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Volumn 46, Issue 13, 2009, Pages 2465-2473

Identification of chicken cathelicidin-2 core elements involved in antibacterial and immunomodulatory activities

Author keywords

Antibacterial activity; Cathelicidin; Chicken; Cytotoxicity; Host defense peptide; Immunomodulation; Innate immunity

Indexed keywords

CATHELICIDIN; CATHELICIDIN 2; INTERLEUKIN 10; INTERLEUKIN 6; INTERLEUKIN 8; MONOCYTE CHEMOTACTIC PROTEIN 1; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 67650508049     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2009.05.019     Document Type: Article
Times cited : (66)

References (53)
  • 3
    • 0027236794 scopus 로고
    • Structural basis of amino acid alpha helix propensity
    • Blaber M., Zhang X.-J., and Matthews B.W. Structural basis of amino acid alpha helix propensity. Science 260 (1993) 1637-1640
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.-J.2    Matthews, B.W.3
  • 4
    • 0029944101 scopus 로고    scopus 로고
    • Sepsis and cytokines: current status
    • Blackwell T.S., and Christman J.W. Sepsis and cytokines: current status. Br. J. Anaesth. 77 (1996) 110-117
    • (1996) Br. J. Anaesth. , vol.77 , pp. 110-117
    • Blackwell, T.S.1    Christman, J.W.2
  • 5
    • 33846006520 scopus 로고    scopus 로고
    • Fowlicidin-3 is an α-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities
    • Bommineni Y.R., Dai H., Gong Y.-X., Soulages J.L., Fernando S.C., DeSilva U., Prakash O., and Zhang G. Fowlicidin-3 is an α-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities. FEBS J. 274 (2007) 418-428
    • (2007) FEBS J. , vol.274 , pp. 418-428
    • Bommineni, Y.R.1    Dai, H.2    Gong, Y.-X.3    Soulages, J.L.4    Fernando, S.C.5    DeSilva, U.6    Prakash, O.7    Zhang, G.8
  • 7
  • 9
    • 0034109713 scopus 로고    scopus 로고
    • Maculatin 1.1, an anti-microbial peptide from the Australian tree frog, Litoria genimaculata solution structure and biological activity
    • Chia B.C.S., Carver J.A., Mulhern T.D., and Bowie J.H. Maculatin 1.1, an anti-microbial peptide from the Australian tree frog, Litoria genimaculata solution structure and biological activity. Eur. J. Biochem. 267 (2000) 1894-1908
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1894-1908
    • Chia, B.C.S.1    Carver, J.A.2    Mulhern, T.D.3    Bowie, J.H.4
  • 11
    • 1542564787 scopus 로고    scopus 로고
    • The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization
    • Davidson D.J., Currie A.J., Reid G.S.D., Bowdish D.M.E., MacDonald K.L., Ma R.C., Hancock R.E.W., and Speert D.P. The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization. J. Immunol. 172 (2004) 1146-1156
    • (2004) J. Immunol. , vol.172 , pp. 1146-1156
    • Davidson, D.J.1    Currie, A.J.2    Reid, G.S.D.3    Bowdish, D.M.E.4    MacDonald, K.L.5    Ma, R.C.6    Hancock, R.E.W.7    Speert, D.P.8
  • 12
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: a measure of the amphiphilicity of a helix
    • Eisenberg D., Weiss R.M., and Terwilliger T.C. The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature 299 (1982) 371-374
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 13
    • 1842581655 scopus 로고    scopus 로고
    • A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release
    • Elssner A., Duncan M., Gavrilin M., and Wewers M.D. A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release. J. Immunol. 172 (2004) 4987-4994
    • (2004) J. Immunol. , vol.172 , pp. 4987-4994
    • Elssner, A.1    Duncan, M.2    Gavrilin, M.3    Wewers, M.D.4
  • 15
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock R.E.W., and Scott M.G. The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 8856-8861
