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Volumn 11, Issue 11, 2013, Pages 1215-1224

Host defense peptides: General overview and an update on their activity against Chlamydia spp.

Author keywords

antibiotic resistance; Chlamydia spp.; Chlamydia trachomatis; HDP; host defense peptides; therapy

Indexed keywords

ALPHA DEFENSIN; ANTIBIOTIC AGENT; BETA DEFENSIN; CATHELICIDIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CECROPIN; DEFENSIN; DOXYCYCLINE; HOST DEFENSE PEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEGRIN; TETRACYCLINE; TETRACYCLINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84888318699     PISSN: 14787210     EISSN: 17448336     Source Type: Journal    
DOI: 10.1586/14787210.2013.841450     Document Type: Review
Times cited : (11)

References (107)
  • 1
    • 0001580533 scopus 로고    scopus 로고
    • Resistance to tetracycline and sulphadiazine in swine C trachomatis isolates
    • March
    • Andersen AA, Rogers DG. Resistance to tetracycline and sulphadiazine in swine C trachomatis isolates. International Chlamydia Symposium. NE, USA, 313-316 March 1998
    • (1998) International Chlamydia Symposium. NE USA , pp. 313-316
    • Andersen, A.A.1    Rogers, D.G.2
  • 2
    • 4644334497 scopus 로고    scopus 로고
    • Tetracycline resistance in Chlamydia suis mediated by genomic islands inserted into the chlamydial inv-like gene
    • Dugan J, Rockey DD, Jones L, Andersen AA. Tetracycline resistance in Chlamydia suis mediated by genomic islands inserted into the chlamydial inv-like gene. Antimicrob. Agents Chemother. 48, 3989-3995 (2004
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 3989-3995
    • Dugan, J.1    Rockey, D.D.2    Jones, L.3    Andersen, A.A.4
  • 3
    • 77957555426 scopus 로고    scopus 로고
    • Antibiotic resistance in Chlamydiae
    • Sandoz KM, Rockey DD. Antibiotic resistance in Chlamydiae. Future Microbiol. 1427-1442 (2010
    • (2010) Future Microbiol , pp. 1427-1442
    • Sandoz, K.M.1    Rockey, D.D.2
  • 4
    • 51049098922 scopus 로고    scopus 로고
    • Tetracycline- resistant Chlamydia suis isolates in Italy
    • Di Francesco A, Donati M, Rossi M et al. Tetracycline- resistant Chlamydia suis isolates in Italy. Vet. Rec. 163(8), 251-252 (2008
    • (2008) Vet. Rec , vol.163 , Issue.8 , pp. 251-252
    • Di Francesco, A.1    Donati, M.2    Rossi, M.3
  • 5
    • 84857656671 scopus 로고    scopus 로고
    • Selection for tetracycline-resistant Chlamydia suis in treated pigs
    • Borel N, Regenscheit N, Di Francesco A et al. Selection for tetracycline-resistant Chlamydia suis in treated pigs. Vet. Microbiol. 156, 143-146 (2012
    • (2012) Vet. Microbiol , vol.156 , pp. 143-146
    • Borel, N.1    Regenscheit, N.2    Di Francesco, A.3
  • 6
    • 84872737900 scopus 로고    scopus 로고
    • Tetracycline-resistant Chlamydia suis in cases of reproductive failure on Belgian Cypriote and Israeli pig production farms
    • Schautteet K, De Clercq E, Miry C et al. Tetracycline-resistant Chlamydia suis in cases of reproductive failure on Belgian, Cypriote and Israeli pig production farms. J. Med. Microbiol. 62, 331-334 (2013
    • (2013) J. Med. Microbiol , vol.62 , pp. 331-334
    • Schautteet, K.1    De Clercq, E.2    Miry, C.3
  • 7
    • 0025202793 scopus 로고
    • Partial characterization of Chlamydia trachomatis isolates resistant to multiple antibiotics
    • Jones RB, Van der Pol B, Martin DH, Shepard MK. Partial characterization of Chlamydia trachomatis isolates resistant to multiple antibiotics. J. Infect. Dis. 162, 1309-1315 (1990
    • (1990) J. Infect. Dis , vol.162 , pp. 1309-1315
    • Jones, R.B.1    Van Der Pol, B.2    Martin, D.H.3    Shepard, M.K.4
  • 9
    • 0034105041 scopus 로고    scopus 로고
    • Multiple drug-resistant Chlamydia trachomatis associated with clinical treatment failure
    • Somani J, Bhullar VB, Workowski KA, Farshy CE, Black CM. Multiple drug-resistant Chlamydia trachomatis associated with clinical treatment failure. J. Infect. Dis. 181, 1421-1427 (2000
    • (2000) J. Infect. Dis , vol.181 , pp. 1421-1427
    • Somani, J.1    Bhullar, V.B.2    Workowski, K.A.3    Farshy, C.E.4    Black, C.M.5
  • 10
    • 14844320488 scopus 로고    scopus 로고
    • Evaluation of antimicrobial resistance and treatment failures for Chlamydia trachomatis: A meeting report
    • Wang SA, Papp JR, Stamm WE, Peeling RW, Martin DH, Holmes KK. Evaluation of antimicrobial resistance and treatment failures for Chlamydia trachomatis: A meeting report. J. Infect. Dis. 191(6), 917-923 (2005
    • (2005) J. Infect. Dis , vol.191 , Issue.6 , pp. 917-923
    • Wang, S.A.1    Papp, J.R.2    Stamm, W.E.3    Peeling, R.W.4    Martin, D.H.5    Holmes, K.K.6
  • 12
    • 34247117757 scopus 로고    scopus 로고
    • Cationic host defence peptides: Innate immune regulatory peptides as a novel approach for treating infections
