메뉴 건너뛰기




Volumn 6, Issue 3, 2011, Pages

Human antimicrobial peptide LL-37 inhibits adhesion of Candida albicans by interacting with yeast cell-wall carbohydrates

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CHITIN; GLUCAN; MANNAN; ANTIMICROBIAL PEPTIDE LL-37; CATHELICIDIN; POLYSTYRENE DERIVATIVE;

EID: 79952679401     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0017755     Document Type: Article
Times cited : (148)

References (69)
  • 4
    • 24644483572 scopus 로고    scopus 로고
    • John E. Bennett Forum on Deep Mycoses Study Design 2004: Candidiasis and salvage therapy for aspergillosis
    • Wenzel RP, (2005) John E. Bennett Forum on Deep Mycoses Study Design 2004: Candidiasis and salvage therapy for aspergillosis. Clin Infect Dis 41 (Suppl 6): S369-370.
    • (2005) Clin Infect Dis , vol.41 , Issue.SUPPL. 6
    • Wenzel, R.P.1
  • 5
    • 0141789642 scopus 로고    scopus 로고
    • Candida albicans secreted aspartyl proteinases in virulence and pathogenesis
    • Naglik JR, Challacombe SJ, Hube B, (2003) Candida albicans secreted aspartyl proteinases in virulence and pathogenesis. Microbiol Mol Biol Rev 67: 400-428.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 400-428
    • Naglik, J.R.1    Challacombe, S.J.2    Hube, B.3
  • 6
    • 67651173120 scopus 로고    scopus 로고
    • Identifying infection-associated genes of Candida albicans in the postgenomic era
    • Wilson D, Thewes S, Zakikhany K, Fradin C, Albrecht A, et al. (2009) Identifying infection-associated genes of Candida albicans in the postgenomic era. FEMS Yeast Res 9: 688-700.
    • (2009) FEMS Yeast Res , vol.9 , pp. 688-700
    • Wilson, D.1    Thewes, S.2    Zakikhany, K.3    Fradin, C.4    Albrecht, A.5
  • 7
    • 33846027505 scopus 로고    scopus 로고
    • Fungal invasion of normally non-phagocytic host cells
    • Filler SG, Sheppard DC, (2006) Fungal invasion of normally non-phagocytic host cells. PLoS Pathog 2: e129.
    • (2006) PLoS Pathog , vol.2
    • Filler, S.G.1    Sheppard, D.C.2
  • 8
    • 33746477658 scopus 로고    scopus 로고
    • Candida-host cell receptor-ligand interactions
    • Filler SG, (2006) Candida-host cell receptor-ligand interactions. Curr Opin Microbiol 9: 333-339.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 333-339
    • Filler, S.G.1
  • 10
    • 77950609407 scopus 로고    scopus 로고
    • Interactions of Candida albicans with epithelial cells
    • Zhu W, Filler SG, (2010) Interactions of Candida albicans with epithelial cells. Cell Microbiol 12: 273-282.
    • (2010) Cell Microbiol , vol.12 , pp. 273-282
    • Zhu, W.1    Filler, S.G.2
  • 11
    • 33748920925 scopus 로고    scopus 로고
    • The structure and synthesis of the fungal cell wall
    • Bowman SM, Free SJ, (2006) The structure and synthesis of the fungal cell wall. Bioessays 28: 799-808.
    • (2006) Bioessays , vol.28 , pp. 799-808
    • Bowman, S.M.1    Free, S.J.2
  • 13
    • 0036156138 scopus 로고    scopus 로고
    • Cytokine and chemokine production by human oral and vaginal epithelial cells in response to Candida albicans
    • Steele C, Fidel PL Jr, (2002) Cytokine and chemokine production by human oral and vaginal epithelial cells in response to Candida albicans. Infect Immun 70: 577-583.
    • (2002) Infect Immun , vol.70 , pp. 577-583
    • Steele, C.1    Fidel Jr., P.L.2
  • 14
    • 22944435825 scopus 로고    scopus 로고
    • Antimicrobial peptides in the oral environment: expression and function in health and disease
    • Dale BA, Fredericks LP, (2005) Antimicrobial peptides in the oral environment: expression and function in health and disease. Curr Issues Mol Biol 7: 119-133.
