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Volumn 6, Issue 10, 2011, Pages

Antiviral activity and increased host defense against influenza infection elicited by the human cathelicidin LL-37

Author keywords

[No Author keywords available]

Indexed keywords

CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; ZANAMIVIR; ANTIMICROBIAL CATIONIC PEPTIDE; ANTIVIRUS AGENT; CAP18 LIPOPOLYSACCHARIDE BINDING PROTEIN; CAP18 LIPOPOLYSACCHARIDE-BINDING PROTEIN;

EID: 80054841451     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025333     Document Type: Article
Times cited : (292)

References (62)
  • 2
    • 34548480179 scopus 로고    scopus 로고
    • alpha -Defensin Inhibits Influenza Virus Replication by Cell-Mediated Mechanism(s)
    • Salvatore M, Garcia-Sastre A, Ruchala P, Lehrer RI, Chang T, et al. (2007) alpha-Defensin Inhibits Influenza Virus Replication by Cell-Mediated Mechanism(s). J Infect Dis 196: 835-843.
    • (2007) J Infect Dis , vol.196 , pp. 835-843
    • Salvatore, M.1    Garcia-Sastre, A.2    Ruchala, P.3    Lehrer, R.I.4    Chang, T.5
  • 3
    • 34250204072 scopus 로고    scopus 로고
    • Human neutrophil defensins increase neutrophil uptake of influenza A virus and bacteria and modify virus-induced respiratory burst responses
    • Tecle T, White MR, Gantz D, Crouch EC, Hartshorn KL, (2007) Human neutrophil defensins increase neutrophil uptake of influenza A virus and bacteria and modify virus-induced respiratory burst responses. J Immunol 178: 8046-8052.
    • (2007) J Immunol , vol.178 , pp. 8046-8052
    • Tecle, T.1    White, M.R.2    Gantz, D.3    Crouch, E.C.4    Hartshorn, K.L.5
  • 5
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense
    • Lai Y, Gallo RL, (2009) AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol 30: 131-141.
    • (2009) Trends Immunol , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 6
    • 21344435975 scopus 로고    scopus 로고
    • Human cathelicidin (LL-37), a multifunctional peptide, is expressed by ocular surface epithelia and has potent antibacterial and antiviral activity
    • Gordon YJ, Huang LC, Romanowski EG, Yates KA, Proske RJ, et al. (2005) Human cathelicidin (LL-37), a multifunctional peptide, is expressed by ocular surface epithelia and has potent antibacterial and antiviral activity. Curr Eye Res 30: 385-394.
    • (2005) Curr Eye Res , vol.30 , pp. 385-394
    • Gordon, Y.J.1    Huang, L.C.2    Romanowski, E.G.3    Yates, K.A.4    Proske, R.J.5
  • 7
    • 0034116709 scopus 로고    scopus 로고
    • Evaluation of the inactivation of infectious Herpes simplex virus by host-defense peptides
    • Yasin B, Pang M, Turner JS, Cho Y, Dinh NN, et al. (2000) Evaluation of the inactivation of infectious Herpes simplex virus by host-defense peptides. Eur J Clin Microbiol Infect Dis 19: 187-194.
    • (2000) Eur J Clin Microbiol Infect Dis , vol.19 , pp. 187-194
    • Yasin, B.1    Pang, M.2    Turner, J.S.3    Cho, Y.4    Dinh, N.N.5
  • 9
    • 18144386593 scopus 로고    scopus 로고
    • Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides
    • Steinstraesser L, Tippler B, Mertens J, Lamme E, Homann HH, et al. (2005) Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides. Retrovirology 2: 2.
    • (2005) Retrovirology , vol.2 , pp. 2
    • Steinstraesser, L.1    Tippler, B.2    Mertens, J.3    Lamme, E.4    Homann, H.H.5
  • 11
    • 0036259887 scopus 로고    scopus 로고
    • Characterization of the mouse Beta defensin 1, defb1, mutant mouse model
    • Morrison G, Kilanowski F, Davidson D, Dorin J, (2002) Characterization of the mouse Beta defensin 1, defb1, mutant mouse model. Infect Immun 70: 3053-3060.