    • Mookherjee N, Hancock RE. Cationic host defence peptides: Innate immune regulatory peptides as a novel approach for treating infections. Cell. Mol. Life Sci. 64(7-8), 922-933 (2007
    • (2007) Cell. Mol. Life Sci , vol.64 , Issue.7-8 , pp. 922-933
    • Mookherjee, N.1    Hancock, R.E.2
  • 13
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415(6870), 389-395 (2002
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 15
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55(1), 27-55 (2003
    • (2003) Pharmacol. Rev , vol.55 , Issue.1 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 17
    • 22944458199 scopus 로고    scopus 로고
    • The role of cathelicidins in the innate host defenses of mammals
    • Zanetti M. The role of cathelicidins in the innate host defenses of mammals. Curr. Issues Mol. Biol. 7(2), 179-196 (2005
    • (2005) Curr. Issues Mol. Biol , vol.7 , Issue.2 , pp. 179-196
    • Zanetti, M.1
  • 19
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock RE, Sahl HG. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24(12), 1551-1557 (2006
    • (2006) Nat. Biotechnol , vol.24 , Issue.12 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 20
    • 33745698864 scopus 로고    scopus 로고
    • Defensins in innate antiviral immunity
    • Klotman ME, Chang TL. Defensins in innate antiviral immunity. Nat. Rev. Immunol. 6(6), 447-456 (2006
    • (2006) Nat. Rev. Immunol , vol.6 , Issue.6 , pp. 447-456
    • Klotman, M.E.1    Chang, T.L.2
  • 21
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense
    • Lai Y, Gallo RL. AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 30(3), 131-141 (2009
    • (2009) Trends Immunol , vol.30 , Issue.3 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 22
    • 77649237880 scopus 로고    scopus 로고
    • Antimicrobial peptides: General overview and clinical implications in human health and diseases
    • Guaní-Guerra E, Santos-Mendoza T, Lugo-Reyes SO, Terán LM. Antimicrobial peptides: General overview and clinical implications in human health and diseases. Clin. Immunol. 135, 1-11 (2010
    • (2010) Clin. Immunol , vol.135 , pp. 1-11
    • Guaní-Guerra, E.1    Santos-Mendoza, T.2    Lugo-Reyes, S.O.3    Terán, L.M.4
  • 23
    • 78249233244 scopus 로고    scopus 로고
    • Antimicrobial peptides: The ancient arm of the human immune system
    • Wiesner J, Vilcinskas A. Antimicrobial peptides: The ancient arm of the human immune system. Virulence 1(5), 440-464 (2010
    • (2010) Virulence , vol.1 , Issue.5 , pp. 440-464
    • Wiesner, J.1    Vilcinskas, A.2
  • 24
    • 79251599753 scopus 로고    scopus 로고
    • Host defense peptides and their antimicrobial-immunomodulatory duality
    • Steinstraesser H, Kraneburg U, Jacobsen F, Al-Benna S. Host defense peptides and their antimicrobial-immunomodulatory duality. Immunobiology 216, 322-333 (2011
    • (2011) Immunobiology , vol.216 , pp. 322-333
    • Steinstraesser, H.1    Kraneburg, U.2    Jacobsen, F.3    Al-Benna, S.4
  • 25
    • 85028092735 scopus 로고    scopus 로고
    • Cathelicidins: Family of antimicrobial peptides: A review
    • Kósciuczuk EM, Lisowski P, Jarczak J et al. Cathelicidins: Family of antimicrobial peptides: A review. Mol. Bio. Rep. 39, 10957-10970 (2012
    • (2012) Mol. Bio. Rep , vol.39 , pp. 10957-10970
    • Kósciuczuk, E.M.1    Lisowski, P.2    Jarczak, J.3
  • 26
    • 83655193502 scopus 로고    scopus 로고
    • A-Defensins in human innate immunity
    • Lehrer RI, Lu W. a-Defensins in human innate immunity. Immunol. Rev. 245(1), 84-112 (2012
    • (2012) Immunol. Rev , vol.245 , Issue.1 , pp. 84-112
    • Lehrer, R.I.1    Lu, W.2
  • 27
    • 16844377323 scopus 로고    scopus 로고
    • Defensins and other antimicrobial peptides: A historical perspective and an update
    • Ganz T. Defensins and other antimicrobial peptides: A historical perspective and an update. Comb. Chem. High Throughput Screen. 8(3), 209-217 (2005
    • (2005) Comb. Chem. High Throughput Screen , vol.8 , Issue.3 , pp. 209-217
    • Ganz, T.1
  • 28
    • 0001216086 scopus 로고    scopus 로고
    • Epithelial antimicrobial peptides in host defense against infection
    • Bals R. Epithelial antimicrobial peptides in host defense against infection. Respir. Res. 1(3), 141-150 (2000
    • (2000) Respir. Res , vol.1 , Issue.3 , pp. 141-150
    • Bals, R.1
  • 29
    • 79960782055 scopus 로고    scopus 로고
    • Antibiotic activities of host defense peptides: More to it than lipid bilayer perturbation
    • Wilmes M, Cammue BP, Sahl HG, Thevissen K. Antibiotic activities of host defense peptides: More to it than lipid bilayer perturbation. Nat. Prod. Rep. 28(8), 1350-1358 (2011
    • (2011) Nat. Prod. Rep , vol.28 , Issue.8 , pp. 1350-1358
    • Wilmes, M.1    Cammue, B.P.2    Sahl, H.G.3    Thevissen, K.4
  • 31
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: From invertebrates to vertebrates
    • Bulet P, Stocklin R, Menin L. Anti-microbial peptides: From invertebrates to vertebrates. Immunol. Rev. 198, 169-184 (2004