    • (2005) Curr Issues Mol Biol , vol.7 , pp. 119-133
    • Dale, B.A.1    Fredericks, L.P.2
  • 15
    • 21744462099 scopus 로고    scopus 로고
    • Human beta-defensins: differential activity against candidal species and regulation by Candida albicans
    • Feng Z, Jiang B, Chandra J, Ghannoum M, Nelson S, et al. (2005) Human beta-defensins: differential activity against candidal species and regulation by Candida albicans. J Dent Res 84: 445-450.
    • (2005) J Dent Res , vol.84 , pp. 445-450
    • Feng, Z.1    Jiang, B.2    Chandra, J.3    Ghannoum, M.4    Nelson, S.5
  • 16
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M, (2002) Antimicrobial peptides of multicellular organisms. Nature 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 17
    • 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
  • 18
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock RE, Sahl HG, (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 24: 1551-1557.
    • (2006) Nat Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 19
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden KA, (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3: 238-250.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 21
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park CB, Kim HS, Kim SC, (1998) Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochemical and Biophysical Research Communications 244: 253-257.
    • (1998) Biochemical and Biophysical Research Communications , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 22
    • 0037428394 scopus 로고    scopus 로고
    • Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes
    • Takeshima K, Chikushi A, Lee KK, Yonehara S, Matsuzaki K, (2003) Translocation of analogues of the antimicrobial peptides magainin and buforin across human cell membranes. Journal of Biological Chemistry 278: 1310-1315.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 1310-1315
    • Takeshima, K.1    Chikushi, A.2    Lee, K.K.3    Yonehara, S.4    Matsuzaki, K.5
  • 24
    • 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
  • 25
    • 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
  • 26
    • 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
  • 27
    • 21444456146 scopus 로고    scopus 로고
    • Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37
    • Ciornei CD, Sigurdardottir T, Schmidtchen A, Bodelsson M, (2005) Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37. Antimicrob Agents Chemother 49: 2845-2850.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2845-2850
    • Ciornei, C.D.1    Sigurdardottir, T.2    Schmidtchen, A.3    Bodelsson, M.4
  • 28
    • 20544447535 scopus 로고    scopus 로고
    • Candidacidal effects of two antimicrobial peptides: histatin 5 causes small membrane defects, but LL-37 causes massive disruption of the cell membrane
    • den Hertog AL, van Marle J, van Veen HA, Van't Hof W, Bolscher JG, et al. (2005) Candidacidal effects of two antimicrobial peptides: histatin 5 causes small membrane defects, but LL-37 causes massive disruption of the cell membrane. Biochem J 388: 689-695.
    • (2005) Biochem J , vol.388 , pp. 689-695
    • den Hertog, A.L.1    van Marle, J.2    van Veen, H.A.3    Van't Hof, W.4    Bolscher, J.G.5
  • 29
    • 33644839600 scopus 로고    scopus 로고
    • Flocculation, adhesion and biofilm formation in yeasts
    • Verstrepen KJ, Klis FM, (2006) Flocculation, adhesion and biofilm formation in yeasts. Mol Microbiol 60: 5-15.
    • (2006) Mol Microbiol , vol.60 , pp. 5-15
    • Verstrepen, K.J.1    Klis, F.M.2
  • 30
    • 29144521244 scopus 로고    scopus 로고
    • Human antimicrobial peptides: defensins, cathelicidins and histatins
    • De Smet K, Contreras R, (2005) Human antimicrobial peptides: defensins, cathelicidins and histatins. Biotechnol Lett 27: 1337-1347.
    • (2005) Biotechnol Lett , vol.27 , pp. 1337-1347
    • De Smet, K.1    Contreras, R.2
  • 31
    • 51949116049 scopus 로고    scopus 로고
    • Candida albicans cell wall proteins
    • Chaffin WL, (2008) Candida albicans cell wall proteins. Microbiol Mol Biol Rev 72: 495-544.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 495-544
    • Chaffin, W.L.1
  • 33
    • 2042489656 scopus 로고    scopus 로고
    • Surface glycans of Candida albicans and other pathogenic fungi: physiological roles, clinical uses, and experimental challenges
    • Masuoka J, (2004) Surface glycans of Candida albicans and other pathogenic fungi: physiological roles, clinical uses, and experimental challenges. Clin Microbiol Rev 17: 281-310.