    • (2002) Infect Immun , vol.70 , pp. 3053-3060
    • Morrison, G.1    Kilanowski, F.2    Davidson, D.3    Dorin, J.4
  • 12
    • 0036259798 scopus 로고    scopus 로고
    • beta-Defensin 1 Contributes to Pulmonary Innate Immunity in Mice
    • Moser C, Weiner DJ, Lysenko E, Bals R, Weiser JN, et al. (2002) beta-Defensin 1 Contributes to Pulmonary Innate Immunity in Mice. Infect Immun 70: 3068-3072.
    • (2002) Infect Immun , vol.70 , pp. 3068-3072
    • Moser, C.1    Weiner, D.J.2    Lysenko, E.3    Bals, R.4    Weiser, J.N.5
  • 13
    • 0037068959 scopus 로고    scopus 로고
    • Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study
    • Putsep K, Carlsson G, Boman HG, Andersson M, (2002) Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet 360: 1144-1149.
    • (2002) Lancet , vol.360 , pp. 1144-1149
    • Putsep, K.1    Carlsson, G.2    Boman, H.G.3    Andersson, M.4
  • 14
    • 35748985576 scopus 로고    scopus 로고
    • Cathelicidin-deficient (Cnlp -/-) mice show increased susceptibility to Pseudomonas aeruginosa keratitis
    • Huang LC, Reins RY, Gallo RL, McDermott AM, (2007) Cathelicidin-deficient (Cnlp-/-) mice show increased susceptibility to Pseudomonas aeruginosa keratitis. Invest Ophthalmol Vis Sci 48: 4498-4508.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 4498-4508
    • Huang, L.C.1    Reins, R.Y.2    Gallo, R.L.3    McDermott, A.M.4
  • 15
    • 17044404692 scopus 로고    scopus 로고
    • Cathelicidin Mediates Innate Intestinal Defense against Colonization with Epithelial Adherent Bacterial Pathogens
    • Iimura M, Gallo RL, Hase K, Miyamoto Y, Eckmann L, et al. (2005) Cathelicidin Mediates Innate Intestinal Defense against Colonization with Epithelial Adherent Bacterial Pathogens. J Immunol 174: 4901-4907.
    • (2005) J Immunol , vol.174 , pp. 4901-4907
    • Iimura, M.1    Gallo, R.L.2    Hase, K.3    Miyamoto, Y.4    Eckmann, L.5
  • 16
    • 0035936156 scopus 로고    scopus 로고
    • Innate antimicrobial peptide protects the skin from invasive bacterial infection
    • Nizet V, Ohtake T, Lauth X, Trowbridge J, Rudisill J, et al. (2001) Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature 414: 454-457.
    • (2001) Nature , vol.414 , pp. 454-457
    • Nizet, V.1    Ohtake, T.2    Lauth, X.3    Trowbridge, J.4    Rudisill, J.5
  • 17
    • 77955494032 scopus 로고    scopus 로고
    • Flagellin Stimulates Protective Lung Mucosal Immunity: Role of Cathelicidin-Related Antimicrobial Peptide
    • Yu FS, Cornicelli MD, Kovach MA, Newstead MW, Zeng X, et al. (2010) Flagellin Stimulates Protective Lung Mucosal Immunity: Role of Cathelicidin-Related Antimicrobial Peptide. J Immunol 185: 1142-1149.
    • (2010) J Immunol , vol.185 , pp. 1142-1149
    • Yu, F.S.1    Cornicelli, M.D.2    Kovach, M.A.3    Newstead, M.W.4    Zeng, X.5
  • 18
    • 33744986714 scopus 로고    scopus 로고
    • The antimicrobial peptide cathelicidin protects the urinary tract against invasive bacterial infection
    • Chromek M, Slamova Z, Bergman P, Kovacs L, Podracka L, et al. (2006) The antimicrobial peptide cathelicidin protects the urinary tract against invasive bacterial infection. Nat Med 12: 636-641.
    • (2006) Nat Med , vol.12 , pp. 636-641
    • Chromek, M.1    Slamova, Z.2    Bergman, P.3    Kovacs, L.4    Podracka, L.5
  • 19
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti M, (2004) Cathelicidins, multifunctional peptides of the innate immunity. J Leukoc Biol 75: 39-48.
