoto, M., Asai, Y. and Ogawa, T. (2003) Treponemal phospholipids inhibit innate immune responses induced by pathogen-associated molecular patterns. J. Biol. Chem. 278, 44205-44213.
    • (2003) J. Biol. Chem , vol.278 , pp. 44205-44213
    • Hashimoto, M.1    Asai, Y.2    Ogawa, T.3
  • 26
    • 0031030348 scopus 로고    scopus 로고
    • Lipopolysaccharide binding protein and soluble CD14 catalyze exchange of phospholipids
    • Yu, B., Hailman, E. and Wright, S. D. (1997) Lipopolysaccharide binding protein and soluble CD14 catalyze exchange of phospholipids. J. Clin. Invest. 99, 315-324.
    • (1997) J. Clin. Invest , vol.99 , pp. 315-324
    • Yu, B.1    Hailman, E.2    Wright, S.D.3
  • 27
    • 0035958848 scopus 로고    scopus 로고
    • A novel linear amphipathic beta-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids
    • Blazyk, J., Wiegand, R., Klein, J., Hammer, J., Epand, R. M., Epand, R. F., Maloy, W. L. and Kari, U. P. (2001) A novel linear amphipathic beta-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids. J. Biol. Chem. 276, 27899-27906.
    • (2001) J. Biol. Chem , vol.276 , pp. 27899-27906
    • Blazyk, J.1    Wiegand, R.2    Klein, J.3    Hammer, J.4    Epand, R.M.5    Epand, R.F.6    Maloy, W.L.7    Kari, U.P.8
  • 28
    • 33748274757 scopus 로고    scopus 로고
    • The molecular mechanisms that govern the specificity of Sushi peptides for gram negative bacterial membrane lipids
    • Li, P., Sun, M., Wohland, T., Yang, D., Ho, B. and Ding, J. L. (2006) The molecular mechanisms that govern the specificity of Sushi peptides for gram negative bacterial membrane lipids. Biochemistry 45, 10554-10562.
    • (2006) Biochemistry , vol.45 , pp. 10554-10562
    • Li, P.1    Sun, M.2    Wohland, T.3    Yang, D.4    Ho, B.5    Ding, J.L.6
  • 29
    • 3142763231 scopus 로고    scopus 로고
    • Endotoxins: Relationships between structure, function, and activity
    • Brandenburg, K. and Wiese, A. (2004) Endotoxins: relationships between structure, function, and activity. Curr. Top. Med. Chem. 4, 1127-1146.
    • (2004) Curr. Top. Med. Chem , vol.4 , pp. 1127-1146
    • Brandenburg, K.1    Wiese, A.2
  • 30
    • 0028272187 scopus 로고
    • The effect of root conditioning with minocycline HCl in removing endotoxin from the roots of periodontally-involved teeth
    • Minabe, M., Takeuchi, K., Kumada, H. and Umemoto, T. (1994) The effect of root conditioning with minocycline HCl in removing endotoxin from the roots of periodontally-involved teeth. J. Periodontol. 65, 387-392.
    • (1994) J. Periodontol , vol.65 , pp. 387-392
    • Minabe, M.1    Takeuchi, K.2    Kumada, H.3    Umemoto, T.4
  • 31
    • 0033991321 scopus 로고    scopus 로고
    • Endotoxin removal from protein solutions
    • Petsch, D. and Anspach, F. B. (2000) Endotoxin removal from protein solutions. J. Biotechnol. 76, 97-119.
    • (2000) J. Biotechnol , vol.76 , pp. 97-119
    • Petsch, D.1    Anspach, F.B.2
  • 33
    • 0019430334 scopus 로고
    • Structural studies on the hexose region of the core in lipopolysaccharides from Enterobacteriaceae
    • Jansson, P. E., Lindberg, A. A., Lindberg, B. and Wollin, R. (1981) Structural studies on the hexose region of the core in lipopolysaccharides from Enterobacteriaceae. Eur. J. Biochem. 115, 571-577.
    • (1981) Eur. J. Biochem , vol.115 , pp. 571-577
    • Jansson, P.E.1    Lindberg, A.A.2    Lindberg, B.3    Wollin, R.4
  • 35
    • 0026989386 scopus 로고
    • Bacterial endotoxins
    • Rietschel, E. T. and Brade, H. (1992) Bacterial endotoxins. Sci. Am. 267, 54-61.
    • (1992) Sci. Am , vol.267 , pp. 54-61
    • Rietschel, E.T.1    Brade, H.2
  • 36
    • 0031965409 scopus 로고    scopus 로고
    • Anti-endotoxin therapeutic options for the treatment of sepsis
    • Lynn, W. A. (1998) Anti-endotoxin therapeutic options for the treatment of sepsis. J. Antimicrob. Chemother. 41 Suppl. A, 71-80.
    • (1998) J. Antimicrob. Chemother , vol.41 , Issue.SUPPL. A , pp. 71-80
    • Lynn, W.A.1
  • 38
    • 0021112129 scopus 로고
    • Fatty acyl derivatives of glucosamine 1-phosphate in Escherichia coli and their relation to lipid A. Complete structure of A diacyl GlcN-1-P found in a phosphatidylglycerol-deficient mutant
    • Takayama, K., Qureshi, N., Mascagni, P., Nashed, M. A., Anderson, L. and Raetz, C. R. (1983) Fatty acyl derivatives of glucosamine 1-phosphate in Escherichia coli and their relation to lipid A. Complete structure of A diacyl GlcN-1-P found in a phosphatidylglycerol-deficient mutant. J. Biol. Chem. 258, 7379-7385.
    • (1983) J. Biol. Chem , vol.258 , pp. 7379-7385
    • Takayama, K.1    Qureshi, N.2    Mascagni, P.3    Nashed, M.A.4    Anderson, L.5    Raetz, C.R.6
  • 39
    • 84961979617 scopus 로고    scopus 로고
    • Interpretation of biological activity data of bacterial endotoxins by simple molecular models of mechanism of action
    • Frecer, V., Ho, B. and Ding, J. L. (2000) Interpretation of biological activity data of bacterial endotoxins by simple molecular models of mechanism of action. Eur. J. Biochem. 267, 837-852.
    • (2000) Eur. J. Biochem , vol.267 , pp. 837-852
    • Frecer, V.1    Ho, B.2    Ding, J.L.3
  • 41
    • 0025166114 scopus 로고
    • CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein
    • Wright, S. D., Ramos, R. A., Tobias, P. S., Ulevitch, R. J. and Mathison, J. C. (1990) CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein. Science 249, 1431-1433.
    • (1990) Science , vol.249 , pp. 1431-1433
    • Wright, S.D.1    Ramos, R.A.2    Tobias, P.S.3    Ulevitch, R.J.4    Mathison, J.C.5
  • 42
    • 43949176031 scopus 로고
    • CD14: Cell surface receptor and differentiation marker
    • Ziegler-Heitbrock, H. W. and Ulevitch, R. J. (1993) CD14: cell surface receptor and differentiation marker, Immunol. Today 14, 121-125.
    • (1993) Immunol. Today , vol.14 , pp. 121-125
    • Ziegler-Heitbrock, H.W.1    Ulevitch, R.J.2
  • 43
    • 15744396047 scopus 로고    scopus 로고
    • Crystal structure of CD14 and its implications for lipopolysaccharide signaling
    • Kim, J. I., Lee, C. J., Jin, M. S., Lee, C. H., Paik, S. G., Lee, H. and Lee, J. O. (2005) Crystal structure of CD14 and its implications for lipopolysaccharide signaling. J. Biol. Chem. 280, 11347-11351.
