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Volumn 8, Issue 4, 2013, Pages

Chicken Cathelicidins Display Antimicrobial Activity against Multiresistant Bacteria without Inducing Strong Resistance

Author keywords

[No Author keywords available]

Indexed keywords

CATHELICIDIN; CATHELICIDIN 1; CATHELICIDIN 2; CATHELICIDIN 3; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; CAP18 LIPOPOLYSACCHARIDE-BINDING PROTEIN;

EID: 84876446755     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0061964     Document Type: Article
Times cited : (38)

References (25)
  • 1
    • 79960959584 scopus 로고    scopus 로고
    • Multiresistant Gram-negative bacteria: The role of high-risk clones in the dissemination of antibiotic resistance
    • Woodford N, Turton JF, Livermore DM, (2011) Multiresistant Gram-negative bacteria: The role of high-risk clones in the dissemination of antibiotic resistance. FEMS Microbiol Rev 35: 736-755.
    • (2011) FEMS Microbiol Rev , vol.35 , pp. 736-755
    • Woodford, N.1    Turton, J.F.2    Livermore, D.M.3
  • 2
    • 84855484682 scopus 로고    scopus 로고
    • New insights into meticillin-resistant Staphylococcus aureus (MRSA) pathogenesis, treatment and resistance
    • Gould IM, David MZ, Esposito S, Garau J, Lina G, et al. (2012) New insights into meticillin-resistant Staphylococcus aureus (MRSA) pathogenesis, treatment and resistance. Int J of Antimicrob Agents 39: 96-104.
    • (2012) Int J of Antimicrob Agents , vol.39 , pp. 96-104
    • Gould, I.M.1    David, M.Z.2    Esposito, S.3    Garau, J.4    Lina, G.5
  • 3
    • 84864041446 scopus 로고    scopus 로고
    • Livestock-associated Staphylococcus aureus
    • Fluit AC, (2012) Livestock-associated Staphylococcus aureus. Clin Microbiol Infect 18: 735-744.
    • (2012) Clin Microbiol Infect , vol.18 , pp. 735-744
    • Fluit, A.C.1
  • 4
    • 0027216093 scopus 로고
    • Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine
    • Boman HG, Agerberth B, Boman A, (1993) Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect Immun 61: 2978-2984.
    • (1993) Infect Immun , vol.61 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 5
    • 0030032395 scopus 로고    scopus 로고
    • Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide
    • Shi J, Ross CR, Chengappa MM, Sylte MJ, McVey DS, et al. (1996) Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide. Antimicrob Agents Chem 40: 115-121.
    • (1996) Antimicrob Agents Chem , vol.40 , pp. 115-121
    • Shi, J.1    Ross, C.R.2    Chengappa, M.M.3    Sylte, M.J.4    McVey, D.S.5
  • 6
    • 42649142893 scopus 로고    scopus 로고
    • The role of the multifunctional peptide LL-37 in host defense
    • Kai-Larsen Y, Agerberth B, (2008) The role of the multifunctional peptide LL-37 in host defense. Front Biosci 13: 3760-3767.
    • (2008) Front Biosci , vol.13 , pp. 3760-3767
    • Kai-Larsen, Y.1    Agerberth, B.2
  • 7
    • 35448966956 scopus 로고    scopus 로고
    • Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway
    • Goitsuka R, Chen CL, Benyon L, Asano Y, Kitamura D, et al. (2007) Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway. Proc Natl Acad Sci USA 104: 15063-15068.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15063-15068
    • Goitsuka, R.1    Chen, C.L.2    Benyon, L.3    Asano, Y.4    Kitamura, D.5
  • 8
    • 33646367203 scopus 로고    scopus 로고
    • Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity
    • Xiao Y, Cai Y, Bommineni YR, Fernando SC, Prakash O, et al. (2006) Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity. J Biol Chem 281: 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
  • 10
    • 67650508049 scopus 로고    scopus 로고
    • Identification of chicken cathelicidin-2 core elements involved in antibacterial and immunomodulatory activities
    • van Dijk A, Molhoek EM, Veldhuizen EJA, Bokhoven JL, Wagendorp E, et al. (2009) Identification of chicken cathelicidin-2 core elements involved in antibacterial and immunomodulatory activities. Mol Immunol 46: 2465-2473.
    • (2009) Mol Immunol , vol.46 , pp. 2465-2473
    • van Dijk, A.1    Molhoek, E.M.2    Veldhuizen, E.J.A.3    Bokhoven, J.L.4    Wagendorp, E.5
  • 11
    • 33846006520 scopus 로고    scopus 로고
    • Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities
    • Bommineni YR, Dai H, Gong YX, Soulages JL, Fernando SC, et al. (2007) Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities. FEBS J 274: 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