    • (2004) J Leukoc Biol , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 20
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sorensen OE, Follin P, Johnsen AH, Calafat J, Tjabringa GS, et al. (2001) Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 97: 3951-3959.
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sorensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5
  • 21
    • 33645224419 scopus 로고    scopus 로고
    • Toll-like receptor triggering of a vitamin D-mediated human antimicrobial response
    • Liu PT, Stenger S, Li H, Wenzel L, Tan BH, et al. (2006) Toll-like receptor triggering of a vitamin D-mediated human antimicrobial response. Science 311: 1770-1773.
    • (2006) Science , vol.311 , pp. 1770-1773
    • Liu, P.T.1    Stenger, S.2    Li, H.3    Wenzel, L.4    Tan, B.H.5
  • 22
    • 58149189055 scopus 로고    scopus 로고
    • Respiratory epithelial cells convert inactive vitamin D to its active form: potential effects on host defense
    • Hansdottir S, Monick MM, Hinde SL, Lovan N, Look DC, et al. (2008) Respiratory epithelial cells convert inactive vitamin D to its active form: potential effects on host defense. J Immunol 181: 7090-7099.
    • (2008) J Immunol , vol.181 , pp. 7090-7099
    • Hansdottir, S.1    Monick, M.M.2    Hinde, S.L.3    Lovan, N.4    Look, D.C.5
  • 23
    • 4344665018 scopus 로고    scopus 로고
    • Cutting edge: 1,25-dihydroxyvitamin D3 is a direct inducer of antimicrobial peptide gene expression
    • Wang TT, Nestel FP, Bourdeau V, Nagai Y, Wang Q, et al. (2004) Cutting edge: 1,25-dihydroxyvitamin D3 is a direct inducer of antimicrobial peptide gene expression. J Immunol 173: 2909-2912.
    • (2004) J Immunol , vol.173 , pp. 2909-2912
    • Wang, T.T.1    Nestel, F.P.2    Bourdeau, V.3    Nagai, Y.4    Wang, Q.5
  • 24
    • 77956199887 scopus 로고    scopus 로고
    • Serum 25-hydroxyvitamin d and the incidence of acute viral respiratory tract infections in healthy adults
    • Sabetta JR, Depetrillo P, Cipriani RJ, Smardin J, Burns LA, et al. (2010) Serum 25-hydroxyvitamin d and the incidence of acute viral respiratory tract infections in healthy adults. PLoS One 5: e11088.
    • (2010) PLoS One , vol.5
    • Sabetta, J.R.1    Depetrillo, P.2    Cipriani, R.J.3    Smardin, J.4    Burns, L.A.5
  • 25
    • 77951961788 scopus 로고    scopus 로고
    • Randomized trial of vitamin D supplementation to prevent seasonal influenza A in schoolchildren
    • Urashima M, Segawa T, Okazaki M, Kurihara M, Wada Y, et al. (2010) Randomized trial of vitamin D supplementation to prevent seasonal influenza A in schoolchildren. Am J Clin Nutr.
    • (2010) Am J Clin Nutr
    • Urashima, M.1    Segawa, T.2    Okazaki, M.3    Kurihara, M.4    Wada, Y.5
  • 26
    • 1642484970 scopus 로고    scopus 로고
    • Selective killing of vaccinia virus by LL-37: implications for eczema vaccinatum
    • Howell MD, Jones JF, Kisich KO, Streib JE, Gallo RL, et al. (2004) Selective killing of vaccinia virus by LL-37: implications for eczema vaccinatum. J Immunol 172: 1763-1767.
    • (2004) J Immunol , vol.172 , pp. 1763-1767
    • Howell, M.D.1    Jones, J.F.2    Kisich, K.O.3    Streib, J.E.4    Gallo, R.L.5
  • 27
    • 0032708355 scopus 로고    scopus 로고
    • Augmentation of innate host defense by expression of a cathelicidin antimicrobial peptide
    • Bals R, Weiner DJ, Moscioni AD, Meegalla RL, Wilson JM, (1999) Augmentation of innate host defense by expression of a cathelicidin antimicrobial peptide. Infect Immun 67: 6084-6089.