    • (2005) J. Biol. Chem , vol.280 , pp. 11347-11351
    • Kim, J.I.1    Lee, C.J.2    Jin, M.S.3    Lee, C.H.4    Paik, S.G.5    Lee, H.6    Lee, J.O.7
  • 44
    • 0033016573 scopus 로고    scopus 로고
    • The molecular pathogenesis of endotoxic shock and organ failure
    • Karima, R., Matsumoto, S., Higashi, H. and Matsushima, K. (1999) The molecular pathogenesis of endotoxic shock and organ failure. Mol. Med. Today 5, 123-132.
    • (1999) Mol. Med. Today , vol.5 , pp. 123-132
    • Karima, R.1    Matsumoto, S.2    Higashi, H.3    Matsushima, K.4
  • 45
    • 0034617274 scopus 로고    scopus 로고
    • Cellular events mediated by lipopolysaccharide-stimulated toll-like receptor 4. MD-2 is required for activation of mitogen-activated protein kinases and Elk-1
    • Yang, H., Young, D. W., Gusovsky, F. and Chow, J. C. (2000) Cellular events mediated by lipopolysaccharide-stimulated toll-like receptor 4. MD-2 is required for activation of mitogen-activated protein kinases and Elk-1. J. Biol. Chem. 275, 20861-20866.
    • (2000) J. Biol. Chem , vol.275 , pp. 20861-20866
    • Yang, H.1    Young, D.W.2    Gusovsky, F.3    Chow, J.C.4
  • 46
    • 0029890168 scopus 로고    scopus 로고
    • Endotoxin signal transduction in macrophages
    • Sweet, M. J. and Hume, D. A. (1996) Endotoxin signal transduction in macrophages. J. Leukoc. Biol. 60, 8-26.
    • (1996) J. Leukoc. Biol , vol.60 , pp. 8-26
    • Sweet, M.J.1    Hume, D.A.2
  • 47
    • 17044370808 scopus 로고    scopus 로고
    • LPS induces the interaction of a transcription factor, LPS-induced TNF-alpha factor, and STAT6(B) with effects on multiple cytokines
    • Tang, X., Marciano, D. L., Leeman, S. E. and Amar, S. (2005) LPS induces the interaction of a transcription factor, LPS-induced TNF-alpha factor, and STAT6(B) with effects on multiple cytokines. Proc. Natl. Acad. Sci. USA 102, 5132-5137.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5132-5137
    • Tang, X.1    Marciano, D.L.2    Leeman, S.E.3    Amar, S.4
  • 48
    • 33645981604 scopus 로고    scopus 로고
    • The specificity of Sushi peptides for endotoxin and anionic phospholipids: Potential application of POPG as an adjuvant for anti-LPS strategies
    • Li, P., Sun, M., Ho, B. and Ding, J. L. (2006) The specificity of Sushi peptides for endotoxin and anionic phospholipids: potential application of POPG as an adjuvant for anti-LPS strategies. Biochem. Soc. Trans. 34, 270-272.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 270-272
    • Li, P.1    Sun, M.2    Ho, B.3    Ding, J.L.4
  • 50
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock, R. E. and Scott, M. G. (2000) The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. USA 97, 8856-8861.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 51
    • 25444458008 scopus 로고    scopus 로고
    • Anti-endotoxin properties of cationic host defence peptides and proteins
    • Bowdish, D. M. and Hancock, R. E. (2005) Anti-endotoxin properties of cationic host defence peptides and proteins. J. Endotoxin Res. 11, 230-236.
    • (2005) J. Endotoxin Res , vol.11 , pp. 230-236
    • Bowdish, D.M.1    Hancock, R.E.2
  • 52
    • 3142689915 scopus 로고    scopus 로고
    • The search for molecular determinants of LPS inhibition by proteins and peptides
    • Pristovsek, P. and Kidric, J. (2004) The search for molecular determinants of LPS inhibition by proteins and peptides. Curr. Top. Med. Chem. 4, 1185-1201.
    • (2004) Curr. Top. Med. Chem , vol.4 , pp. 1185-1201
    • Pristovsek, P.1    Kidric, J.2
  • 53
    • 0016428571 scopus 로고
    • Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli
    • Weiss, J., Franson, R. C., Beckerdite, S., Schmeidler, K. and Elsbach, P. (1975) Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli, J. Clin. Invest. 55, 33-42.
    • (1975) J. Clin. Invest , vol.55 , pp. 33-42
    • Weiss, J.1    Franson, R.C.2    Beckerdite, S.3    Schmeidler, K.4    Elsbach, P.5
  • 54
    • 0026497337 scopus 로고
    • High-affinity binding of the bactericidal/permeability-increasing protein and a recombinant amino-terminal fragment to the lipid A region of lipopolysaccharide
    • Gazzano-Santoro, H., Parent, J. B., Grinna, L., Horwitz, A., Parsons, T., Theofan, G., Elsbach, P., Weiss, J. and Conlon, P. J. (1992) High-affinity binding of the bactericidal/permeability-increasing protein and a recombinant amino-terminal fragment to the lipid A region of lipopolysaccharide. Infect. Immun. 60, 4754-4761.
    • (1992) Infect. Immun , vol.60 , pp. 4754-4761
    • Gazzano-Santoro, H.1    Parent, J.B.2    Grinna, L.3    Horwitz, A.4    Parsons, T.5    Theofan, G.6    Elsbach, P.7    Weiss, J.8    Conlon, P.J.9
  • 55
    • 0031776895 scopus 로고    scopus 로고
    • The bactericidal/permeability-increasing protein (BPI) in antibacterial host defense
    • Elsbach, P. (1998) The bactericidal/permeability-increasing protein (BPI) in antibacterial host defense. J. Leukoc. Biol. 64, 14-18.
    • (1998) J. Leukoc. Biol , vol.64 , pp. 14-18
    • Elsbach, P.1
  • 56
    • 0033994735 scopus 로고    scopus 로고
    • CD14-dependent and independent pathways in lipopolysaccharide-induced activation of a murine B-cell line, CH12. LX
    • Kimura, S., Tamamura, T., Nakagawa, I., Koga, T., Fujiwara, T. and Hamada, S. (2000) CD14-dependent and independent pathways in lipopolysaccharide-induced activation of a murine B-cell line, CH12. LX. Scand. J. Immunol. 51, 392-399.
    • (2000) Scand. J. Immunol , vol.51 , pp. 392-399
    • Kimura, S.1    Tamamura, T.2    Nakagawa, I.3    Koga, T.4    Fujiwara, T.5    Hamada, S.6
  • 57
    • 0020416253 scopus 로고
    • Limulus anti-LPS factor: An anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system
    • Tanaka, S., Nakamura, T., Morita, T. and Iwanaga, S. (1982) Limulus anti-LPS factor: an anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system. Biochem. Biophys. Res. Commun. 105, 717-723.
    • (1982) Biochem. Biophys. Res. Commun , vol.105 , pp. 717-723
    • Tanaka, S.1    Nakamura, T.2    Morita, T.3    Iwanaga, S.4
  • 58
    • 0024316023 scopus 로고
    • Identification of a lipid A binding site in the acute phase reactant lipopolysaccharide binding protein
    • Tobias, P. S., Soldau, K. and Ulevitch, R. J. (1989) Identification of a lipid A binding site in the acute phase reactant lipopolysaccharide binding protein. J. Biol. Chem. 264, 10867-10871.