  • 12
    • 77952546164 scopus 로고    scopus 로고
    • The central kink region of fowlicidin-2, an alpha-helical host defense peptide, is critically involved in bacterial killing and endotoxin neutralization
    • Xiao Y, Herrera AI, Bommineni YR, Soulages JL, Prakash O, et al. (2009) The central kink region of fowlicidin-2, an alpha-helical host defense peptide, is critically involved in bacterial killing and endotoxin neutralization. J Innate Immun 1: 268-280.
    • (2009) J Innate Immun , vol.1 , pp. 268-280
    • Xiao, Y.1    Herrera, A.I.2    Bommineni, Y.R.3    Soulages, J.L.4    Prakash, O.5
  • 14
    • 84876448817 scopus 로고    scopus 로고
    • Tissue expression and developmental regulation of chicken cathelicidin antimicrobial peptides
    • Achanta M, Sunkara LT, Dai G, Bommineni YR, Jiang W, et al. (2012) Tissue expression and developmental regulation of chicken cathelicidin antimicrobial peptides. J Anim Sci and Biotechnol 3: 15.
    • (2012) J Anim Sci and Biotechnol , vol.3 , pp. 15
    • Achanta, M.1    Sunkara, L.T.2    Dai, G.3    Bommineni, Y.R.4    Jiang, W.5
  • 17
    • 34548290744 scopus 로고    scopus 로고
    • Porcine beta-defensin 2 displays broad antimicrobial activity against pathogenic intestinal bacteria
    • Veldhuizen EJA, Rijnders M, Claassen EA, van Dijk A, Haagsman HP, (2008) Porcine beta-defensin 2 displays broad antimicrobial activity against pathogenic intestinal bacteria. Mol Immunol 45: 386-394.
    • (2008) Mol Immunol , vol.45 , pp. 386-394
    • Veldhuizen, E.J.A.1    Rijnders, M.2    Claassen, E.A.3    van Dijk, A.4    Haagsman, H.P.5
  • 19
    • 0036532403 scopus 로고    scopus 로고
    • How do bacteria resist human antimicrobial peptides?
    • Peschel A, (2002) How do bacteria resist human antimicrobial peptides? Trends Microbiol 10: 179-186.
    • (2002) Trends Microbiol , vol.10 , pp. 179-186
    • Peschel, A.1
  • 20
    • 79960938721 scopus 로고    scopus 로고
    • Bacterial resistance mechanisms against host defense peptides
    • Koprivnjak T, Peschel A, (2011) Bacterial resistance mechanisms against host defense peptides. Cell Mol Life Sci 68: 2243-2254.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 2243-2254
    • Koprivnjak, T.1    Peschel, A.2
  • 21
    • 0032538292 scopus 로고    scopus 로고
    • Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides
    • Guo L, Lim KB, Poduje CM, Daniel M, Gunn JS, et al. (1998) Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides. Cell 95: 189-198.
    • (1998) Cell , vol.95 , pp. 189-198
    • Guo, L.1    Lim, K.B.2    Poduje, C.M.3    Daniel, M.4    Gunn, J.S.5
  • 22
    • 0033919460 scopus 로고    scopus 로고
    • A PhoP-regulated outer membrane protease of Salmonella enterica serovar Typhimurium promotes resistance to alpha-helical antimicrobial peptides
    • Guina T, Yi EC, Wang H, Hackett M, Miller SI, (2000) A PhoP-regulated outer membrane protease of Salmonella enterica serovar Typhimurium promotes resistance to alpha-helical antimicrobial peptides. J Bacteriol 182: 4077-4086.
    • (2000) J Bacteriol , vol.182 , pp. 4077-4086
    • Guina, T.1    Yi, E.C.2    Wang, H.3    Hackett, M.4    Miller, S.I.5
  • 23
    • 0028148530 scopus 로고
    • Further characterization of the PhoP regulon: Identification of new PhoP-activated virulence loci
    • Belden WJ, Miller SI, (1994) Further characterization of the PhoP regulon: Identification of new PhoP-activated virulence loci. Infect Immun 62: 5095-5101.
    • (1994) Infect Immun , vol.62 , pp. 5095-5101
    • Belden, W.J.1    Miller, S.I.2
  • 24
    • 0032539553 scopus 로고    scopus 로고
    • Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family
    • Shafer WM, Qu X, Waring AJ, Lehrer RI, (1998) Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family. Proc Natl Acad Sci USA 95: 1829-1833.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.2    Waring, A.J.3    Lehrer, R.I.4
  • 25
    • 84857172277 scopus 로고    scopus 로고
    • OmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation of human LL-37
    • Thomassin JL, Brannon JR, Gibbs BF, Gruenheid S, Le Moual H, (2012) OmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation of human LL-37. Infect Immun 80: 483-492.
    • (2012) Infect Immun , vol.80 , pp. 483-492
    • Thomassin, J.L.1    Brannon, J.R.2    Gibbs, B.F.3    Gruenheid, S.4    Le Moual, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.