    • (2004) Clin Microbiol Rev , vol.17 , pp. 281-310
    • Masuoka, J.1
  • 34
    • 34748873304 scopus 로고    scopus 로고
    • The cell wall: a carbohydrate armour for the fungal cell
    • Latge JP, (2007) The cell wall: a carbohydrate armour for the fungal cell. Mol Microbiol 66: 279-290.
    • (2007) Mol Microbiol , vol.66 , pp. 279-290
    • Latge, J.P.1
  • 35
    • 0026729502 scopus 로고
    • Role of specific determinants in mannan of Candida albicans serotype A in adherence to human buccal epithelial cells
    • Miyakawa Y, Kuribayashi T, Kagaya K, Suzuki M, Nakase T, et al. (1992) Role of specific determinants in mannan of Candida albicans serotype A in adherence to human buccal epithelial cells. Infect Immun 60: 2493-2499.
    • (1992) Infect Immun , vol.60 , pp. 2493-2499
    • Miyakawa, Y.1    Kuribayashi, T.2    Kagaya, K.3    Suzuki, M.4    Nakase, T.5
  • 36
    • 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
  • 38
    • 24644446352 scopus 로고    scopus 로고
    • Candiduria
    • Kauffman CA, (2005) Candiduria. Clin Infect Dis 41 (Suppl 6): S371-376.
    • (2005) Clin Infect Dis , vol.41 , Issue.SUPPL. 6
    • Kauffman, C.A.1
  • 41
    • 51949104801 scopus 로고    scopus 로고
    • Human host defense peptide LL-37 prevents bacterial biofilm formation
    • Overhage J, Campisano A, Bains M, Torfs EC, Rehm BH, et al. (2008) Human host defense peptide LL-37 prevents bacterial biofilm formation. Infect Immun 76: 4176-4182.
    • (2008) Infect Immun , vol.76 , pp. 4176-4182
    • Overhage, J.1    Campisano, A.2    Bains, M.3    Torfs, E.C.4    Rehm, B.H.5
  • 42
    • 58149263244 scopus 로고    scopus 로고
    • The roles of cathelicidin LL-37 in immune defences and novel clinical applications
    • Nijnik A, Hancock RE, (2009) The roles of cathelicidin LL-37 in immune defences and novel clinical applications. Curr Opin Hematol 16: 41-47.
    • (2009) Curr Opin Hematol , vol.16 , pp. 41-47
    • Nijnik, A.1    Hancock, R.E.2
  • 43
    • 74049150646 scopus 로고    scopus 로고
    • Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation of Staphylococcus epidermidis
    • Hell E, Giske CG, Nelson A, Romling U, Marchini G, (2010) Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation of Staphylococcus epidermidis. Lett Appl Microbiol 50: 211-215.
    • (2010) Lett Appl Microbiol , vol.50 , pp. 211-215
    • Hell, E.1    Giske, C.G.2    Nelson, A.3    Romling, U.4    Marchini, G.5
  • 44
    • 34247370223 scopus 로고    scopus 로고
    • A novel method for purifying recombinant human host defense cathelicidin LL-37 by utilizing its inherent property of aggregation
    • Li Y, Li X, Li H, Lockridge O, Wang G, (2007) A novel method for purifying recombinant human host defense cathelicidin LL-37 by utilizing its inherent property of aggregation. Protein Expr Purif 54: 157-165.
    • (2007) Protein Expr Purif , vol.54 , pp. 157-165
    • Li, Y.1    Li, X.2    Li, H.3    Lockridge, O.4    Wang, G.5
  • 45
    • 65949101251 scopus 로고    scopus 로고
    • Inhibition of cathelicidin activity by bacterial exopolysaccharides
    • Foschiatti M, Cescutti P, Tossi A, Rizzo R, (2009) Inhibition of cathelicidin activity by bacterial exopolysaccharides. Mol Microbiol 72: 1137-1146.
