메뉴 건너뛰기




Volumn 15, Issue 2, 2009, Pages 87-95

Complement Activation Products C3a and C4a as Endogenous Antimicrobial Peptides

Author keywords

Anaphylatoxins; Antimicrobial peptides; Bactericidal activity; C3a; C4a; Complement; Host defense

Indexed keywords

COMPLEMENT COMPONENT C3A; COMPLEMENT COMPONENT C4A;

EID: 67349284794     PISSN: 15733149     EISSN: 15733904     Source Type: Journal    
DOI: 10.1007/s10989-009-9180-5     Document Type: Article
Times cited : (15)

References (59)
  • 1
    • 39149139017 scopus 로고    scopus 로고
    • The opportunistic human pathogenic fungus Aspergillus fumigatus evades the host complement system
    • J Behnsen A Hartmann 2008 The opportunistic human pathogenic fungus Aspergillus fumigatus evades the host complement system Infect Immun 76 2 820 827
    • (2008) Infect Immun , vol.76 , Issue.2 , pp. 820-827
    • Behnsen, J.1    Hartmann, A.2
  • 3
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • DOI 10.1038/nrmicro1098
    • KA Brogden 2005 Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3 3 238 250 (Pubitemid 40298223)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 4
    • 36248971186 scopus 로고    scopus 로고
    • The role of the complement anaphylatoxins in the recruitment of eosinophils
    • DOI 10.1016/j.intimp.2007.07.006, PII S1567576907002020
    • RG DiScipio IU Schraufstatter 2007 The role of the complement anaphylatoxins in the recruitment of eosinophils Int Immunopharmacol 7 14 1909 1923 (Pubitemid 350138516)
    • (2007) International Immunopharmacology , vol.7 , Issue.14 , pp. 1909-1923
    • DiScipio, R.G.1    Schraufstatter, I.U.2
  • 5
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.03.030, PII S000527360600126X
    • UH Durr US Sudheendra 2006 LL-37, the only human member of the cathelicidin family of antimicrobial peptides Biochim Biophys Acta 1758 9 1408 1425 (Pubitemid 44436081)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1408-1425
    • Durr, U.H.N.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 6
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • G Ehrenstein H Lecar 1977 Electrically gated ionic channels in lipid bilayers Q Rev Biophys 10 1 1 34 (Pubitemid 8065109)
    • (1977) Quarterly Reviews of Biophysics , vol.10 , Issue.1 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 7
    • 0035678319 scopus 로고    scopus 로고
    • Salmonella typhimurium outer membrane remodeling: Role in resistance to host innate immunity
    • DOI 10.1016/S1286-4579(01)01494-0
    • RK Ernst T Guina 2001 Salmonella typhimurium outer membrane remodeling: role in resistance to host innate immunity Microbes Infect 3 14-15 1327 1334 (Pubitemid 34033769)
    • (2001) Microbes and Infection , vol.3 , Issue.14-15 , pp. 1327-1334
    • Ernst, R.K.1    Guina, T.2    Miller, S.I.3
  • 8
    • 0024412074 scopus 로고
    • Streptococcal M protein: Molecular design and biological behavior
    • VA Fischetti 1989 Streptococcal M protein: molecular design and biological behavior Clin Microbiol Rev 2 3 285 314 (Pubitemid 19181596)
    • (1989) Clinical Microbiology Reviews , vol.2 , Issue.3 , pp. 285-314
    • Fischetti, V.A.1
  • 9
    • 0035069470 scopus 로고    scopus 로고
    • Antimicrobial proteins and peptides in host defense
    • T Ganz 2001 Antimicrobial proteins and peptides in host defense Semin Respir Infect 16 1 4 10 (Pubitemid 32275119)
    • (2001) Seminars in Respiratory Infections , vol.16 , Issue.1 , pp. 4-10
    • Ganz, T.1
  • 11
    • 34248228732 scopus 로고    scopus 로고
    • Interaction with C4b-binding protein contributes to nontypeable Haemophilus influenzae serum resistance