    • (2004) Immunol. Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 32
    • 0031574103 scopus 로고    scopus 로고
    • The cathelicidin family of antimicrobial peptide precursors: A component of the oxygen-independent defense mechanisms of neutrophils
    • Zanetti M, Gennaro R, Romeo D. The cathelicidin family of antimicrobial peptide precursors: A component of the oxygen-independent defense mechanisms of neutrophils. Ann. N.Y. Acad. Sci. 832, 147-162 (1997
    • (1997) Ann. N.Y. Acad. Sci , vol.832 , pp. 147-162
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 33
    • 0022402545 scopus 로고
    • Defensins Natural peptide antibiotics of human neutrophils
    • Ganz T, Selsted ME, Szklarek D et al. Defensins. Natural peptide antibiotics of human neutrophils. J. Clin. Invest. 76(4), 1427-1435 (1985
    • (1985) J. Clin. Invest , vol.76 , Issue.4 , pp. 1427-1435
    • Ganz, T.1    Selsted, M.E.2    Szklarek, D.3
  • 34
    • 84864138907 scopus 로고    scopus 로고
    • Antimicrobial peptides: Clinical relevance and therapeutic implications
    • Pinheiro da Silva F, Machado MC. Antimicrobial peptides: Clinical relevance and therapeutic implications. Peptides 36, 308-314 (2012
    • (2012) Peptides , vol.36 , pp. 308-314
    • Pinheiro Da Silva, F.1    Machado, M.C.2
  • 35
    • 38749117873 scopus 로고    scopus 로고
    • Developmental switch of intestinal antimicrobial peptide expression
    • Ménard S, Förster V, Lotz M et al. Developmental switch of intestinal antimicrobial peptide expression. J. Exp. Med. 205(1), 183-193 (2008
    • (2008) J. Exp. Med , vol.205 , Issue.1 , pp. 183-193
    • Ménard, S.1    Förster, V.2    Lotz, M.3
  • 36
    • 0021142387 scopus 로고
    • Purification and antibacterial activity of antimicrobial peptides of rabbit granulocytes
    • Selsted ME, Szklarek D, Lehrer RI. Purification and antibacterial activity of antimicrobial peptides of rabbit granulocytes. Infect. Immun. 45(1), 150-154 (1984
    • (1984) Infect. Immun , vol.45 , Issue.1 , pp. 150-154
    • Selsted, M.E.1    Szklarek, D.2    Lehrer, R.I.3
  • 37
    • 0027472180 scopus 로고
    • The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics
    • Zanetti M, Del Sal G, Storici P, Schneider C, Romeo D. The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics. J. Biol. Chem. 268(1), 522-526 (1993
    • (1993) J. Biol. Chem , vol.268 , Issue.1 , pp. 522-526
    • Zanetti, M.1    Del Sal, G.2    Storici, P.3    Schneider, C.4    Romeo, D.5
  • 38
    • 4444246692 scopus 로고    scopus 로고
    • Primate defensins
    • Lehrer RI. Primate defensins. Nat. Rev. Microbiol. 2(9), 727-738 (2004
    • (2004) Nat. Rev. Microbiol , vol.2 , Issue.9 , pp. 727-738
    • Lehrer, R.I.1
  • 39
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins
    • Tang YQ, Yuan J, Osapay G et al. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science 286(5439), 498-502 (1999
    • (1999) Science , vol.286 , Issue.5439 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3
  • 40
    • 0031046654 scopus 로고    scopus 로고
    • Antimicrobial peptides of leukocytes
    • Ganz T, Lehrer RI. Antimicrobial peptides of leukocytes. Curr. Opin. Hematol. 4(1), 53-58 (1997
    • (1997) Curr. Opin. Hematol , vol.4 , Issue.1 , pp. 53-58
    • Ganz, T.1    Lehrer, R.I.2
  • 41
    • 0026457997 scopus 로고
    • Paneth cells of the human small intestine express an antimicrobial peptide gene
    • Jones DE, Bevins CL. Paneth cells of the human small intestine express an antimicrobial peptide gene. J. Biol. Chem. 267(32), 23216-23225 (1992
    • (1992) J. Biol. Chem , vol.267 , Issue.32 , pp. 23216-23225
    • Jones, D.E.1    Bevins, C.L.2
  • 42
    • 0031898688 scopus 로고    scopus 로고
    • Gene expression, immunolocalization, and secretion of human defensin-5 in human female reproductive tract
    • Quayle AJ, Porter EM, Nussbaum AA et al. Gene expression, immunolocalization, and secretion of human defensin-5 in human female reproductive tract. Am. J. Pathol. 152(5), 1247-1258 (1998
    • (1998) Am. J. Pathol , vol.152 , Issue.5 , pp. 1247-1258
    • Quayle, A.J.1    Porter, E.M.2    Nussbaum, A.A.3
  • 43
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz T. Defensins: Antimicrobial peptides of innate immunity. Nat. Rev. Immunol. 3(9), 710-720 (2003
    • (2003) Nat. Rev. Immunol , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 44
    • 0036040263 scopus 로고    scopus 로고
    • Expression of beta-defensin 1 and 2 mRNA by human monocytes, macrophages and dendritic cells
    • Duits LA, Ravensbergen B, Rademaker M, Hiemstra PS, Nibbering PH. Expression of beta-defensin 1 and 2 mRNA by human monocytes, macrophages and dendritic cells. Immunology 106(4), 517-525 (2002
    • (2002) Immunology , vol.106 , Issue.4 , pp. 517-525
    • Duits, L.A.1    Ravensbergen, B.2    Rademaker, M.3    Hiemstra, P.S.4    Nibbering, P.H.5
  • 45
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M, Gennaro R, Romeo D. Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett. 374, 1-5 (1995