    • (1989) J. Biol. Chem , vol.264 , pp. 10867-10871
    • Tobias, P.S.1    Soldau, K.2    Ulevitch, R.J.3
  • 59
    • 0025178843 scopus 로고
    • Investigation of endotoxin binding cationic proteins from granulocytes; agglutination of erythrocytes sensitized with Re-LPS
    • Hirata, M., Yoshida, M., Inada, K. and Kirikae, T. (1990) Investigation of endotoxin binding cationic proteins from granulocytes; agglutination of erythrocytes sensitized with Re-LPS. Adv. Exp. Med. Biol. 256, 287-299.
    • (1990) Adv. Exp. Med. Biol , vol.256 , pp. 287-299
    • Hirata, M.1    Yoshida, M.2    Inada, K.3    Kirikae, T.4
  • 60
    • 0029620277 scopus 로고
    • Lactoferrin-lipopolysaccharide interaction: Involvement of the 28-34 loop region of human lactoferrin in the high-affinity binding to Escherichia coli 055B5 lipopolysaccharide
    • Elass-Rochard, E., Roseanu, A., Legrand, D., Trif, M., Salmon, V., Motas, C., Montreuil, J. and Spik, G. (1995) Lactoferrin-lipopolysaccharide interaction: involvement of the 28-34 loop region of human lactoferrin in the high-affinity binding to Escherichia coli 055B5 lipopolysaccharide. Biochem. J. 312 (Pt 3), 839-845.
    • (1995) Biochem. J , vol.312 , Issue.PART 3 , pp. 839-845
    • Elass-Rochard, E.1    Roseanu, A.2    Legrand, D.3    Trif, M.4    Salmon, V.5    Motas, C.6    Montreuil, J.7    Spik, G.8
  • 62
    • 0021799698 scopus 로고
    • Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS)
    • Morita, T., Ohtsubo, S., Nakamura, T., Tanaka, S., Iwanaga, S., Ohashi, K. and Niwa, M. (1985) Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS). J. Biochem. (Tokyo) 97, 1611-1620.
    • (1985) J. Biochem. (Tokyo) , vol.97 , pp. 1611-1620
    • Morita, T.1    Ohtsubo, S.2    Nakamura, T.3    Tanaka, S.4    Iwanaga, S.5    Ohashi, K.6    Niwa, M.7
  • 63
    • 0027171383 scopus 로고
    • Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 A resolution
    • Hoess, A., Watson, S., Siber, G. R. and Liddington, R. (1993) Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 A resolution. EMBO J. 12, 3351-3356.
    • (1993) EMBO J , vol.12 , pp. 3351-3356
    • Hoess, A.1    Watson, S.2    Siber, G.R.3    Liddington, R.4
  • 64
    • 0035674626 scopus 로고    scopus 로고
    • CD14 and LBP in endotoxemia and infections caused by Gram-negative bacteria
    • Heumann, D. (2001) CD14 and LBP in endotoxemia and infections caused by Gram-negative bacteria. J. Endotoxin Res. 7, 439-441.
    • (2001) J. Endotoxin Res , vol.7 , pp. 439-441
    • Heumann, D.1
  • 68
    • 0026599845 scopus 로고
    • The role of bactericidal/permeability-increasing protein as a natural inhibitor of bacterial endotoxin
    • Marra, M. N., Wilde, C. G., Collins, M. S., Snable, J. L., Thornton, M. B. and Scott, R. W. (1992) The role of bactericidal/permeability-increasing protein as a natural inhibitor of bacterial endotoxin. J. Immunol. 148, 532-537.
    • (1992) J. Immunol , vol.148 , pp. 532-537
    • Marra, M.N.1    Wilde, C.G.2    Collins, M.S.3    Snable, J.L.4    Thornton, M.B.5    Scott, R.W.6
  • 70
    • 0029460562 scopus 로고
    • Structure and functions of endotoxin-binding peptides derived from CAP18
    • Hirata, M., Zhong, J., Wright, S. C. and Larrick, J. W. (1995) Structure and functions of endotoxin-binding peptides derived from CAP18. Prog. Clin. Biol. Res. 392, 317-326.
    • (1995) Prog. Clin. Biol. Res , vol.392 , pp. 317-326
    • Hirata, M.1    Zhong, J.2    Wright, S.C.3    Larrick, J.W.4
  • 71
    • 0032193238 scopus 로고    scopus 로고
    • A synthetic lipopolysaccharide-binding peptide based on amino acids 27-39 of serum amyloid P component inhibits lipopolysaccharide- induced responses in human blood
    • de Haas, C. J., van der Tol, M. E., Van Kessel, K. P., Verhoef, J. and Van Strijp, J. A. (1998) A synthetic lipopolysaccharide-binding peptide based on amino acids 27-39 of serum amyloid P component inhibits lipopolysaccharide- induced responses in human blood. J. Immunol. 161, 3607-3615.
    • (1998) J. Immunol , vol.161 , pp. 3607-3615
    • de Haas, C.J.1    van der Tol, M.E.2    Van Kessel, K.P.3    Verhoef, J.4    Van Strijp, J.A.5
  • 72
    • 0034650823 scopus 로고    scopus 로고
    • Cutting edge: Cationic anti-microbial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein
    • Scott, M. G., Vreugdenhil, A. C., Buurman, W. A., Hancock, R. E. and Gold, M. R. (2000) Cutting edge: cationic anti-microbial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein. J. Immunol. 164, 549-553.
    • (2000) J. Immunol , vol.164 , pp. 549-553
    • Scott, M.G.1    Vreugdenhil, A.C.2    Buurman, W.A.3    Hancock, R.E.4    Gold, M.R.5
  • 73
    • 0141781239 scopus 로고    scopus 로고
    • Inhibition of LPS-responses by synthetic peptides derived from LBP associates with the ability of the peptides to block LBP-LPS interaction
    • Arana Mde, J., Vallespi, M. G., Chinea, G., Vallespi, G. V., Rodriguez-Alonso, I., Garay, H. E., Buurman, W. A. and Reyes, O. (2003) Inhibition of LPS-responses by synthetic peptides derived from LBP associates with the ability of the peptides to block LBP-LPS interaction. J. Endotoxin Res. 9, 281-291.
    • (2003) J. Endotoxin Res , vol.9 , pp. 281-291
    • Arana Mde, J.1    Vallespi, M.G.2    Chinea, G.3    Vallespi, G.V.4    Rodriguez-Alonso, I.5    Garay, H.E.6    Buurman, W.A.7    Reyes, O.8
  • 74
    • 3843136392 scopus 로고    scopus 로고
    • Structure/function studies of an endotoxin-neutralizing peptide derived from bactericidal/permeability-increasing protein
    • Wasiluk, K. R., Leslie, D. B., Vietzen, P. S., Mayo, K. H. and Dunn, D. L. (2004) Structure/function studies of an endotoxin-neutralizing peptide derived from bactericidal/permeability-increasing protein. Surgery 136, 253-260.
    • (2004) Surgery , vol.136 , pp. 253-260
    • Wasiluk, K.R.1    Leslie, D.B.2    Vietzen, P.S.3    Mayo, K.H.4    Dunn, D.L.5
  • 75
    • 0032007337 scopus 로고    scopus 로고
    • Role of the bactericidal/permeability- increasing protein in host defence
    • Elsbach, P. and Weiss, J. (1998) Role of the bactericidal/permeability- increasing protein in host defence. Curr. Opin. Immunol. 10, 45-49.