    • T Hallstrom H Jarva 2007 Interaction with C4b-binding protein contributes to nontypeable Haemophilus influenzae serum resistance J Immunol 178 10 6359 6366 (Pubitemid 46717420)
    • (2007) Journal of Immunology , vol.178 , Issue.10 , pp. 6359-6366
    • Hallstrom, T.1    Jarva, H.2    Riesbeck, K.3    Blom, A.M.4
  • 12
    • 47949122480 scopus 로고    scopus 로고
    • Haemophilus influenzae interacts with the human complement inhibitor factor H
    • T Hallstrom PF Zipfel 2008 Haemophilus influenzae interacts with the human complement inhibitor factor H J Immunol 181 1 537 545
    • (2008) J Immunol , vol.181 , Issue.1 , pp. 537-545
    • Hallstrom, T.1    Zipfel, P.F.2
  • 13
    • 58149237156 scopus 로고    scopus 로고
    • The Staphylococcus aureus protein Sbi acts as a complement inhibitor and forms a tripartite complex with host complement Factor H and C3b
    • K Haupt M Reuter 2008 The Staphylococcus aureus protein Sbi acts as a complement inhibitor and forms a tripartite complex with host complement Factor H and C3b PLoS Pathog 4 12 e1000250
    • (2008) PLoS Pathog , vol.4 , Issue.12 , pp. 1000250
    • Haupt, K.1    Reuter, M.2
  • 14
    • 34250356056 scopus 로고    scopus 로고
    • Molecular dynamics simulations of indolicidin association with model lipid bilayers
    • DOI 10.1529/biophysj.107.108050
    • JC Hsu CM Yip 2007 Molecular dynamics simulations of indolicidin association with model lipid bilayers Biophys J 92 12 L100 L102 (Pubitemid 46910525)
    • (2007) Biophysical Journal , vol.92 , Issue.12
    • Hsu, J.C.Y.1    Yip, C.M.2
  • 15
    • 0025104689 scopus 로고
    • Structure and function of C3a anaphylatoxin
    • TE Hugli 1990 Structure and function of C3a anaphylatoxin Curr Top Microbiol Immunol 153 181 208
    • (1990) Curr Top Microbiol Immunol , vol.153 , pp. 181-208
    • Hugli, T.E.1
  • 16
    • 0043066684 scopus 로고    scopus 로고
    • Complement resistance mechanisms of streptococci
    • DOI 10.1016/S0161-5890(03)00108-1
    • H Jarva TS Jokiranta 2003 Complement resistance mechanisms of streptococci Mol Immunol 40 2-4 95 107 (Pubitemid 36959820)
    • (2003) Molecular Immunology , vol.40 , Issue.2-4 , pp. 95-107
    • Jarva, H.1    Jokiranta, T.S.2    Wurzner, R.3    Meri, S.4
  • 17
    • 58749101895 scopus 로고    scopus 로고
    • Pore formation induced by an antimicrobial peptide: Electrostatic effects
    • F Jean-Francois J Elezgaray 2008 Pore formation induced by an antimicrobial peptide: electrostatic effects Biophys J 95 12 5748 5756
    • (2008) Biophys J , vol.95 , Issue.12 , pp. 5748-5756
    • Jean-Francois, F.1    Elezgaray, J.2
  • 18
    • 50849105103 scopus 로고    scopus 로고
    • Yersinia enterocolitica serum resistance proteins YadA and ail bind the complement regulator C4b-binding protein
    • V Kirjavainen H Jarva 2008 Yersinia enterocolitica serum resistance proteins YadA and ail bind the complement regulator C4b-binding protein PLoS Pathog 4 8 e1000140
    • (2008) PLoS Pathog , vol.4 , Issue.8 , pp. 1000140
    • Kirjavainen, V.1    Jarva, H.2
  • 19
    • 22644433305 scopus 로고    scopus 로고
    • Complement escape of human pathogenic bacteria by acquisition of complement regulators
    • DOI 10.1016/j.molimm.2005.06.016, PII S0161589005002014, 10th Meeting on Complement in Human Disease
    • P Kraiczy R Wurzner 2006 Complement escape of human pathogenic bacteria by acquisition of complement regulators Mol Immunol 43 1-2 31 44 (Pubitemid 41024919)
    • (2006) Molecular Immunology , vol.43 , Issue.1-2 , pp. 31-44
    • Kraiczy, P.1    Wurzner, R.2
  • 20
    • 37749038976 scopus 로고    scopus 로고