    • (1995) FEBS Lett , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 46
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 75(1), 39-48 (2004
    • (2004) J. Leukoc. Biol , vol.75 , Issue.1 , pp. 39-48
    • Zanetti, M.1
  • 47
    • 33746087225 scopus 로고    scopus 로고
    • Control of the innate epithelial antimicrobial response is cell-type specific and dependent on relevant microenvironmental stimuli
    • Schauber J, Dorschner RA, Yamasaki K, Brouha B, Gallo RL. Control of the innate epithelial antimicrobial response is cell-type specific and dependent on relevant microenvironmental stimuli. Immunology 118(4), 509-519 (2006
    • (2006) Immunology , vol.118 , Issue.4 , pp. 509-519
    • Schauber, J.1    Dorschner, R.A.2    Yamasaki, K.3    Brouha, B.4    Gallo, R.L.5
  • 48
    • 29144521244 scopus 로고    scopus 로고
    • Human antimicrobial peptides: Defensins, cathelicidins and histatins
    • De Smet K, Contreras R. Human antimicrobial peptides: Defensins, cathelicidins and histatins. Biotechnol. Lett. 27, 1337-1347 (2005
    • (2005) Biotechnol. Lett , vol.27 , pp. 1337-1347
    • De Smet, K.1    Contreras, R.2
  • 49
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman HG. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13, 61-92 (1995
    • (1995) Annu. Rev. Immunol , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 50
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • Hancock RE, Lehrer R. Cationic peptides: A new source of antibiotics. Trends Biotechnol. 16(2), 82-88 (1998
    • (1998) Trends Biotechnol , vol.16 , Issue.2 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 51
    • 80053605687 scopus 로고    scopus 로고
    • Antimicrobial peptides important in innate immunity
    • Cederlund A, Gudmundsson GH, Agerberth B. Antimicrobial peptides important in innate immunity. FEBS J. 278, 3942-3951 (2011
    • (2011) FEBS J. , vol.278 , pp. 3942-3951
    • Cederlund, A.1    Gudmundsson, G.H.2    Agerberth, B.3
  • 52
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA. Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3(3), 238-250 (2005
    • (2005) Nat. Rev. Microbiol , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 53
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein G, Lecar H. Electrically gated ionic channels in lipid bilayers. Q. Rev. Biophys. 10(1), 1-34 (1977
    • (1977) Q. Rev. Biophys , vol.10 , Issue.1 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 54
    • 0026969265 scopus 로고
    • Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes
    • Pouny Y, Rapaport D, Mor A, Nicolas P, Shai Y. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 31(49), 12416-12423 (1992
    • (1992) Biochemistry , vol.31 , Issue.49 , pp. 12416-12423
    • Pouny, Y.1    Rapaport, D.2    Mor, A.3    Nicolas, P.4    Shai, Y.5
  • 55
    • 0029775069 scopus 로고    scopus 로고
    • An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation
    • Matsuzaki K, Murase O, Fujii N, Miyajima K. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35, 11361-11368 (1996
    • (1996) Biochemistry , vol.35 , pp. 11361-11368
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 56
    • 77950470139 scopus 로고    scopus 로고
    • Direct evidence from single-cell analysis that human {alpha}-defensins block adenovirus uncoating to neutralize infection
    • Nguyen EK, Nemerow GR, Smith JG. Direct evidence from single-cell analysis that human {alpha}-defensins block adenovirus uncoating to neutralize infection. J. Virol. 84(8), 4041-4049 (2010
    • (2010) J. Virol , vol.84 , Issue.8 , pp. 4041-4049
    • Nguyen, E.K.1    Nemerow, G.R.2    Smith, J.G.3
  • 57
    • 31944451136 scopus 로고    scopus 로고
    • Human alpha-defensins block papillomavirus infection
    • Buck CB, Day PM, Thompson CD et al. Human alpha-defensins block papillomavirus infection. Proc. Natl. Acad. Sci. U.S.A. 103(5), 1516-1521 (2006
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , Issue.5 , pp. 1516-1521
    • Buck, C.B.1    Day, P.M.2    Thompson, C.D.3
  • 58
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman HG. Antibacterial peptides: Basic facts and emerging concepts. J. Intern. Med. 254(3), 197-215 (2003
    • (2003) J. Intern. Med , vol.254 , Issue.3 , pp. 197-215
    • Boman, H.G.1
  • 59
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson J, Gudmundsson GH, Rottenberg ME, Berndt KD, Agerberth B. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. J. Biol. Chem. 273(6), 3718-3724 (1998
    • (1998) J. Biol. Chem , vol.273 , Issue.6 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 61
    • 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. Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect. Immun. 61(7), 2978-2984 (1993
    • (1993) Infect. Immun , vol.61 , Issue.7 , pp. 2978-2984
    • Boman, H.G.1    Agerberth, B.2    Boman, A.3
  • 62
    • 0035853022 scopus 로고    scopus 로고