    • (1999) Infect Immun , vol.67 , pp. 6084-6089
    • Bals, R.1    Weiner, D.J.2    Moscioni, A.D.3    Meegalla, R.L.4    Wilson, J.M.5
  • 28
    • 1042278913 scopus 로고    scopus 로고
    • In vitro and in vivo antimicrobial activity of two alpha-helical cathelicidin peptides and of their synthetic analogs
    • Benincasa M, Skerlavaj B, Gennaro R, Pellegrini A, Zanetti M, (2003) In vitro and in vivo antimicrobial activity of two alpha-helical cathelicidin peptides and of their synthetic analogs. Peptides 24: 1723-1731.
    • (2003) Peptides , vol.24 , pp. 1723-1731
    • Benincasa, M.1    Skerlavaj, B.2    Gennaro, R.3    Pellegrini, A.4    Zanetti, M.5
  • 29
    • 79961064178 scopus 로고    scopus 로고
    • Modulation of human {beta}-defensin-1 (hBD-1) in plasmacytoid dendritic cells (PDC), monocytes, and epithelial cells by influenza virus, Herpes simplex virus, and Sendai virus and its possible role in innate immunity
    • Ryan LK, Dai J, Yin Z, Megjugorac N, Uhlhorn V, et al. (2011) Modulation of human {beta}-defensin-1 (hBD-1) in plasmacytoid dendritic cells (PDC), monocytes, and epithelial cells by influenza virus, Herpes simplex virus, and Sendai virus and its possible role in innate immunity. J Leukoc Biol 90: 343-356.
    • (2011) J Leukoc Biol , vol.90 , pp. 343-356
    • Ryan, L.K.1    Dai, J.2    Yin, Z.3    Megjugorac, N.4    Uhlhorn, V.5
  • 31
    • 0030047118 scopus 로고    scopus 로고
    • Susceptibility of Chlamydia trachomatis to protegrins and defensins
    • Yasin B, Harwig SS, Lehrer RI, Wagar EA, (1996) Susceptibility of Chlamydia trachomatis to protegrins and defensins. Infect Immun 64: 709-713.
    • (1996) Infect Immun , vol.64 , pp. 709-713
    • Yasin, B.1    Harwig, S.S.2    Lehrer, R.I.3    Wagar, E.A.4
  • 32
    • 42949110073 scopus 로고    scopus 로고
    • Enhanced resistance to bacterial infection in protegrin-1 transgenic mice
    • Cheung QC, Turner PV, Song C, Wu D, Cai HY, et al. (2008) Enhanced resistance to bacterial infection in protegrin-1 transgenic mice. Antimicrob Agents Chemother 52: 1812-1819.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 1812-1819
    • Cheung, Q.C.1    Turner, P.V.2    Song, C.3    Wu, D.4    Cai, H.Y.5
  • 33
    • 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 AP, Anderson GM, Wang JM, et al. (2000) 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: 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
  • 34
    • 51649104412 scopus 로고    scopus 로고
    • Neutrophil secretion products pave the way for inflammatory monocytes
    • Soehnlein O, Zernecke A, Eriksson EE, Rothfuchs AG, Pham CT, et al. (2008) Neutrophil secretion products pave the way for inflammatory monocytes. Blood 112: 1461-1471.
    • (2008) Blood , vol.112 , pp. 1461-1471
    • Soehnlein, O.1    Zernecke, A.2    Eriksson, E.E.3    Rothfuchs, A.G.4    Pham, C.T.5
  • 35
    • 70449363613 scopus 로고    scopus 로고
    • Evidence that cathelicidin peptide LL-37 may act as a functional ligand for CXCR2 on human neutrophils
    • Zhang Z, Cherryholmes G, Chang F, Rose DM, Schraufstatter I, et al. (2009) Evidence that cathelicidin peptide LL-37 may act as a functional ligand for CXCR2 on human neutrophils. Eur J Immunol 39: 3181-3194.
    • (2009) Eur J Immunol , vol.39 , pp. 3181-3194
    • Zhang, Z.1    Cherryholmes, G.2    Chang, F.3    Rose, D.M.4    Schraufstatter, I.5
  • 36
    • 0036785559 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses
    • Scott MG, Davidson DJ, Gold MR, Bowdish D, Hancock RE, (2002) The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. J Immunol 169: 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.5
  • 37
    • 0346996865 scopus 로고    scopus 로고
    • The Antimicrobial Peptide LL-37 Activates Innate Immunity at the Airway Epithelial Surface by Transactivation of the Epidermal Growth Factor Receptor
    • Tjabringa GS, Aarbiou J, Ninaber DK, Drijfhout JW, Sorensen OE, et al. (2003) The Antimicrobial Peptide LL-37 Activates Innate Immunity at the Airway Epithelial Surface by Transactivation of the Epidermal Growth Factor Receptor. J Immunol 171: 6690-6696.