    • Immune evasion of the human pathogen Pseudomonas aeruginosa: Elongation factor Tuf is a factor H and plasminogen binding protein
    • A Kunert J Losse 2007 Immune evasion of the human pathogen Pseudomonas aeruginosa: elongation factor Tuf is a factor H and plasminogen binding protein J Immunol 179 5 2979 2988
    • (2007) J Immunol , vol.179 , Issue.5 , pp. 2979-2988
    • Kunert, A.1    Losse, J.2
  • 21
    • 38349048514 scopus 로고    scopus 로고
    • Complement evasion by human pathogens
    • JD Lambris D Ricklin 2008 Complement evasion by human pathogens Nat Rev Microbiol 6 2 132 142
    • (2008) Nat Rev Microbiol , vol.6 , Issue.2 , pp. 132-142
    • Lambris, J.D.1    Ricklin, D.2
  • 22
    • 62249106715 scopus 로고    scopus 로고
    • Characteristics of the main groups of human host-defensive peptides
    • K Lapis 2009 Characteristics of the main groups of human host-defensive peptides Orv Hetil 150 3 109 119
    • (2009) Orv Hetil , vol.150 , Issue.3 , pp. 109-119
    • Lapis, K.1
  • 23
    • 62449140880 scopus 로고    scopus 로고
    • Phosphoethanolamine substitution of lipid A and resistance of Neisseria gonorrhoeae to cationic antimicrobial peptides and complement-mediated killing by normal human serum
    • LA Lewis B Choudhury 2008 Phosphoethanolamine substitution of lipid A and resistance of Neisseria gonorrhoeae to cationic antimicrobial peptides and complement-mediated killing by normal human serum Infect Immun 77 1112 1120
    • (2008) Infect Immun , vol.77 , pp. 1112-1120
    • Lewis, L.A.1    Choudhury, B.2
  • 25
    • 0141484326 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa
    • DOI 10.1046/j.1365-2958.2003.03673.x
    • JB McPhee S Lewenza 2003 Cationic antimicrobial peptides activate a two-component regulatory system, PmrA-PmrB, that regulates resistance to polymyxin B and cationic antimicrobial peptides in Pseudomonas aeruginosa Mol Microbiol 50 1 205 217 (Pubitemid 37222798)
    • (2003) Molecular Microbiology , vol.50 , Issue.1 , pp. 205-217
    • McPhee, J.B.1    Lewenza, S.2    Hancock, R.E.W.3
  • 26
    • 34548039239 scopus 로고    scopus 로고
    • Defensins in the immunology of bacterial infections
    • DOI 10.1016/j.coi.2007.06.008, PII S0952791507001124
    • A Menendez B Brett Finlay 2007 Defensins in the immunology of bacterial infections Curr Opin Immunol 19 4 385 391 (Pubitemid 47284860)
    • (2007) Current Opinion in Immunology , vol.19 , Issue.4 , pp. 385-391
    • Menendez, A.1    Brett Finlay, B.2
  • 27
    • 0036716484 scopus 로고    scopus 로고
    • The yeast Candida albicans binds complement regulators factor H and FHL-1
    • T Meri A Hartmann 2002 The yeast Candida albicans binds complement regulators factor H and FHL-1 Infect Immun 70 9 5185 5192
    • (2002) Infect Immun , vol.70 , Issue.9 , pp. 5185-5192
    • Meri, T.1    Hartmann, A.2
  • 28
    • 7044262339 scopus 로고    scopus 로고
    • The hyphal and yeast forms of Candida albicans bind the complement regulator C4b-binding protein
    • DOI 10.1128/IAI.72.11.6633-6641.2004
    • T Meri AM Blom 2004 The hyphal and yeast forms of Candida albicans bind the complement regulator C4b-binding protein Infect Immun 72 11 6633 6641 (Pubitemid 39425446)
    • (2004) Infection and Immunity , vol.72 , Issue.11 , pp. 6633-6641
    • Meri, T.1    Blom, A.M.2    Hartmann, A.3    Lenk, D.4    Meri, S.5    Zipfel, P.F.6
  • 29
    • 0019841406 scopus 로고
    • Comparative study on biological activities of various anaphylatoxins (C4a, C3a, C5a). Investigations on their ability to induce platelet secretion