    • The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding
    • Kragol G, Lovas S, Varadi G, Condie BA, Hoffmann R, Otvos L Jr The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding. Biochemistry 40(10), 3016-3026 (2001
    • (2001) Biochemistry , vol.40 , Issue.10 , pp. 3016-3026
    • Kragol, G.1    Lovas, S.2    Varadi, G.3    Condie, B.A.4    Hoffmann, R.5    Otvos Jr., L.6
  • 63
    • 84872856945 scopus 로고    scopus 로고
    • Peptide antimicrobials: Cell wall as a bacterial target
    • Yount NY, Yeaman MR. Peptide antimicrobials: Cell wall as a bacterial target. Ann. N.Y. Acad. Sci. 1277, 127-138 (2013
    • (2013) Ann. N.Y. Acad. Sci , vol.1277 , pp. 127-138
    • Yount, N.Y.1    Yeaman, M.R.2
  • 64
    • 77952976637 scopus 로고    scopus 로고
    • Plectasin, a fungal defensin, targets the bacterial cell wall precursor Lipid II
    • Schneider T, Kruse T, Wimmer R et al. Plectasin, a fungal defensin, targets the bacterial cell wall precursor Lipid II. Science 328(5982), 1168-1172 (2010
    • (2010) Science , vol.328 , Issue.5982 , pp. 1168-1172
    • Schneider, T.1    Kruse, T.2    Wimmer, R.3
  • 65
    • 77952693839 scopus 로고    scopus 로고
    • Human beta-defensin 3 inhibits cell wall biosynthesis in Staphylococci
    • Sass V, Schneider T, Wilmes M et al. Human beta-defensin 3 inhibits cell wall biosynthesis in Staphylococci. Infect. Immun. 78(6), 2793-2800 (2010
    • (2010) Infect. Immun , vol.78 , Issue.6 , pp. 2793-2800
    • Sass, V.1    Schneider, T.2    Wilmes, M.3
  • 66
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock RE. Peptide antibiotics. Lancet 349(9049), 418-422 (1997
    • (1997) Lancet , vol.349 , Issue.9049 , pp. 418-422
    • Hancock, R.E.1
  • 67
    • 10744229792 scopus 로고    scopus 로고
    • Defensins from insects and plants interact with fungal glucosylceramides
    • Thevissen K, Warnecke DC, François IE et al. Defensins from insects and plants interact with fungal glucosylceramides. J. Biol. Chem. 279(6), 3900-3905 (2004
    • (2004) J. Biol. Chem , vol.279 , Issue.6 , pp. 3900-3905
    • Thevissen, K.1    Warnecke, D.C.2    François, I.E.3
  • 68
  • 69
    • 9644299700 scopus 로고    scopus 로고
    • Antimicrobial activity of Bac7 fragments against drug-resistant clinical isolates
    • Benincasa M, Scocchi M, Podda E, Skerlavaj B, Dolzani L, Gennaro R. Antimicrobial activity of Bac7 fragments against drug-resistant clinical isolates. Peptides 25(12), 2055-2061 (2004
    • (2004) Peptides , vol.25 , Issue.12 , pp. 2055-2061
    • Benincasa, M.1    Scocchi, M.2    Podda, E.3    Skerlavaj, B.4    Dolzani, L.5    Gennaro, R.6
  • 70
    • 0024797674 scopus 로고
    • Monocyte-chemotactic activity of defensins from human neutrophils
    • Territo MC, Ganz T, Selsted ME, Lehrer R. Monocyte-chemotactic activity of defensins from human neutrophils. J. Clin. Invest. 84(6), 2017-2020 (1989
    • (1989) J. Clin. Invest , vol.84 , Issue.6 , pp. 2017-2020
    • Territo, M.C.1    Ganz, T.2    Selsted, M.E.3    Lehrer, R.4
  • 71
    • 18644363054 scopus 로고    scopus 로고
    • Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant
    • Kurosaka K, Chen Q, Yarovinsky F, Oppenheim JJ, Yang D. Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant. J. Immunol. 174(10), 6257-6265 (2005
    • (2005) J. Immunol , vol.174 , Issue.10 , pp. 6257-6265
    • Kurosaka, K.1    Chen, Q.2    Yarovinsky, F.3    Oppenheim, J.J.4    Yang, D.5
  • 72
    • 0036240209 scopus 로고    scopus 로고
    • A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis
    • Niyonsaba F, Iwabuchi K, Someya A et al. A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis. Immunology 106(1), 20-26 (2002
    • (2002) Immunology , vol.106 , Issue.1 , pp. 20-26
    • Niyonsaba, F.1    Iwabuchi, K.2    Someya, A.3
  • 73
    • 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, Wewers MD. A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release.J. Immunol. 172(8), 4987-4994 (2004
    • (2004) J. Immunol. , vol.172 , Issue.8 , pp. 4987-4994
    • Elssner, A.1    Duncan, M.2    Gavrilin, M.3    Wewers, M.D.4
  • 74
    • 0035058454 scopus 로고    scopus 로고
    • Evaluation of the effects of peptide antibiotics human bdefensins- 1/-2 and LL-37 on histamine release and prostaglandin D2 production from mast cells
    • Niyonsaba F, Someya A, Hirata M, Ogawa H, Nagaoka I. Evaluation of the effects of peptide antibiotics human bdefensins- 1/-2 and LL-37 on histamine release and prostaglandin D2 production from mast cells. Eur. J. Immunol. 31, 1066-1075 (2001
    • (2001) Eur. J. Immunol , vol.31 , pp. 1066-1075
    • Niyonsaba, F.1    Someya, A.2    Hirata, M.3    Ogawa, H.4    Nagaoka, I.5
  • 75
    • 1542564787 scopus 로고    scopus 로고
    • The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization
    • Davidson DJ, Currie AJ, Reid GS et al. The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization. J. Immunol. 172(2), 1146-1156 (2004