    • (1998) Curr. Opin. Immunol , vol.10 , pp. 45-49
    • Elsbach, P.1    Weiss, J.2
  • 77
    • 0033862396 scopus 로고    scopus 로고
    • Bactericidal and endotoxin neutralizing activity of a peptide derived from Limulus antilipopolysaccharide factor
    • Weiss, C. A., 3rd, Wasiluk, K. R., Kellogg, T. A. and Dunn, D. L. (2000) Bactericidal and endotoxin neutralizing activity of a peptide derived from Limulus antilipopolysaccharide factor. Surgery 128, 339-344.
    • (2000) Surgery , vol.128 , pp. 339-344
    • Weiss 3rd, C.A.1    Wasiluk, K.R.2    Kellogg, T.A.3    Dunn, D.L.4
  • 78
    • 0029097115 scopus 로고
    • Structure, function, and membrane integration of defensins
    • White, S. H., Wimley, W. C. and Selsted, M. E. (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
  • 79
  • 80
    • 0029087339 scopus 로고
    • Peptide derivatives of three distinct lipopolysaccharide binding proteins inhibit lipopolysaccharide-induced tumor necrosis factor-alpha secretion in vitro
    • Battafaraono, R. J., Dahlberg, P. S., Ratz, C. A., Johnston, J. W., Gray, B. H., Haseman, J. R., Mayo, K. H. and Dunn, D. L. (1995) Peptide derivatives of three distinct lipopolysaccharide binding proteins inhibit lipopolysaccharide-induced tumor necrosis factor-alpha secretion in vitro. Surgery 118, 318-324.
    • (1995) Surgery , vol.118 , pp. 318-324
    • Battafaraono, R.J.1    Dahlberg, P.S.2    Ratz, C.A.3    Johnston, J.W.4    Gray, B.H.5    Haseman, J.R.6    Mayo, K.H.7    Dunn, D.L.8
  • 81
    • 34548831343 scopus 로고    scopus 로고
    • A peptide derived from human bactericidal/permeability- increasing protein (BPI) exerts bactericidal activity against Gram-negative bacterial isolates obtained from clinical cases of bovine mastitis
    • Chockalingam, A., McKinney, C. E., Rinaldi, M., Zarlenga, D. S. and Bannerman, D. D. (2007) A peptide derived from human bactericidal/permeability- increasing protein (BPI) exerts bactericidal activity against Gram-negative bacterial isolates obtained from clinical cases of bovine mastitis. Vet. Microbiol. 125, 80-90.
    • (2007) Vet. Microbiol , vol.125 , pp. 80-90
    • Chockalingam, A.1    McKinney, C.E.2    Rinaldi, M.3    Zarlenga, D.S.4    Bannerman, D.D.5
  • 83
    • 0029128705 scopus 로고
    • The solution structure of the active domain of CAP18- a lipopolysaccharide binding protein from rabbit leukocytes
    • Chen, C., Brock, R., Luh, F., Chou, P. J., Larrick, J. W., Huang, R. F. and Huang, T. H. (1995) The solution structure of the active domain of CAP18- a lipopolysaccharide binding protein from rabbit leukocytes. FEBS Lett. 370, 46-52.
    • (1995) FEBS Lett , vol.370 , pp. 46-52
    • Chen, C.1    Brock, R.2    Luh, F.3    Chou, P.J.4    Larrick, J.W.5    Huang, R.F.6    Huang, T.H.7
  • 84
    • 0027158358 scopus 로고
    • Synthetic bactericidal peptide based on CAP37: A 37-kDa human neutrophil granule-associated cationic antimicrobial protein chemotactic for monocytes
    • Pereira, H. A., Erdem, I., Pohl, J. and Spitznagel, J. K. (1993) Synthetic bactericidal peptide based on CAP37: a 37-kDa human neutrophil granule-associated cationic antimicrobial protein chemotactic for monocytes. Proc. Natl. Acad. Sci. USA 90, 4733-4737.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4733-4737
    • Pereira, H.A.1    Erdem, I.2    Pohl, J.3    Spitznagel, J.K.4
  • 85
    • 0029028016 scopus 로고
    • Lipopolysaccharide (LPS) neutralizing peptides reveal a lipid A binding site of LPS binding protein
    • Taylor, A. H., Heavner, G., Nedelman, M., Sherris, D., Brunt, E., Knight, D. and Ghrayeb, J. (1995) Lipopolysaccharide (LPS) neutralizing peptides reveal a lipid A binding site of LPS binding protein. J. Biol. Chem. 270, 17934-17938.
    • (1995) J. Biol. Chem , vol.270 , pp. 17934-17938
    • Taylor, A.H.1    Heavner, G.2    Nedelman, M.3    Sherris, D.4    Brunt, E.5    Knight, D.6    Ghrayeb, J.7
  • 86
    • 0032975547 scopus 로고    scopus 로고
    • Neutralization of endotoxin in vitro and in vivo by a human lactoferrin-derived peptide
    • Zhang, G. H., Mann, D. M. and Tsai, C. M. (1999) Neutralization of endotoxin in vitro and in vivo by a human lactoferrin-derived peptide. Infect. Immun. 67, 1353-1358.
    • (1999) Infect. Immun , vol.67 , pp. 1353-1358
    • Zhang, G.H.1    Mann, D.M.2    Tsai, C.M.3
  • 87
    • 0029824838 scopus 로고    scopus 로고
    • Anti-endotoxin activity of cationic peptide antimicrobial agents
    • Gough, M., Hancock, R. E. and Kelly, N. M. (1996) Anti-endotoxin activity of cationic peptide antimicrobial agents. Infect. Immun. 64, 4922-4927.
    • (1996) Infect. Immun , vol.64 , pp. 4922-4927
    • Gough, M.1    Hancock, R.E.2    Kelly, N.M.3
  • 88
    • 0017119987 scopus 로고
    • Binding of polymyxin B to the lipid A portion of bacterial lipopolysaccharides
    • Morrison, D. C. and Jacobs, D. M. (1976) Binding of polymyxin B to the lipid A portion of bacterial lipopolysaccharides. Immunochemistry 13, 813-818.
    • (1976) Immunochemistry , vol.13 , pp. 813-818
    • Morrison, D.C.1    Jacobs, D.M.2
  • 89
    • 4344638189 scopus 로고    scopus 로고
    • De novo design of potent antimicrobial peptides
    • Frecer, V., Ho, B. and Ding, J. L. (2004) De novo design of potent antimicrobial peptides. Antimicrob. Agents Chemother. 48, 3349-3357.
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 3349-3357
    • Frecer, V.1    Ho, B.2    Ding, J.L.3
  • 90
    • 0032916291 scopus 로고    scopus 로고
    • Host defence (cationic) peptides: What is their future clinical potential?
    • Hancock, R. E. (1999) Host defence (cationic) peptides: what is their future clinical potential? Drugs 57, 469-473.
    • (1999) Drugs , vol.57 , pp. 469-473
    • Hancock, R.E.1
  • 91
    • 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
  • 92
    • 13444269022 scopus 로고    scopus 로고
    • The ancient origin of the complement system
    • Zhu, Y., Thangamani, S., Ho, B. and Ding, J. L. (2005) The ancient origin of the complement system. EMBO 24, 382-394.