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8856-8861
    • Hancock, R.E.W.1    Scott, M.G.2
  • 17
    • 0033975319 scopus 로고    scopus 로고
    • Influence of synthetic antiendotoxin peptides on lipopolysaccharide (LPS) recognition and LPS-induced proinflammatory cytokine responses by cells expressing membrane-bound CD14
    • Iwagaki A., Porro M., and Pollack M. Influence of synthetic antiendotoxin peptides on lipopolysaccharide (LPS) recognition and LPS-induced proinflammatory cytokine responses by cells expressing membrane-bound CD14. Infect. Immun. 68 (2000) 1655-1663
    • (2000) Infect. Immun. , vol.68 , pp. 1655-1663
    • Iwagaki, A.1    Porro, M.2    Pollack, M.3
  • 20
    • 0025260032 scopus 로고
    • Side chain contributions to the stability of alpha-helical structure in peptides
    • Lyu P.C., Liff M.I., Marky L.A., and Kallenbach N.R. Side chain contributions to the stability of alpha-helical structure in peptides. Science 250 (1990) 669-673
    • (1990) Science , vol.250 , pp. 669-673
    • Lyu, P.C.1    Liff, M.I.2    Marky, L.A.3    Kallenbach, N.R.4
  • 21
    • 0030738014 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria
    • Matsuzaki K., Sugishita K., Harada M., Fujii N., and Miyajima K. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim. Biophys. Acta 1327 (1997) 119-130
    • (1997) Biochim. Biophys. Acta , vol.1327 , pp. 119-130
    • Matsuzaki, K.1    Sugishita, K.2    Harada, M.3    Fujii, N.4    Miyajima, K.5
  • 25
    • 15244352726 scopus 로고    scopus 로고
    • Antibacterial cathelicidin peptide CAP11 inhibits the lipopolysaccharide (LPS)-induced suppression of neutrophil apoptosis by blocking the binding of LPS to target cells
    • Nagaoka I., Yomogida S., Tamura H., and Hirata M. Antibacterial cathelicidin peptide CAP11 inhibits the lipopolysaccharide (LPS)-induced suppression of neutrophil apoptosis by blocking the binding of LPS to target cells. Inflamm. Res. 53 (2004) 609-622
    • (2004) Inflamm. Res. , vol.53 , pp. 609-622
    • Nagaoka, I.1    Yomogida, S.2    Tamura, H.3    Hirata, M.4
  • 26
    • 0036736465 scopus 로고    scopus 로고
    • Analysis of the cytotoxicity of synthetic antimicrobial peptides on mouse leucocytes: implications for systemic use
    • Pacor S., Giangaspero A., Bacac M., Sava G., and Tossi A. Analysis of the cytotoxicity of synthetic antimicrobial peptides on mouse leucocytes: implications for systemic use. J. Antimicrob. Chemother. 50 (2002) 339-348
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 339-348
    • Pacor, S.1    Giangaspero, A.2    Bacac, M.3    Sava, G.4    Tossi, A.5
  • 28
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II
    • Park C.B., Yi K.-S., Matsuzaki K., Kim M.S., and Kim S.C. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 8245-8250
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.-S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 29
    • 0037973366 scopus 로고    scopus 로고
    • A guide to selection and appropriate use of macrolides in skin infections
    • Parsad D., Pandhi R., and Dogra S. A guide to selection and appropriate use of macrolides in skin infections. Am. J.Clin. Dermatol. 4 (2003) 389-397
    • (2003) Am. J.Clin. Dermatol. , vol.4 , pp. 389-397
    • Parsad, D.1    Pandhi, R.2    Dogra, S.3
  • 30
    • 0024504201 scopus 로고
    • The dynamic properties of melittin in solution. Investigations by NMR and molecular dynamics
    • Pastore A., Harvey T.S., Dempsey C.E., and Campbell I.D. The dynamic properties of melittin in solution. Investigations by NMR and molecular dynamics. Eur. Biophys. J. 16 (1989) 363-367