    • (2004) J. Immunol , vol.172 , Issue.2 , pp. 1146-1156
    • Davidson, D.J.1    Currie, A.J.2    Reid, G.S.3
  • 76
    • 80053165002 scopus 로고    scopus 로고
    • Cathelin-related antimicrobial peptide differentially regulates T- and B-cell function
    • Kin NW, Chen Y, Stefanov EK, Gallo RL, Kearney JF. Cathelin-related antimicrobial peptide differentially regulates T- and B-cell function. Eur. J. Immunol. 41(10), 3006-3016 (2011
    • (2011) Eur. J. Immunol , vol.41 , Issue.10 , pp. 3006-3016
    • Kin, N.W.1    Chen, Y.2    Stefanov, E.K.3    Gallo, R.L.4    Kearney, J.F.5
  • 77
    • 84873496907 scopus 로고    scopus 로고
    • Multiple immune-modulatory functions of cathelicidin host defense peptides
    • Choi K-Y, Mookherjee N. Multiple immune-modulatory functions of cathelicidin host defense peptides. Front. Immunol. 3(149), 1-4 (2012
    • (2012) Front. Immunol , vol.3 , Issue.149 , pp. 1-4
    • Choi, K.-Y.1    Mookherjee, N.2
  • 78
    • 33644978944 scopus 로고    scopus 로고
    • Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides Peptide properties and plausible modes of action
    • Rosenfeld Y, Papo N, Shai Y. Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action. J. Biol. Chem. 281(3), 1636-1643 (2006
    • (2006) J. Biol. Chem , vol.281 , Issue.3 , pp. 1636-1643
    • Rosenfeld, Y.1    Papo, N.2    Shai, Y.3
  • 79
    • 33847040438 scopus 로고    scopus 로고
    • Antimicrobial peptides human beta-defensins stimulate epidermal keratinocyte migration, proliferation and production of proinflammatory cytokines and chemokines
    • Niyonsaba F, Ushio H, Nakano N et al. Antimicrobial peptides human beta-defensins stimulate epidermal keratinocyte migration, proliferation and production of proinflammatory cytokines and chemokines. J. Invest. Dermatol. 127(3), 594-604 (2007
    • (2007) J. Invest. Dermatol , vol.127 , Issue.3 , pp. 594-604
    • Niyonsaba, F.1    Ushio, H.2    Nakano, N.3
  • 80
    • 0038142308 scopus 로고    scopus 로고
    • An angiogenic role for the human peptide antibiotic LL-37/hCAP-18
    • Koczulla R, Von Degenfeld G, Kupatt C et al. An angiogenic role for the human peptide antibiotic LL-37/hCAP-18. J. Clin. Invest. 111(11), 1665-1672 (2003
    • (2003) J. Clin. Invest , vol.111 , Issue.11 , pp. 1665-1672
    • Koczulla, R.1    Von Degenfeld, G.2    Kupatt, C.3
  • 81
    • 0034946907 scopus 로고    scopus 로고
    • Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus
    • Dorschner RA, Pestonjamasp VK, Tamakuwala S et al. Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus. J. Invest. Dermatol. 117(1), 91-97 (2001
    • (2001) J. Invest. Dermatol , vol.117 , Issue.1 , pp. 91-97
    • Dorschner, R.A.1    Pestonjamasp, V.K.2    Tamakuwala, S.3
  • 82
    • 0037335205 scopus 로고    scopus 로고
    • The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium
    • Heilborn JD, Nilsson MF, Kratz G et al. The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium. J. Invest. Dermatol. 120(3), 379-389 (2003
    • (2003) J. Invest. Dermatol , vol.120 , Issue.3 , pp. 379-389
    • Heilborn, J.D.1    Nilsson, M.F.2    Kratz, G.3
  • 83
    • 48149114517 scopus 로고    scopus 로고
    • Host defense peptides in wound healing
    • Steinstraesser L, Koehler T, Jacobsen F et al. Host defense peptides in wound healing. Mol. Med. 14(7-8), 528-537 (2008
    • (2008) Mol. Med , vol.14 , Issue.7-8 , pp. 528-537
    • Steinstraesser, L.1    Koehler, T.2    Jacobsen, F.3
  • 84
    • 38749148077 scopus 로고    scopus 로고
    • Ovarian cancers overexpress the antimicrobial protein hCAP-18 and its derivative LL-37 increases ovarian cancer cell proliferation and invasion
    • Coffelt SB, Waterman RS, Florez L et al. Ovarian cancers overexpress the antimicrobial protein hCAP-18 and its derivative LL-37 increases ovarian cancer cell proliferation and invasion. Int. J. Cancer 122(5), 1030-1039 (2008
    • (2008) Int. J. Cancer , vol.122 , Issue.5 , pp. 1030-1039
    • Coffelt, S.B.1    Waterman, R.S.2    Florez, L.3
  • 85
    • 34848838572 scopus 로고    scopus 로고
    • Functional analysis of the host defense peptide Human Beta Defensin-1: New insight into its potential role in cancer
    • Bullard RS, Gibson W, Bose SK et al. Functional analysis of the host defense peptide Human Beta Defensin-1: New insight into its potential role in cancer. Mol. Immunol. 45(3), 839-848 (2008
    • (2008) Mol. Immunol , vol.45 , Issue.3 , pp. 839-848
    • Bullard, R.S.1    Gibson, W.2    Bose, S.K.3
  • 86
    • 73949092172 scopus 로고    scopus 로고
    • The host defense peptide cathelicidin is required for NK cell-mediated suppression of tumor growth
    • Büchau AS, Morizane S, Trawbridge J et al. The host defense peptide cathelicidin is required for NK cell-mediated suppression of tumor growth. J. Immunol. 184(1), 369-378 (2010
    • (2010) J. Immunol , vol.184 , Issue.1 , pp. 369-378
    • Büchau, A.S.1    Morizane, S.2    Trawbridge, J.3
  • 87
    • 0035126317 scopus 로고    scopus 로고