    • (2003) J Immunol , vol.171 , pp. 6690-6696
    • Tjabringa, G.S.1    Aarbiou, J.2    Ninaber, D.K.3    Drijfhout, J.W.4    Sorensen, O.E.5
  • 38
    • 77951044334 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 modulates the inflammatory and host defense response of human neutrophils
    • Alalwani MS, Sierigk J, Herr C, Pinkenburg O, Gallo R, et al. (2010) The antimicrobial peptide LL-37 modulates the inflammatory and host defense response of human neutrophils. Eur J Immunol 40: 1118-1126.
    • (2010) Eur J Immunol , vol.40 , pp. 1118-1126
    • Alalwani, M.S.1    Sierigk, J.2    Herr, C.3    Pinkenburg, O.4    Gallo, R.5
  • 39
    • 70349635632 scopus 로고    scopus 로고
    • Secondary necrosis of apoptotic neutrophils induced by the human cathelicidin LL-37 is not proinflammatory to phagocytosing macrophages
    • Li HN, Barlow PG, Bylund J, Mackellar A, Bjorstad A, et al. (2009) Secondary necrosis of apoptotic neutrophils induced by the human cathelicidin LL-37 is not proinflammatory to phagocytosing macrophages. J Leukoc Biol 86: 891-902.
    • (2009) J Leukoc Biol , vol.86 , pp. 891-902
    • Li, H.N.1    Barlow, P.G.2    Bylund, J.3    Mackellar, A.4    Bjorstad, A.5
  • 40
    • 50849112078 scopus 로고    scopus 로고
    • Neutrophil secondary necrosis is induced by LL-37 derived from cathelicidin
    • Zhang Z, Cherryholmes G, Shively JE, (2008) Neutrophil secondary necrosis is induced by LL-37 derived from cathelicidin. J Leukoc Biol 84: 780-788.
    • (2008) J Leukoc Biol , vol.84 , pp. 780-788
    • Zhang, Z.1    Cherryholmes, G.2    Shively, J.E.3
  • 43
    • 69949184887 scopus 로고    scopus 로고
    • Vitamin D3 induces autophagy in human monocytes/macrophages via cathelicidin
    • Yuk JM, Shin DM, Lee HM, Yang CS, Jin HS, et al. (2009) Vitamin D3 induces autophagy in human monocytes/macrophages via cathelicidin. Cell Host Microbe 6: 231-243.
    • (2009) Cell Host Microbe , vol.6 , pp. 231-243
    • Yuk, J.M.1    Shin, D.M.2    Lee, H.M.3    Yang, C.S.4    Jin, H.S.5
  • 44
    • 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, Bowdish DM, MacDonald KL, et al. (2004) The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization. J Immunol 172: 1146-1156.
    • (2004) J Immunol , vol.172 , pp. 1146-1156
    • Davidson, D.J.1    Currie, A.J.2    Reid, G.S.3    Bowdish, D.M.4    MacDonald, K.L.5
  • 45
    • 34948862264 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide
    • Lande R, Gregorio J, Facchinetti V, Chatterjee B, Wang YH, et al. (2007) Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide. Nature 449: 564-569.
    • (2007) Nature , vol.449 , pp. 564-569
    • Lande, R.1    Gregorio, J.2    Facchinetti, V.3    Chatterjee, B.4    Wang, Y.H.5
  • 46
    • 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, (2004) A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release. J Immunol 172: 4987-4994.
    • (2004) J Immunol , vol.172 , pp. 4987-4994
    • Elssner, A.1    Duncan, M.2    Gavrilin, M.3    Wewers, M.D.4
  • 47
    • 30044433704 scopus 로고    scopus 로고
    • Modulation of the TLR-Mediated Inflammatory Response by the Endogenous Human Host Defense Peptide LL-37
    • Mookherjee N, Brown KL, Bowdish DM, Doria S, Falsafi R, et al. (2006) Modulation of the TLR-Mediated Inflammatory Response by the Endogenous Human Host Defense Peptide LL-37. J Immunol 176: 2455-2464.