    • S Meuer TE Hugli 1981 Comparative study on biological activities of various anaphylatoxins (C4a, C3a, C5a). Investigations on their ability to induce platelet secretion Inflammation 5 4 263 273 (Pubitemid 12186480)
    • (1981) Inflammation , vol.5 , Issue.4 , pp. 263-273
    • Meuer, S.1    Hugli, T.E.2    Andreatta, R.H.3
  • 30
    • 34247117757 scopus 로고    scopus 로고
    • Cationic host defence peptides: Innate immune regulatory peptides as a novel approach for treating infections
    • DOI 10.1007/s00018-007-6475-6
    • N Mookherjee RE Hancock 2007 Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections Cell Mol Life Sci 64 7-8 922 933 (Pubitemid 46597762)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.7-8 , pp. 922-933
    • Mookherjee, N.1    Hancock, R.E.W.2
  • 31
    • 0023890664 scopus 로고
    • Molecular organization and function of the complement system
    • HJ Muller-Eberhard 1988 Molecular organization and function of the complement system Annu Rev Biochem 57 321 347 (Pubitemid 18171394)
    • (1988) Annual Review of Biochemistry , vol.57 , pp. 321-347
    • Muller-Eberhard, H.J.1
  • 33
    • 20544442905 scopus 로고    scopus 로고
    • Alarmins: Chemotactic activators of immune responses
    • DOI 10.1016/j.coi.2005.06.002, PII S0952791505000865
    • JJ Oppenheim D Yang 2005 Alarmins: chemotactic activators of immune responses Curr Opin Immunol 17 4 359 365 (Pubitemid 40848537)
    • (2005) Current Opinion in Immunology , vol.17 , Issue.SPEC. ISS. 4 , pp. 359-365
    • Oppenheim, J.J.1    Yang, D.2
  • 35
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic α-helical antimicrobial peptides
    • Z Oren Y Shai 1998 Mode of action of linear amphipathic alpha-helical antimicrobial peptides Biopolymers 47 6 451 463 (Pubitemid 128637353)
    • (1998) Biopolymers , vol.47 , Issue.6 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 36
    • 0345714694 scopus 로고    scopus 로고
    • Recruitment of Complement Factor H-Like Protein 1 Promotes Intracellular Invasion by Group A Streptococci
    • DOI 10.1128/IAI.71.12.7119-7128.2003
    • V Pandiripally L Wei 2003 Recruitment of complement factor H-like protein 1 promotes intracellular invasion by group A streptococci Infect Immun 71 12 7119 7128 (Pubitemid 37475344)
    • (2003) Infection and Immunity , vol.71 , Issue.12 , pp. 7119-7128
    • Pandiripally, V.1    Wei, L.2    Skerka, C.3    Zipfel, P.F.4    Cue, D.5
  • 38
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides
    • DOI 10.1074/jbc.274.13.8405
    • A Peschel M Otto 1999 Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides J Biol Chem 274 13 8405 8410 (Pubitemid 29164628)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kalbacher, H.4    Jung, G.5    Gotz, F.6
  • 40
    • 38049134765 scopus 로고    scopus 로고
    • Gpm1p is a factor H-, FHL-1-, and plasminogen-binding surface protein of Candida albicans
    • S Poltermann A Kunert 2007 Gpm1p is a factor H-, FHL-1-, and plasminogen-binding surface protein of Candida albicans J Biol Chem 282 52 37537 37544
    • (2007) J Biol Chem , vol.282 , Issue.52 , pp. 37537-37544
    • Poltermann, S.1    Kunert, A.2
  • 41
    • 1642422948 scopus 로고    scopus 로고
    • Efflux-mediated multiresistance in Gram-negative bacteria
    • DOI 10.1111/j.1469-0691.2004.00763.x
    • K Poole 2004 Efflux-mediated multiresistance in Gram-negative bacteria Clin Microbiol Infect 10 1 12 26 (Pubitemid 38128588)
    • (2004) Clinical Microbiology and Infection , vol.10 , Issue.1 , pp. 12-26
    • Poole, K.1
  • 42
    • 24044514016 scopus 로고    scopus 로고
    • Efflux-mediated antimicrobial resistance
    • DOI 10.1093/jac/dki171
    • K Poole 2005 Efflux-mediated antimicrobial resistance J Antimicrob Chemother 56 1 20 51 (Pubitemid 41418335)