    • Down regulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator
    • Islam D, Bandholtz L, Nilsson J et al. Down regulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator. Nat. Med. 7(2), 180-185 (2001
    • (2001) Nat. Med , vol.7 , Issue.2 , pp. 180-185
    • Islam, D.1    Bandholtz, L.2    Nilsson, J.3
  • 88
    • 0036796983 scopus 로고    scopus 로고
    • Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B
    • Ulvatne H, Haukland HH, Samuelsen Ø, Kramer M, Vorland LH. Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B. J. Antimicrob. Chemother. 50(4), 461-467 (2002
    • (2002) J. Antimicrob. Chemother , vol.50 , Issue.4 , pp. 461-467
    • Ulvatne, H.1    Haukland, H.H.2    Samuelsen, O.3    Kramer, M.4    Vorland, L.H.5
  • 89
    • 9644255763 scopus 로고    scopus 로고
    • Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureusderived proteinases
    • Sieprawska-Lupa M, Mydel P, Krawczyk K et al. Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureusderived proteinases. Antimicrob. Agents Chemother. 48(12), 4673-4679 (2004
    • (2004) Antimicrob. Agents Chemother , vol.48 , Issue.12 , pp. 4673-4679
    • Sieprawska-Lupa, M.1    Mydel, P.2    Krawczyk, K.3
  • 90
    • 33846079739 scopus 로고    scopus 로고
    • The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci
    • Lai Y, Villaruz AE, Li M, Cha DJ, Sturdevant DE, Otto M. The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci. Mol. Microbiol. 63(2), 497-506 (2007
    • (2007) Mol. Microbiol , vol.63 , Issue.2 , pp. 497-506
    • Lai, Y.1    Villaruz, A.E.2    Li, M.3    Cha, D.J.4    Sturdevant, D.E.5    Otto, M.6
  • 91
    • 0033794504 scopus 로고    scopus 로고
    • Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium
    • Gunn JS, Ryan SS, Van Velkinburgh JC, Ernst RK, Miller SI. Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium. Infect. Immun. 68(11), 6139-6146 (2000
    • (2000) Infect. Immun , vol.68 , Issue.11 , pp. 6139-6146
    • Gunn, J.S.1    Ryan, S.S.2    Van Velkinburgh, J.C.3    Ernst, R.K.4    Miller, S.I.5
  • 92
    • 0035821289 scopus 로고    scopus 로고
    • Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with l-lysine
    • Peschel A, Jack RW, Otto M et al. Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with l-lysine. J. Exp. Med. 193(9), 1067-1076 (2001
    • (2001) J. Exp. Med , vol.193 , Issue.9 , pp. 1067-1076
    • Peschel, A.1    Jack, R.W.2    Otto, M.3
  • 93
    • 20444406092 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with bacterial polysaccharides from lung pathogens
    • Herasimenka Y, Benincasa M, Mattiuzzo M, Cescutti P, Gennaro R, Rizzo R. Interaction of antimicrobial peptides with bacterial polysaccharides from lung pathogens. Peptides 26(7), 1127-1132 (2005
    • (2005) Peptides , vol.26 , Issue.7 , pp. 1127-1132
    • Herasimenka, Y.1    Benincasa, M.2    Mattiuzzo, M.3    Cescutti, P.4    Gennaro, R.5    Rizzo, R.6
  • 94
    • 70349650567 scopus 로고    scopus 로고
    • Activity of antimicrobial peptides in the presence of polysaccharides produced by pulmonary pathogens
    • Benincasa M, Mattiuzzo M, Herasimenka Y, Cescutti P, Rizzo R, Gennaro R. Activity of antimicrobial peptides in the presence of polysaccharides produced by pulmonary pathogens. J. Pept. Sci. 15(9), 595-600 (2009
    • (2009) J. Pept. Sci , vol.15 , Issue.9 , pp. 595-600
    • Benincasa, M.1    Mattiuzzo, M.2    Herasimenka, Y.3    Cescutti, P.4    Rizzo, R.5    Gennaro, R.6
  • 95
    • 0030047118 scopus 로고    scopus 로고
    • Susceptibility of Chlamydia trachomatis to protegrins and defensins
    • Yasin B, Harwig SSL, Lehrer RI, Wagar EA. Susceptibility of Chlamydia trachomatis to protegrins and defensins. Infect. Immun. 64 (3), 709-713 (1996
    • (1996) Infect. Immun , vol.64 , Issue.3 , pp. 709-713
    • Yasin, B.1    Harwig, S.S.L.2    Lehrer, R.I.3    Wagar, E.A.4
  • 96
    • 0027169823 scopus 로고
    • Protegrins: Leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins
    • Kokryakov VN, Harwig SS, Panyutich EA et al. Protegrins: Leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett. 327(2), 231-236 (1993
    • (1993) FEBS Lett , vol.327 , Issue.2 , pp. 231-236
    • Kokryakov, V.N.1    Harwig, S.S.2    Panyutich, E.A.3
  • 97
    • 0029958321 scopus 로고    scopus 로고
    • Protegrins: Structural requirements for inactivating elementary bodies of Chlamydia trachomatis
    • Yasin B, Lehrer RI, Harwig SSL, Wagar EA. Protegrins: Structural requirements for inactivating elementary bodies of Chlamydia trachomatis. Infect. Immun. 64(11), 4863-4866 (1996
    • (1996) Infect. Immun , vol.64 , Issue.11 , pp. 4863-4866
    • Yasin, B.1    Lehrer, R.I.2    Harwig, S.S.L.3    Wagar, E.A.4
  • 98
    • 0038702319 scopus 로고    scopus 로고
    • Susceptibility of human and murine Chlamydia trachomatis serovars to granulocyte- and epithelium derived antimicrobial peptides