    • (2006) J Immunol , vol.176 , pp. 2455-2464
    • Mookherjee, N.1    Brown, K.L.2    Bowdish, D.M.3    Doria, S.4    Falsafi, R.5
  • 48
    • 0035884820 scopus 로고    scopus 로고
    • Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells
    • Nagaoka I, Hirota S, Niyonsaba F, Hirata M, Adachi Y, et al. (2001) Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells. J Immunol 167: 3329-3338.
    • (2001) J Immunol , vol.167 , pp. 3329-3338
    • Nagaoka, I.1    Hirota, S.2    Niyonsaba, F.3    Hirata, M.4    Adachi, Y.5
  • 49
    • 38849088077 scopus 로고    scopus 로고
    • Host Defense Peptide LL-37, in Synergy with Inflammatory Mediator IL-1beta, Augments Immune Responses by Multiple Pathways
    • Yu J, Mookherjee N, Wee K, Bowdish DM, Pistolic J, et al. (2007) Host Defense Peptide LL-37, in Synergy with Inflammatory Mediator IL-1beta, Augments Immune Responses by Multiple Pathways. J Immunol 179: 7684-7691.
    • (2007) J Immunol , vol.179 , pp. 7684-7691
    • Yu, J.1    Mookherjee, N.2    Wee, K.3    Bowdish, D.M.4    Pistolic, J.5
  • 50
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza a virus through recognition of viral RNA
    • Allen IC, Scull MA, Moore CB, Holl EK, McElvania-TeKippe E, et al. (2009) The NLRP3 inflammasome mediates in vivo innate immunity to influenza a virus through recognition of viral RNA. Immunity 30: 556-565.
    • (2009) Immunity , vol.30 , pp. 556-565
    • Allen, I.C.1    Scull, M.A.2    Moore, C.B.3    Holl, E.K.4    McElvania-TeKippe, E.5
  • 51
    • 64049096334 scopus 로고    scopus 로고
    • The intracellular sensor NLRP3 mediates key innate and healing responses to influenza A virus via the regulation of caspase-1
    • Thomas PG, Dash P, Aldridge JR Jr, Ellebedy AH, Reynolds C, et al. (2009) The intracellular sensor NLRP3 mediates key innate and healing responses to influenza A virus via the regulation of caspase-1. Immunity 30: 566-575.
    • (2009) Immunity , vol.30 , pp. 566-575
    • Thomas, P.G.1    Dash, P.2    Aldridge Jr., J.R.3    Ellebedy, A.H.4    Reynolds, C.5
  • 52
    • 60549112774 scopus 로고    scopus 로고
    • Inflammasome recognition of influenza virus is essential for adaptive immune responses
    • Ichinohe T, Lee HK, Ogura Y, Flavell R, Iwasaki A, (2009) Inflammasome recognition of influenza virus is essential for adaptive immune responses. J Exp Med 206: 79-87.
    • (2009) J Exp Med , vol.206 , pp. 79-87
    • Ichinohe, T.1    Lee, H.K.2    Ogura, Y.3    Flavell, R.4    Iwasaki, A.5
  • 53
    • 0033564334 scopus 로고    scopus 로고
    • Virus infection activates IL-1 beta and IL-18 production in human macrophages by a caspase-1-dependent pathway
    • Pirhonen J, Sareneva T, Kurimoto M, Julkunen I, Matikainen S, (1999) Virus infection activates IL-1 beta and IL-18 production in human macrophages by a caspase-1-dependent pathway. J Immunol 162: 7322-7329.
    • (1999) J Immunol , vol.162 , pp. 7322-7329
    • Pirhonen, J.1    Sareneva, T.2    Kurimoto, M.3    Julkunen, I.4    Matikainen, S.5
  • 54
    • 54449099369 scopus 로고    scopus 로고
    • The multifunctional NS1 protein of influenza A viruses
    • Hale BG, Randall RE, Ortin J, Jackson D, (2008) The multifunctional NS1 protein of influenza A viruses. J Gen Virol 89: 2359-2376.