    • (2005) EMBO , vol.24 , pp. 382-394
    • Zhu, Y.1    Thangamani, S.2    Ho, B.3    Ding, J.L.4
  • 93
    • 34047259526 scopus 로고    scopus 로고
    • Preservation of antimicrobial properties of complement peptide C3a, from invertebrates to humans
    • Pasupuleti, M., Walse, B., Nordahl, E. A., Morgelin, M., Malmsten, M. and Schmidtchen, A. (2007) Preservation of antimicrobial properties of complement peptide C3a, from invertebrates to humans. J. Biol. Chem. 282, 2520-2528.
    • (2007) J. Biol. Chem , vol.282 , pp. 2520-2528
    • Pasupuleti, M.1    Walse, B.2    Nordahl, E.A.3    Morgelin, M.4    Malmsten, M.5    Schmidtchen, A.6
  • 94
    • 0035920142 scopus 로고    scopus 로고
    • Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides
    • Nagai, T., Osaki, T. and Kawabata, S. (2001) Functional conversion of hemocyanin to phenoloxidase by horseshoe crab antimicrobial peptides. J. Biol. Chem. 276, 27166-27170.
    • (2001) J. Biol. Chem , vol.276 , pp. 27166-27170
    • Nagai, T.1    Osaki, T.2    Kawabata, S.3
  • 95
    • 34548785607 scopus 로고    scopus 로고
    • Respiratory protein-generated reactive oxygen species as an antimicrobial strategy
    • Jiang, N., Tan, N. S., Ho, B. and Ding, J. L. (2007) Respiratory protein-generated reactive oxygen species as an antimicrobial strategy. Nat. Immunol. 8, 1114-1122.
    • (2007) Nat. Immunol , vol.8 , pp. 1114-1122
    • Jiang, N.1    Tan, N.S.2    Ho, B.3    Ding, J.L.4
  • 96
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure
    • Nakamura, T., Furunaka, H., Miyata, T., Tokunaga, F., Muta, T., Iwanaga, S., Niwa, M., Takao, T. and Shimonishi, Y. (1988) Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J. Biol. Chem. 263, 16709-16713.
    • (1988) J. Biol. Chem , vol.263 , pp. 16709-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6    Niwa, M.7    Takao, T.8    Shimonishi, Y.9
  • 97
    • 0025735356 scopus 로고
    • Limulus factor C. An endotoxin-sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like, and lectin-like domains
    • Muta, T., Miyata, T., Misumi, Y., Tokunaga, F., Nakamura, T., Toh, Y., Ikehara, Y. and Iwanaga, S. (1991) Limulus factor C. An endotoxin-sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like, and lectin-like domains. J. Biol. Chem. 266, 6554-6561.
    • (1991) J. Biol. Chem , vol.266 , pp. 6554-6561
    • Muta, T.1    Miyata, T.2    Misumi, Y.3    Tokunaga, F.4    Nakamura, T.5    Toh, Y.6    Ikehara, Y.7    Iwanaga, S.8
  • 98
    • 0027328307 scopus 로고
    • Two forms of factor C from the amoebocytes of Carcinoscorpius rotundicauda: Purification and characterisation
    • Ding, J. L., Navas, M. A., 3rd and Ho, B. (1993) Two forms of factor C from the amoebocytes of Carcinoscorpius rotundicauda: purification and characterisation. Biochim. Biophys. Acta 1202, 149-156.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 149-156
    • Ding, J.L.1    Navas 3rd, M.A.2    Ho, B.3
  • 99
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • Iwanaga, S. and Lee, B. L. (2005) Recent advances in the innate immunity of invertebrate animals. J. Biochem. Mol. Biol. 38, 128-150.
    • (2005) J. Biochem. Mol. Biol , vol.38 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 100
    • 0036467504 scopus 로고    scopus 로고
    • The molecular basis of innate immunity in the horseshoe crab
    • Iwanaga, S. (2002) The molecular basis of innate immunity in the horseshoe crab, Curr. Opin. Immunol. 14, 87-95.
    • (2002) Curr. Opin. Immunol , vol.14 , pp. 87-95
    • Iwanaga, S.1
  • 102
    • 0029257172 scopus 로고
    • Molecular cloning and sequence analysis of factor C cDNA from the Singapore horseshoe crab, Carcinoscorpius rotundicauda
    • Ding, J. L., Navas, M. A., 3rd and Ho, B. (1995) Molecular cloning and sequence analysis of factor C cDNA from the Singapore horseshoe crab, Carcinoscorpius rotundicauda. Mol. Mar. Biol. Biotechnol. 4, 90-103.
    • (1995) Mol. Mar. Biol. Biotechnol , vol.4 , pp. 90-103
    • Ding, J.L.1    Navas 3rd, M.A.2    Ho, B.3
  • 103
    • 0029692452 scopus 로고    scopus 로고
    • Clotting and immune defense in Limulidae
    • Muta, T. and Iwanaga, S. (1996) Clotting and immune defense in Limulidae. Prog. Mol. Subcell. Biol. 15, 154-189.
    • (1996) Prog. Mol. Subcell. Biol , vol.15 , pp. 154-189
    • Muta, T.1    Iwanaga, S.2
  • 104
    • 0021015452 scopus 로고
    • An improved Limulus gelation assay
    • Ho, B. (1983) An improved Limulus gelation assay. Microbios. Lett. 24, 81-84.
    • (1983) Microbios. Lett , vol.24 , pp. 81-84
    • Ho, B.1
  • 105
    • 0020398633 scopus 로고
    • Endotoxin-induced degranulation of the Limulus amebocyte
    • Armstrong, P. B. and Rickles, F. R. (1982) Endotoxin-induced degranulation of the Limulus amebocyte. Exp. Cell Res. 140, 15-24.
    • (1982) Exp. Cell Res , vol.140 , pp. 15-24
    • Armstrong, P.B.1    Rickles, F.R.2
  • 106
    • 34548449911 scopus 로고    scopus 로고
    • Recombinant Factor C competes against LBP to bind lipopolysaccharide and neutralizes the endotoxicity
    • Li, P., Ho, B. and Ding, J. L. (2007) Recombinant Factor C competes against LBP to bind lipopolysaccharide and neutralizes the endotoxicity. J. Endotoxin Res. 13, 150-157.
    • (2007) J. Endotoxin Res , vol.13 , pp. 150-157
    • Li, P.1    Ho, B.2    Ding, J.L.3
  • 107
    • 0035426586 scopus 로고    scopus 로고
    • A new era in pyrogen testing
    • Ding, J. L. and Ho, B. (2001) A new era in pyrogen testing. Trends Biotechnol. 19, 277-281.
    • (2001) Trends Biotechnol , vol.19 , pp. 277-281
    • Ding, J.L.1    Ho, B.2
  • 108
    • 0014799610 scopus 로고
    • Detection of endotoxin in human blood and demonstration of an inhibitor
    • Levin, J., Tomasulo, P. A. and Oser, R. S. (1970) Detection of endotoxin in human blood and demonstration of an inhibitor. J. Lab. Clin. Med. 75, 903-911.
    • (1970) J. Lab. Clin. Med , vol.75 , pp. 903-911
    • Levin, J.1    Tomasulo, P.A.2    Oser, R.S.3
  • 109
    • 0029556203 scopus 로고
    • Expression of Carcinoscorpius rotundicauda factor C cDNA
    • Roopashree, S. D., Chai, C., Ho, B. and Ding, J. L. (1995) Expression of Carcinoscorpius rotundicauda factor C cDNA. Biochem. Mol. Biol. Int. 35, 841-849.