    • (2005) Journal of Antimicrobial Chemotherapy , vol.56 , Issue.1 , pp. 20-51
    • Poole, K.1
  • 43
    • 0036030617 scopus 로고    scopus 로고
    • Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37
    • DOI 10.1046/j.1365-2958.2002.03146.x
    • A Schmidtchen IM Frick 2002 Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37 Mol Microbiol 46 1 157 168 (Pubitemid 35238020)
    • (2002) Molecular Microbiology , vol.46 , Issue.1 , pp. 157-168
    • Schmidtchen, A.1    Frick, I.-M.2    Andersson, E.3    Tapper, H.4    Bjorck, L.5
  • 45
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y Shai 1999 Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim Biophys Acta 1462 1-2 55 70
    • (1999) Biochim Biophys Acta , vol.1462 , Issue.12 , pp. 55-70
    • Shai, Y.1
  • 48
    • 18244379035 scopus 로고    scopus 로고
    • Identification of cptA, a PmrA-regulated locus required for phosphoethanolamine modification of the Salmonella enterica serovar typhimurium lipopolysaccharide core
    • DOI 10.1128/JB.187.10.3391-3399.2005
    • R Tamayo B Choudhury 2005 Identification of cptA, a PmrA-regulated locus required for phosphoethanolamine modification of the Salmonella enterica serovar typhimurium lipopolysaccharide core J Bacteriol 187 10 3391 3399 (Pubitemid 40628693)
    • (2005) Journal of Bacteriology , vol.187 , Issue.10 , pp. 3391-3399
    • Tamayo, R.1    Choudhury, B.2    Septer, A.3    Merighi, M.4    Carlson, R.5    Gunn, J.S.6
  • 50
    • 33845933103 scopus 로고    scopus 로고
    • Synergistic transmembrane alignment of the antimicrobial heterodimer PGLa/magainin
    • DOI 10.1074/jbc.M604759200
    • P Tremouilhac E Strandberg 2006 Synergistic transmembrane alignment of the antimicrobial heterodimer PGLa/magainin J Biol Chem 281 43 32089 32094 (Pubitemid 46036763)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.43 , pp. 32089-32094
    • Tremouilhac, P.1    Strandberg, E.2    Wadhwani, P.3    Ulrich, A.S.4
  • 54
    • 0035810399 scopus 로고    scopus 로고
    • Complement. First of two parts
    • MJ Walport 2001 Complement. First of two parts N Engl J Med 344 14 1058 1066
    • (2001) N Engl J Med , vol.344 , Issue.14 , pp. 1058-1066
    • Walport, M.J.1
  • 55
    • 0035849176 scopus 로고    scopus 로고
    • Complement. Second of two parts
    • MJ Walport 2001 Complement. Second of two parts N Engl J Med 344 15 1140 1144
    • (2001) N Engl J Med , vol.344 , Issue.15 , pp. 1140-1144
    • Walport, M.J.1
  • 57
    • 52349123671 scopus 로고    scopus 로고
    • Pore structure, thinning effect, and lateral diffusive dynamics of oriented lipid membranes interacting with antimicrobial peptide protegrin-1: 31P and 2H solid-state NMR study
    • S Wi C Kim 2008 Pore structure, thinning effect, and lateral diffusive dynamics of oriented lipid membranes interacting with antimicrobial peptide protegrin-1: 31P and 2H solid-state NMR study J Phys Chem B 112 36 11402 11414
    • (2008) J Phys Chem B , vol.112 , Issue.36 , pp. 11402-11414
    • Wi, S.1    Kim, C.2
  • 59
    • 34548259156 scopus 로고    scopus 로고
    • Complement evasion of pathogens: Common strategies are shared by diverse organisms
    • DOI 10.1016/j.molimm.2007.06.149, PII S0161589007002581, XIth European meeting on Complement in Human Disease
    • PF Zipfel R Wurzner 2007 Complement evasion of pathogens: common strategies are shared by diverse organisms Mol Immunol 44 16 3850 3857 (Pubitemid 47332624)
    • (2007) Molecular Immunology , vol.44 , Issue.16 , pp. 3850-3857
    • Zipfel, P.F.1    Wurzner, R.2    Skerka, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.