    • Chong-Cerrillo C, Selsted ME, Peterson EM, de la Maza LM. Susceptibility of human and murine Chlamydia trachomatis serovars to granulocyte- and epithelium derived antimicrobial peptides. J. Peptide Res. 61, 237-242 (2003
    • (2003) J. Peptide Res , vol.61 , pp. 237-242
    • Chong-Cerrillo, C.1    Selsted, M.E.2    Peterson, E.M.3    De La Maza, L.M.4
  • 99
    • 0037389862 scopus 로고    scopus 로고
    • Activity of Novispirin G-10, a novel antimicrobial peptide against Chlamydia trachomatis and vaginosis-associated bacteria
    • Yasin B, Pang M, Lehrer RI, Wagar EA. Activity of Novispirin G-10, a novel antimicrobial peptide against Chlamydia trachomatis and vaginosis-associated bacteria. Exp. Mol. Pathol. 74(2), 190-195 (2003
    • (2003) Exp. Mol. Pathol , vol.74 , Issue.2 , pp. 190-195
    • Yasin, B.1    Pang, M.2    Lehrer, R.I.3    Wagar, E.A.4
  • 100
    • 3843140679 scopus 로고    scopus 로고
    • A cumulative experience examining the effect of natural and synthetic antimicrobial peptides vs
    • Yasin B, Pang M, Wagar EA. A cumulative experience examining the effect of natural and synthetic antimicrobial peptides vs. Chlamydia trachomatis. J. Pept. Res. 64(2), 65-71 (2004
    • (2004) Chlamydia trachomatis. J. Pept. Res , vol.64 , Issue.2 , pp. 65-71
    • Yasin, B.1    Pang, M.2    Wagar, E.A.3
  • 101
    • 77953583965 scopus 로고    scopus 로고
    • Increasing effect of high dose of PG-1 peptide on the infectivity of Chlamydophila abortus
    • Donati M, Di Francesco A, Gennaro R et al. Increasing effect of high dose of PG-1 peptide on the infectivity of Chlamydophila abortus. FEMS Immunol. Med.Microbiol. 59, 221-222 (2010
    • (2010) FEMS Immunol. Med.Microbiol , vol.59 , pp. 221-222
    • Donati, M.1    Di Francesco, A.2    Gennaro, R.3
  • 102
    • 34250202198 scopus 로고    scopus 로고
    • Sensitivity of Chlamydia suis to cathelicidin peptides
    • Donati M, Di Francesco A, Gennaro R et al. Sensitivity of Chlamydia suis to cathelicidin peptides. Vet. Microbiol. 123, 269-273 (2007
    • (2007) Vet. Microbiol , vol.123 , pp. 269-273
    • Donati, M.1    Di Francesco, A.2    Gennaro, R.3
  • 103
    • 57649207925 scopus 로고    scopus 로고
    • The cell-penetrating peptide, Pep-1, has activity against intracellular chlamydial growth but not extracellular forms of Chlamydia trachomatis
    • Park N, Yamanaka K, Tran D et al. The cell-penetrating peptide, Pep-1, has activity against intracellular chlamydial growth but not extracellular forms of Chlamydia trachomatis. J. Antimicrob. Chemother. 63(1), 115-123 (2009
    • (2009) J. Antimicrob. Chemother , vol.63 , Issue.1 , pp. 115-123
    • Park, N.1    Yamanaka, K.2    Tran, D.3
  • 104
    • 0036135329 scopus 로고    scopus 로고
    • In vitro microbicidal activities of cecropin peptides D2A21 and D4E1 and gel formulations containing 0.1 to 2% D2A21 against Chlamydia trachomatis
    • Ballweber LM, Jaynes JE, Stamm WE, Lampe MF. In vitro microbicidal activities of cecropin peptides D2A21 and D4E1 and gel formulations containing 0.1 to 2% D2A21 against Chlamydia trachomatis. Antimicrob. Agents Chemother. 46(1), 34-41 (2002
    • (2002) Antimicrob. Agents Chemother , vol.46 , Issue.1 , pp. 34-41
    • Ballweber, L.M.1    Jaynes, J.E.2    Stamm, W.E.3    Lampe, M.F.4
  • 105
    • 75749137270 scopus 로고    scopus 로고
    • Evaluation of WLBU2 peptide and 3-Ooctyl- sn-glycerol lipid as active ingredients for a topical microbicide formulation targeting Chlamydia trachomatis
    • Skinner MC, Kiselev AO, Isaacs CE, Mietzner TA, Montelaro RC, Lampe MF. Evaluation of WLBU2 peptide and 3-Ooctyl- sn-glycerol lipid as active ingredients for a topical microbicide formulation targeting Chlamydia trachomatis. Antimicrob. Agents Chemother. 54(2), 62-7236 (2010
    • (2010) Antimicrob. Agents Chemother , vol.54 , Issue.2 , pp. 62-7236
    • Skinner, M.C.1    Kiselev, A.O.2    Isaacs, C.E.3    Mietzner, T.A.4    Montelaro, R.C.5    Lampe, M.F.6
  • 106
    • 67349277796 scopus 로고    scopus 로고
    • Chlamydia trachomatis serovar distribution and other concurrent sexually transmitted infections in heterosexual men with urethritis in Italy
    • Donati M, Di Francesco A, D́Antuono A et al. Chlamydia trachomatis serovar distribution and other concurrent sexually transmitted infections in heterosexual men with urethritis in Italy. Eur. J. Clin. Microbiol. Infect. Dis. 28(5), 523-526 (2009
    • (2009) Eur. J. Clin. Microbiol. Infect. Dis , vol.28 , Issue.5 , pp. 523-526
    • Donati, M.1    Di Francesco, A.2    D́Antuono, A.3
  • 107
    • 33748413776 scopus 로고    scopus 로고
    • Antibacterial peptides for therapeutic use: Obstacles and realistic outlook
    • Marr AK, Gooderham WJ, Hancock RE. Antibacterial peptides for therapeutic use: Obstacles and realistic outlook. Curr. Opin. Pharmacol. 6(5), 468-472 (2006
    • (2006) Curr. Opin. Pharmacol , vol.6 , Issue.5 , pp. 468-472
    • Marr, A.K.1    Gooderham, W.J.2    Hancock, R.E.3


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