    • (1995) Biochem. Mol. Biol. Int , vol.35 , pp. 841-849
    • Roopashree, S.D.1    Chai, C.2    Ho, B.3    Ding, J.L.4
  • 110
    • 0030969606 scopus 로고    scopus 로고
    • Expression of full length and deletion homologues of Carcinoscorpius rotundicauda Factor C in Saccharomyces cerevisiae: Immunoreactivity and endotoxin binding
    • Ding, J. L., Chai, C., Pui, A. W. M. and Ho, B. (1997) Expression of full length and deletion homologues of Carcinoscorpius rotundicauda Factor C in Saccharomyces cerevisiae: immunoreactivity and endotoxin binding. J. Endotoxin Res. 4, 33-43.
    • (1997) J. Endotoxin Res , vol.4 , pp. 33-43
    • Ding, J.L.1    Chai, C.2    Pui, A.W.M.3    Ho, B.4
  • 111
    • 0030947963 scopus 로고    scopus 로고
    • Recombinant COS-1 cells express Carcinoscorpius rotundicauda Factor C
    • Roopashree, S. D., Ho, B. and Ding, J. L. (1997) Recombinant COS-1 cells express Carcinoscorpius rotundicauda Factor C. Biotech. Lett. 19, 357-361.
    • (1997) Biotech. Lett , vol.19 , pp. 357-361
    • Roopashree, S.D.1    Ho, B.2    Ding, J.L.3
  • 112
    • 0037184084 scopus 로고    scopus 로고
    • Modular arrangement and secretion of a multidomain serine protease. Evidence for involvement of proline-rich region and N-glycans in the secretion pathway
    • Wang, J., Tan, N. S., Ho, B. and Ding, J. L. (2002) Modular arrangement and secretion of a multidomain serine protease. Evidence for involvement of proline-rich region and N-glycans in the secretion pathway. J. Biol. Chem. 277, 36363-36372.
    • (2002) J. Biol. Chem , vol.277 , pp. 36363-36372
    • Wang, J.1    Tan, N.S.2    Ho, B.3    Ding, J.L.4
  • 113
    • 0035896016 scopus 로고    scopus 로고
    • Solution structure and dynamics of the central CCP module pair of a poxvirus complement control protein
    • Henderson, C. E., Bromek, K., Mullin, N. P., Smith, B. O., Uhrin, D. and Barlow, P. N. (2001) Solution structure and dynamics of the central CCP module pair of a poxvirus complement control protein. J. Mol. Biol. 307, 323-339.
    • (2001) J. Mol. Biol , vol.307 , pp. 323-339
    • Henderson, C.E.1    Bromek, K.2    Mullin, N.P.3    Smith, B.O.4    Uhrin, D.5    Barlow, P.N.6
  • 114
    • 0343092000 scopus 로고    scopus 로고
    • High-affinity LPS binding domain(s) in recombinant factor C of a horseshoe crab neutralizes LPS-induced lethality
    • Tan, N. S., Ho, B. and Ding, J. L. (2000) High-affinity LPS binding domain(s) in recombinant factor C of a horseshoe crab neutralizes LPS-induced lethality. FASEB J. 14, 859-870.
    • (2000) FASEB J , vol.14 , pp. 859-870
    • Tan, N.S.1    Ho, B.2    Ding, J.L.3
  • 115
    • 0033813364 scopus 로고    scopus 로고
    • Definition of endotoxin binding sites in horseshoe crab factor C recombinant sushi proteins and neutralization of endotoxin by sushi peptides
    • Tan, N. S., Ng, M. L., Yau, Y. H., Chong, P. K., Ho, B. and Ding, J. L. (2000) Definition of endotoxin binding sites in horseshoe crab factor C recombinant sushi proteins and neutralization of endotoxin by sushi peptides. FASEB J. 14, 1801-1813.
    • (2000) FASEB J , vol.14 , pp. 1801-1813
    • Tan, N.S.1    Ng, M.L.2    Yau, Y.H.3    Chong, P.K.4    Ho, B.5    Ding, J.L.6
  • 116
    • 0033770364 scopus 로고    scopus 로고
    • The role of polar and facial amphipathic character in determining lipopolysaccharide-binding properties in synthetic cationic peptides
    • David, S. A., Awasthi, S. K. and Balaram, P. (2000)The role of polar and facial amphipathic character in determining lipopolysaccharide-binding properties in synthetic cationic peptides. J. Endotoxin Res. 6, 249-256.
    • (2000) J. Endotoxin Res , vol.6 , pp. 249-256
    • David, S.A.1    Awasthi, S.K.2    Balaram, P.3
  • 117
    • 0034806998 scopus 로고    scopus 로고
    • High therapeutic index of factor C Sushi peptides: Potent antimicrobials against Pseudomonas aeruginosa
    • Yau, Y. H., Ho, B., Tan, N. S., Ng, M. L. and Ding, J. L. (2001) High therapeutic index of factor C Sushi peptides: potent antimicrobials against Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 45, 2820-2825.
    • (2001) Antimicrob. Agents Chemother , vol.45 , pp. 2820-2825
    • Yau, Y.H.1    Ho, B.2    Tan, N.S.3    Ng, M.L.4    Ding, J.L.5
  • 118
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host defense peptides
    • Maloy, W. L. and Kari, U. P. (1995) Structure-activity studies on magainins and other host defense peptides. Biopolymers 37, 105-122.
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 119
    • 0034866022 scopus 로고    scopus 로고
    • Conformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance
    • Bak, M., Bywater, R. P., Hohwy, M., Thomsen, J. K., Adelhorst, K., Jakobsen, H. J., Sorensen, O. W. and Nielsen, N. C. (2001) Conformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance. Biophys. J. 81, 1684-1698.
    • (2001) Biophys. J , vol.81 , pp. 1684-1698
    • Bak, M.1    Bywater, R.P.2    Hohwy, M.3    Thomsen, J.K.4    Adelhorst, K.5    Jakobsen, H.J.6    Sorensen, O.W.7    Nielsen, N.C.8
  • 120
    • 0023746603 scopus 로고
    • Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils
    • Romeo, D., Skerlavaj, B., Bolognesi, M. and Gennaro, R. (1988) Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J. Biol. Chem. 263, 9573-9575.
    • (1988) J. Biol. Chem , vol.263 , pp. 9573-9575
    • Romeo, D.1    Skerlavaj, B.2    Bolognesi, M.3    Gennaro, R.4
  • 121
    • 84903421873 scopus 로고    scopus 로고
    • Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin
    • Hwang, P. M., Zhou, N., Shan, X., Arrowsmith, C. H. and Vogel, H. J. (1998) Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry 37, 4288-4298.
    • (1998) Biochemistry , vol.37 , pp. 4288-4298
    • Hwang, P.M.1    Zhou, N.2    Shan, X.3    Arrowsmith, C.H.4    Vogel, H.J.5
  • 123
  • 124
    • 0035836463 scopus 로고    scopus 로고
    • Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from Rhesus macaque leukocytes
    • Trabi, M., Schirra, H. J. and Craik, D. J. (2001) Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from Rhesus macaque leukocytes. Biochemistry 40, 4211-4221.