    • (1989) Eur. Biophys. J. , vol.16 , pp. 363-367
    • Pastore, A.1    Harvey, T.S.2    Dempsey, C.E.3    Campbell, I.D.4
  • 31
    • 0042828863 scopus 로고    scopus 로고
    • PR-39, a porcine antimicrobial peptide, inhibits apoptosis: involvement of caspase-3
    • Ramanathan B., Wu H., Ross C.R., and Blecha F. PR-39, a porcine antimicrobial peptide, inhibits apoptosis: involvement of caspase-3. Dev. Comp. Immunol. 28 (2004) 163-169
    • (2004) Dev. Comp. Immunol. , vol.28 , pp. 163-169
    • Ramanathan, B.1    Wu, H.2    Ross, C.R.3    Blecha, F.4
  • 32
    • 0036785559 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses
    • Scott M.G., Davidson D.J., Gold M.R., Bowdish D., and Hancock R.E.W. The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. J. Immunol. 169 (2002) 3883-3891
    • (2002) J. Immunol. , vol.169 , pp. 3883-3891
    • Scott, M.G.1    Davidson, D.J.2    Gold, M.R.3    Bowdish, D.4    Hancock, R.E.W.5
  • 34
    • 0034650823 scopus 로고    scopus 로고
    • Cutting edge: cationic antimicrobial 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. Cutting edge: cationic antimicrobial peptides block the binding of lipopolysaccharide (LPS) to LPS binding protein. J. Immunol. 164 (2000) 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
  • 35
    • 0242637115 scopus 로고    scopus 로고
    • Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance
    • Shinnar A.E., Butler K.L., and Park H.J. Cathelicidin family of antimicrobial peptides: proteolytic processing and protease resistance. Bioorg. Chem. 31 (2003) 425-436
    • (2003) Bioorg. Chem. , vol.31 , pp. 425-436
    • Shinnar, A.E.1    Butler, K.L.2    Park, H.J.3
  • 37
    • 0034798343 scopus 로고    scopus 로고
    • Veterinary use and antibiotic resistance
    • Teuber M. Veterinary use and antibiotic resistance. Curr. Opin. Microbiol. 4 (2001) 493-499
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 493-499
    • Teuber, M.1
  • 38
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, alpha-helical antimicrobial peptides
    • Tossi A., Sandri L., and Giangaspero A. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55 (2000) 4-30
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 39
    • 11444259936 scopus 로고    scopus 로고
    • New consensus hydrophobicity scale extended to non-proteinogenic amino acids
    • Benedetti E., and Pedone C. (Eds), Edizioni Ziino, Napoli, Italy, Sorrento
    • Tossi A., Sandri L., and Giangaspero A. New consensus hydrophobicity scale extended to non-proteinogenic amino acids. In: Benedetti E., and Pedone C. (Eds). Proceedings of the 27th European Peptide Symposium (2002), Edizioni Ziino, Napoli, Italy, Sorrento
    • (2002) Proceedings of the 27th European Peptide Symposium
    • Tossi, A.1    Sandri, L.2    Giangaspero A3
  • 40
    • 0024300821 scopus 로고
    • Purification of a monocyte chemotactic factor secreted by nonhuman primate vascular cells in culture
    • Valente A.J., Graves D.T., Vialle-Valentin C.E., Delgado R., and Schwartz C.J. Purification of a monocyte chemotactic factor secreted by nonhuman primate vascular cells in culture. Biochemistry 27 (1988) 4162-4168
    • (1988) Biochemistry , vol.27 , pp. 4162-4168
    • Valente, A.J.1    Graves, D.T.2    Vialle-Valentin, C.E.3    Delgado, R.4    Schwartz, C.J.5
  • 44
    • 34347386061 scopus 로고    scopus 로고
    • Glycopeptide-resistant enterococci: deciphering virulence, resistance and epidemicity
    • Willems R.J., and Bonten M.J. Glycopeptide-resistant enterococci: deciphering virulence, resistance and epidemicity. Curr. Opin. Infect. Dis. 20 (2007) 384-390
    • (2007) Curr. Opin. Infect. Dis. , vol.20 , pp. 384-390