    • (2008) J Gen Virol , vol.89 , pp. 2359-2376
    • Hale, B.G.1    Randall, R.E.2    Ortin, J.3    Jackson, D.4
  • 55
    • 11444262203 scopus 로고    scopus 로고
    • Influenza A mutant viruses with altered NS1 protein function provoke caspase-1 activation in primary human macrophages, resulting in fast apoptosis and release of high levels of interleukins 1beta and 18
    • Stasakova J, Ferko B, Kittel C, Sereinig S, Romanova J, et al. (2005) Influenza A mutant viruses with altered NS1 protein function provoke caspase-1 activation in primary human macrophages, resulting in fast apoptosis and release of high levels of interleukins 1beta and 18. J Gen Virol 86: 185-195.
    • (2005) J Gen Virol , vol.86 , pp. 185-195
    • Stasakova, J.1    Ferko, B.2    Kittel, C.3    Sereinig, S.4    Romanova, J.5
  • 56
    • 33749514992 scopus 로고    scopus 로고
    • Genomic analysis of increased host immune and cell death responses induced by 1918 influenza virus
    • Kash JC, Tumpey TM, Proll SC, Carter V, Perwitasari O, et al. (2006) Genomic analysis of increased host immune and cell death responses induced by 1918 influenza virus. Nature 443: 578-581.
    • (2006) Nature , vol.443 , pp. 578-581
    • Kash, J.C.1    Tumpey, T.M.2    Proll, S.C.3    Carter, V.4    Perwitasari, O.5
  • 57
    • 33749511112 scopus 로고    scopus 로고
    • Fatal outcome of human influenza A (H5N1) is associated with high viral load and hypercytokinemia
    • de Jong MD, Simmons CP, Thanh TT, Hien VM, Smith GJ, et al. (2006) Fatal outcome of human influenza A (H5N1) is associated with high viral load and hypercytokinemia. Nat Med 12: 1203-1207.
    • (2006) Nat Med , vol.12 , pp. 1203-1207
    • de Jong, M.D.1    Simmons, C.P.2    Thanh, T.T.3    Hien, V.M.4    Smith, G.J.5
  • 58
    • 1642405248 scopus 로고    scopus 로고
    • Beta-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis
    • Chen CI, Schaller-Bals S, Paul KP, Wahn U, Bals R, (2004) Beta-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis. J Cyst Fibros 3: 45-50.
    • (2004) J Cyst Fibros , vol.3 , pp. 45-50
    • Chen, C.I.1    Schaller-Bals, S.2    Paul, K.P.3    Wahn, U.4    Bals, R.5
  • 59
    • 0036528903 scopus 로고    scopus 로고
    • Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection
    • Schaller-Bals S, Schulze A, Bals R, (2002) Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection. Am J Respir Crit Care Med 165: 992-995.
    • (2002) Am J Respir Crit Care Med , vol.165 , pp. 992-995
    • Schaller-Bals, S.1    Schulze, A.2    Bals, R.3
  • 60
    • 67649160595 scopus 로고    scopus 로고
    • Interactions of {alpha}-, {beta}-, and {theta}-Defensins with Influenza A Virus and Surfactant Protein D
    • Doss M, White MR, Tecle T, Gantz D, Crouch EC, et al. (2009) Interactions of {alpha}-, {beta}-, and {theta}-Defensins with Influenza A Virus and Surfactant Protein D. J Immunol 182: 7878-7887.
    • (2009) J Immunol , vol.182 , pp. 7878-7887
    • Doss, M.1    White, M.R.2    Tecle, T.3    Gantz, D.4    Crouch, E.C.5
  • 62
    • 78149423945 scopus 로고    scopus 로고
    • The human host defense peptide LL-37 interacts with Neisseria meningitidis capsular polysaccharides and inhibits inflammatory mediators release
    • Zughaier SM, Svoboda P, Pohl J, Stephens DS, Shafer WM, (2010) The human host defense peptide LL-37 interacts with Neisseria meningitidis capsular polysaccharides and inhibits inflammatory mediators release. PLoS One 5: e13627.
    • (2010) PLoS One , vol.5
    • Zughaier, S.M.1    Svoboda, P.2    Pohl, J.3    Stephens, D.S.4    Shafer, W.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.