    • (2001) Biochemistry , vol.40 , pp. 4211-4221
    • Trabi, M.1    Schirra, H.J.2    Craik, D.J.3
  • 125
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger, B. (1997) Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156, 197-211.
    • (1997) J. Membr. Biol , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 126
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R. M. and Vogel, H. J. (1999) Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462, 11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 127
    • 0035795730 scopus 로고    scopus 로고
    • Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance
    • Mozsolits, H., Wirth, H. J., Werkmeister, J. and Aguilar, M. I. (2001) Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance. Biochim. Biophys. Acta 1512, 64-76.
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 64-76
    • Mozsolits, H.1    Wirth, H.J.2    Werkmeister, J.3    Aguilar, M.I.4
  • 128
    • 4644245658 scopus 로고    scopus 로고
    • Helix induction in antimicrobial peptides by alginate in biofilms
    • Chan, C., Burrows, L. L. and Deber, C. M. (2004) Helix induction in antimicrobial peptides by alginate in biofilms. J. Biol. Chem. 279, 38749-38754.
    • (2004) J. Biol. Chem , vol.279 , pp. 38749-38754
    • Chan, C.1    Burrows, L.L.2    Deber, C.M.3
  • 129
    • 0033979845 scopus 로고    scopus 로고
    • Phylloxin, a novel peptide antibiotic of the dermaseptin family of antimicrobial/opioid peptide precursors
    • Pierre, T. N., Seon, A. A., Amiche, M. and Nicolas, P. (2000) Phylloxin, a novel peptide antibiotic of the dermaseptin family of antimicrobial/opioid peptide precursors. Eur. J. Biochem. 267, 370-378.
    • (2000) Eur. J. Biochem , vol.267 , pp. 370-378
    • Pierre, T.N.1    Seon, A.A.2    Amiche, M.3    Nicolas, P.4
  • 130
    • 0028208901 scopus 로고
    • Orientational and aggregational states of magainin 2 in phospholipid bilayers
    • Matsuzaki, K., Murase, O., Tokuda, H., Funakoshi, S., Fujii, N. and Miyajima, K. (1994) Orientational and aggregational states of magainin 2 in phospholipid bilayers. Biochemistry 33, 3342-3349.
    • (1994) Biochemistry , vol.33 , pp. 3342-3349
    • Matsuzaki, K.1    Murase, O.2    Tokuda, H.3    Funakoshi, S.4    Fujii, N.5    Miyajima, K.6
  • 131
    • 0039981711 scopus 로고    scopus 로고
    • The tendency of magainin to associate upon binding to phospholipid bilayers
    • Schumann, M., Dathe, M., Wieprecht, T., Beyermann, M. and Bienert, M. (1997) The tendency of magainin to associate upon binding to phospholipid bilayers. Biochemistry 36, 4345-4351.
    • (1997) Biochemistry , vol.36 , pp. 4345-4351
    • Schumann, M.1    Dathe, M.2    Wieprecht, T.3    Beyermann, M.4    Bienert, M.5
  • 132
    • 33745152360 scopus 로고    scopus 로고
    • Li, P., Sun, M., Wohland, T., Ho, B. and Ding, J. L. (2006) The molecular mechanism of interaction between sushi peptide and Pseudomonas endotoxin. Cell. Mol. Immunol. 3, 21-28.
    • Li, P., Sun, M., Wohland, T., Ho, B. and Ding, J. L. (2006) The molecular mechanism of interaction between sushi peptide and Pseudomonas endotoxin. Cell. Mol. Immunol. 3, 21-28.
  • 133
    • 9644252819 scopus 로고    scopus 로고
    • Perturbation of Lipopolysaccharide (LPS) Micelles by Sushi 3 (S3) antimicrobial peptide. The importance of an intermolecular disulfide bond in S3 dimer for binding, disruption, and neutralization of LPS
    • Li, P., Wohland, T., Ho, B. and Ding, J. L. (2004) Perturbation of Lipopolysaccharide (LPS) Micelles by Sushi 3 (S3) antimicrobial peptide. The importance of an intermolecular disulfide bond in S3 dimer for binding, disruption, and neutralization of LPS. J. Biol. Chem. 279, 50150-50156.
    • (2004) J. Biol. Chem , vol.279 , pp. 50150-50156
    • Li, P.1    Wohland, T.2    Ho, B.3    Ding, J.L.4
  • 134
    • 33646474970 scopus 로고    scopus 로고
    • Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy
    • Porcelli, F., Buck-Koehntop, B. A., Thennarasu, S., Ramamoorthy, A. and Veglia, G. (2006) Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy. Biochemistry 45, 5793-5799.
    • (2006) Biochemistry , vol.45 , pp. 5793-5799
    • Porcelli, F.1    Buck-Koehntop, B.A.2    Thennarasu, S.3    Ramamoorthy, A.4    Veglia, G.5
  • 135
    • 0037159195 scopus 로고    scopus 로고
    • 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.
    • 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.
  • 136
    • 0141919277 scopus 로고    scopus 로고
    • Human salivary MUC7 mucin peptides: Effect of size, charge and cysteine residues on antifungal activity
    • Situ, H., Wei, G., Smith, C. J., Mashhoon, S. and Bobek, L. A. (2003) Human salivary MUC7 mucin peptides: effect of size, charge and cysteine residues on antifungal activity. Biochem. J. 375, 175-182.
    • (2003) Biochem. J , vol.375 , pp. 175-182
    • Situ, H.1    Wei, G.2    Smith, C.J.3    Mashhoon, S.4    Bobek, L.A.5
  • 138
    • 0037184958 scopus 로고    scopus 로고
    • Correlations of cationic charges with salt sensitivity and microbial specificity of cystine-stabilized beta -strand antimicrobial peptides
    • Tam, J. P., Lu, Y. A. and Yang, J. L. (2002) Correlations of cationic charges with salt sensitivity and microbial specificity of cystine-stabilized beta -strand antimicrobial peptides. J. Biol. Chem. 277, 50450-50456.
    • (2002) J. Biol. Chem , vol.277 , pp. 50450-50456
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3
  • 139
    • 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., Hunter, H. N., Aseyev, V., Starner, T. D., Wiencek, J. M., McCray, P. B. Jr., Tack, B. F. and Vogel, H. J. (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 Jr., P.B.6    Tack, B.F.7    Vogel, H.J.8
  • 140
    • 4444246183 scopus 로고    scopus 로고
    • Increased diversity of intestinal anti-microbial peptides by covalent dimer formation
    • Hornef, M. W., Putsep, K., Karlsson, J., Refai, E. and Andersson, M. (2004) Increased diversity of intestinal anti-microbial peptides by covalent dimer formation. Nat. Immunol. 5, 836-843.
    • (2004) Nat. Immunol , vol.5 , pp. 836-843
    • Hornef, M.W.1    Putsep, K.2    Karlsson, J.3    Refai, E.4    Andersson, M.5
  • 141
    • 0037457904 scopus 로고    scopus 로고
    • Enhanced membrane permeabilization and antibacterial activity of a disulfide-dimerized magainin analogue
    • Dempsey, C. E., Ueno, S. and Avison, M. B. (2003) Enhanced membrane permeabilization and antibacterial activity of a disulfide-dimerized magainin analogue. Biochemistry 42, 402-409.