    • Willems, R.J.1    Bonten, M.J.2
  • 45
    • 33646367203 scopus 로고    scopus 로고
    • Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity
    • Xiao Y., Cai Y., Bommineni Y.R., Fernando S.C., Prakash O., Gilliland S.E., and Zhang G. Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity. J. Biol. Chem. 281 (2006) 2858-2867
    • (2006) J. Biol. Chem. , vol.281 , pp. 2858-2867
    • Xiao, Y.1    Cai, Y.2    Bommineni, Y.R.3    Fernando, S.C.4    Prakash, O.5    Gilliland, S.E.6    Zhang, G.7
  • 46
    • 33745266360 scopus 로고    scopus 로고
    • Structure-activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in chicken
    • Xiao Y., Dai H., Bommineni Y.R., Soulages J.L., Gong Y.-X., Prakash O., and Zhang G. Structure-activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in chicken. FEBS J. 273 (2006) 2581-2593
    • (2006) FEBS J. , vol.273 , pp. 2581-2593
    • Xiao, Y.1    Dai, H.2    Bommineni, Y.R.3    Soulages, J.L.4    Gong, Y.-X.5    Prakash, O.6    Zhang, G.7
  • 47
    • 67650361369 scopus 로고    scopus 로고
    • The central kink region of fowlicidin-2, an α-helical host defence peptide, is critically involved in bacterial killing and endotoxin neutralization
    • Xiao Y., Herrera A.I., Bommineni Y.R., Soulages J.L., Prakash O., and Zhang G. The central kink region of fowlicidin-2, an α-helical host defence peptide, is critically involved in bacterial killing and endotoxin neutralization. J. Innate Immun. (2008) 1-13
    • (2008) J. Innate Immun. , pp. 1-13
    • Xiao, Y.1    Herrera, A.I.2    Bommineni, Y.R.3    Soulages, J.L.4    Prakash, O.5    Zhang, G.6
  • 48
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • Yang D., Chen Q., Schmidt A.P., Anderson G.M., Wang J.M., Wooters J., Oppenheim J.J., and Chertov O. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 192 (2000) 1069-1074
    • (2000) J. Exp. Med. , vol.192 , pp. 1069-1074
    • Yang, D.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6    Oppenheim, J.J.7    Chertov, O.8
  • 49
    • 32344447342 scopus 로고    scopus 로고
    • Possible role of a PXXP central hinge in the antibacterial activity and membrane interaction of PMAP-23, a member of cathelicidin family
    • Yang S.-T., Jeon J.-H., Kim Y., Shin S.Y., Hahm K.-S., and Kim J.I. Possible role of a PXXP central hinge in the antibacterial activity and membrane interaction of PMAP-23, a member of cathelicidin family. Biochemistry 45 (2006) 1775-1784
    • (2006) Biochemistry , vol.45 , pp. 1775-1784
    • Yang, S.-T.1    Jeon, J.-H.2    Kim, Y.3    Shin, S.Y.4    Hahm, K.-S.5    Kim, J.I.6
  • 50
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 51
    • 27944443662 scopus 로고    scopus 로고
    • Tuning the biological properties of amphipathic alpha-helical antimicrobial peptides: rational use of minimal amino acid substitutions
    • Zelezetsky I., Pag U., Sahl H.-G., and Tossi A. Tuning the biological properties of amphipathic alpha-helical antimicrobial peptides: rational use of minimal amino acid substitutions. Peptides 26 (2005) 2368-2376
    • (2005) Peptides , vol.26 , pp. 2368-2376
    • Zelezetsky, I.1    Pag, U.2    Sahl, H.-G.3    Tossi, A.4
  • 52
    • 33748933561 scopus 로고    scopus 로고
    • Alpha-helical antimicrobial peptides-using a sequence template to guide structure-activity relationship studies
    • Zelezetsky I., and Tossi A. Alpha-helical antimicrobial peptides-using a sequence template to guide structure-activity relationship studies. Biochim. Biophys. Acta 1758 (2006) 1436-1449
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1436-1449
    • Zelezetsky, I.1    Tossi, A.2


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