    • (2003) Biochemistry , vol.42 , pp. 402-409
    • Dempsey, C.E.1    Ueno, S.2    Avison, M.B.3
  • 142
    • 0141705727 scopus 로고    scopus 로고
    • Tandem repeats of Sushi3 peptide with enhanced LPS-binding and -neutralizing activities
    • Li, C., Ng, M. L., Zhu, Y., Ho, B. and Ding, J. L. (2003) Tandem repeats of Sushi3 peptide with enhanced LPS-binding and -neutralizing activities. Protein Eng. 16, 629-635.
    • (2003) Protein Eng , vol.16 , pp. 629-635
    • Li, C.1    Ng, M.L.2    Zhu, Y.3    Ho, B.4    Ding, J.L.5
  • 143
    • 0029928757 scopus 로고    scopus 로고
    • The role of hemolymph coagulation in innate immunity
    • Muta, T. and Iwanaga, S. (1996) The role of hemolymph coagulation in innate immunity. Curr. Opin. Immunol. 8, 41-47.
    • (1996) Curr. Opin. Immunol , vol.8 , pp. 41-47
    • Muta, T.1    Iwanaga, S.2
  • 144
    • 0742305683 scopus 로고    scopus 로고
    • A serine protease zymogen functions as a pattern-recognition receptor for lipopolysaccharides
    • Ariki, S., Koori, K., Osaki, T., Motoyama, K., Inamori, K. and Kawabata, S. (2004) A serine protease zymogen functions as a pattern-recognition receptor for lipopolysaccharides. Proc. Natl. Acad. Sci. USA 101, 953-958.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 953-958
    • Ariki, S.1    Koori, K.2    Osaki, T.3    Motoyama, K.4    Inamori, K.5    Kawabata, S.6
  • 145
    • 0028286765 scopus 로고
    • Lipopolysaccharide (LPS) binding protein, truncated at Ile-197, binds LPS but does not transfer LPS to CD14
    • Han, J., Mathison, J. C., Ulevitch, R. J. and Tobias, P. S. (1994) Lipopolysaccharide (LPS) binding protein, truncated at Ile-197, binds LPS but does not transfer LPS to CD14. J. Biol. Chem. 269, 8172-8175.
    • (1994) J. Biol. Chem , vol.269 , pp. 8172-8175
    • Han, J.1    Mathison, J.C.2    Ulevitch, R.J.3    Tobias, P.S.4
  • 146
    • 1942454707 scopus 로고    scopus 로고
    • HP(2- 9)-magainin 2(1-12), a synthetic hybrid peptide, exerts its antifungal effect on Candida albicans by damaging the plasma membrane
    • Park, Y., Lee, D. G. and Hahm, K. S. (2004) HP(2- 9)-magainin 2(1-12), a synthetic hybrid peptide, exerts its antifungal effect on Candida albicans by damaging the plasma membrane. J. Pept. Sci. 10, 204-209.
    • (2004) J. Pept. Sci , vol.10 , pp. 204-209
    • Park, Y.1    Lee, D.G.2    Hahm, K.S.3
  • 148
    • 0034824532 scopus 로고    scopus 로고
    • The effect of charge increase on the specificity and activity of a short antimicrobial peptide
    • Hong, S. Y., Park, T. G. and Lee, K. H. (2001) The effect of charge increase on the specificity and activity of a short antimicrobial peptide. Peptides 22, 1669-1674.
    • (2001) Peptides , vol.22 , pp. 1669-1674
    • Hong, S.Y.1    Park, T.G.2    Lee, K.H.3
  • 149
    • 21244432036 scopus 로고    scopus 로고
    • Temperature dependence of the binding of endotoxins to the polycationic peptides polymyxin B and its nonapeptide
    • Brandenburg, K., David, A., Howe, J., Koch, M. H., Andra, J. and Garidel, P. (2005) Temperature dependence of the binding of endotoxins to the polycationic peptides polymyxin B and its nonapeptide. Biophys. J. 88, 1845-1858.
    • (2005) Biophys. J , vol.88 , pp. 1845-1858
    • Brandenburg, K.1    David, A.2    Howe, J.3    Koch, M.H.4    Andra, J.5    Garidel, P.6
  • 150
    • 0034727645 scopus 로고    scopus 로고
    • Interaction of polyphemusin I and structural analogs with bacterial membranes, lipopolysaccharide, and lipid monolayers
    • Zhang, L., Scott, M. G., Yan, H., Mayer, L. D. and Hancock, R. E. (2000) Interaction of polyphemusin I and structural analogs with bacterial membranes, lipopolysaccharide, and lipid monolayers. Biochemistry 39, 14504-14514.
    • (2000) Biochemistry , vol.39 , pp. 14504-14514
    • Zhang, L.1    Scott, M.G.2    Yan, H.3    Mayer, L.D.4    Hancock, R.E.5
  • 151
    • 0030037217 scopus 로고    scopus 로고
    • Transbilayer transport of ions and lipids coupled with mastoparan X translocation
    • Matsuzaki, K., Yoneyama, S., Murase, O. and Miyajima, K. (1996) Transbilayer transport of ions and lipids coupled with mastoparan X translocation. Biochemistry 35, 8450-8456.
    • (1996) Biochemistry , vol.35 , pp. 8450-8456
    • Matsuzaki, K.1    Yoneyama, S.2    Murase, O.3    Miyajima, K.4
  • 152
    • 0035882755 scopus 로고    scopus 로고
    • High-performance affinity capture-removal of bacterial pyrogen from solutions
    • Ding, J. L., Zhu, Y. and Ho, B. (2001) High-performance affinity capture-removal of bacterial pyrogen from solutions. J. Chromatogr. B Biomed. Sci. Appl. 759, 237-246.
    • (2001) J. Chromatogr. B Biomed. Sci. Appl , vol.759 , pp. 237-246
    • Ding, J.L.1    Zhu, Y.2    Ho, B.3
  • 153
    • 0030949875 scopus 로고    scopus 로고
    • Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman, M. J., Anderson, G. M., Stolzenberg, E. D., Kari, U. P., Zasloff, M. and Wilson, J. M. (1997) Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88, 553-560.
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 154
    • 0029870085 scopus 로고    scopus 로고
    • Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid
    • Smith, J. J., Travis, S. M., Greenberg, E. P. and Welsh, M. J. (1996) Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid. Cell 85, 229-236.
    • (1996) Cell , vol.85 , pp. 229-236
    • Smith, J.J.1    Travis, S.M.2    Greenberg, E.P.3    Welsh, M.J.4
  • 155
    • 22244452942 scopus 로고    scopus 로고
    • Membrane fluidity is a key modulator of membrane binding, insertion, and activity of 5-lipoxygenase
    • Pande, A. H., Qin, S. and Tatulian, S. A. (2005) Membrane fluidity is a key modulator of membrane binding, insertion, and activity of 5-lipoxygenase. Biophys. J. 88, 4084-4094.
    • (2005) Biophys. J , vol.88 , pp. 4084-4094
    • Pande, A.H.1    Qin, S.2    Tatulian, S.A.3
  • 156
    • 33847019613 scopus 로고    scopus 로고
    • Atomic force microscopy study of the antimicrobial action of Sushi peptides on Gram negative bacteria
    • Li, A., Lee, P. Y., Ho, B., Ding, J. L. and Lim, C. T. (2007) Atomic force microscopy study of the antimicrobial action of Sushi peptides on Gram negative bacteria. Biochim. Biophys. Acta 1768, 411-418.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 411-418
    • Li, A.1    Lee, P.Y.2    Ho, B.3    Ding, J.L.4    Lim, C.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.