    • (2009) Mol Microbiol , vol.72 , pp. 1137-1146
    • Foschiatti, M.1    Cescutti, P.2    Tossi, A.3    Rizzo, R.4
  • 46
    • 68949117860 scopus 로고    scopus 로고
    • LL-37 complexation with glycosaminoglycans in cystic fibrosis lungs inhibits antimicrobial activity, which can be restored by hypertonic saline
    • Bergsson G, Reeves EP, McNally P, Chotirmall SH, Greene CM, et al. (2009) LL-37 complexation with glycosaminoglycans in cystic fibrosis lungs inhibits antimicrobial activity, which can be restored by hypertonic saline. J Immunol 183: 543-551.
    • (2009) J Immunol , vol.183 , pp. 543-551
    • Bergsson, G.1    Reeves, E.P.2    McNally, P.3    Chotirmall, S.H.4    Greene, C.M.5
  • 47
    • 0022365462 scopus 로고
    • Immunochemical study on the mannans of Candida albicans NIH A-207, NIH B-792, and J-1012 strains prepared by fractional precipitation with cetyltrimethylammonium bromide
    • Shibata N, Ichikawa T, Tojo M, Takahashi M, Ito N, et al. (1985) Immunochemical study on the mannans of Candida albicans NIH A-207, NIH B-792, and J-1012 strains prepared by fractional precipitation with cetyltrimethylammonium bromide. Arch Biochem Biophys 243: 338-348.
    • (1985) Arch Biochem Biophys , vol.243 , pp. 338-348
    • Shibata, N.1    Ichikawa, T.2    Tojo, M.3    Takahashi, M.4    Ito, N.5
  • 48
    • 33749125248 scopus 로고    scopus 로고
    • Galectin-3 induces death of Candida species expressing specific beta-1,2-linked mannans
    • Kohatsu L, Hsu DK, Jegalian AG, Liu FT, Baum LG, (2006) Galectin-3 induces death of Candida species expressing specific beta-1,2-linked mannans. J Immunol 177: 4718-4726.
    • (2006) J Immunol , vol.177 , pp. 4718-4726
    • Kohatsu, L.1    Hsu, D.K.2    Jegalian, A.G.3    Liu, F.T.4    Baum, L.G.5
  • 49
    • 0027290863 scopus 로고
    • Chemical definition of an epitope/adhesin molecule on Candida albicans
    • Li RK, Cutler JE, (1993) Chemical definition of an epitope/adhesin molecule on Candida albicans. J Biol Chem 268: 18293-18299.
    • (1993) J Biol Chem , vol.268 , pp. 18293-18299
    • Li, R.K.1    Cutler, J.E.2
  • 50
    • 0036895520 scopus 로고    scopus 로고
    • Synthetic analogues of beta-1,2 oligomannosides prevent intestinal colonization by the pathogenic yeast Candida albicans
    • Dromer F, Chevalier R, Sendid B, Improvisi L, Jouault T, et al. (2002) Synthetic analogues of beta-1,2 oligomannosides prevent intestinal colonization by the pathogenic yeast Candida albicans. Antimicrob Agents Chemother 46: 3869-3876.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3869-3876
    • Dromer, F.1    Chevalier, R.2    Sendid, B.3    Improvisi, L.4    Jouault, T.5
  • 52
    • 34047250154 scopus 로고    scopus 로고
    • The 65 kDa mannoprotein gene of Candida albicans encodes a putative beta-glucanase adhesin required for hyphal morphogenesis and experimental pathogenicity
    • Sandini S, La Valle R, De Bernardis F, Macri C, Cassone A, (2007) The 65 kDa mannoprotein gene of Candida albicans encodes a putative beta-glucanase adhesin required for hyphal morphogenesis and experimental pathogenicity. Cell Microbiol 9: 1223-1238.
    • (2007) Cell Microbiol , vol.9 , pp. 1223-1238
    • Sandini, S.1    la Valle, R.2    de Bernardis, F.3    Macri, C.4    Cassone, A.5
  • 53
    • 53849108792 scopus 로고    scopus 로고
    • Identification of a novel protein promoting the colonization and survival of Finegoldia magna, a bacterial commensal and opportunistic pathogen
    • Frick IM, Karlsson C, Morgelin M, Olin AI, Janjusevic R, et al. (2008) Identification of a novel protein promoting the colonization and survival of Finegoldia magna, a bacterial commensal and opportunistic pathogen. Mol Microbiol 70: 695-708.
    • (2008) Mol Microbiol , vol.70 , pp. 695-708
    • Frick, I.M.1    Karlsson, C.2    Morgelin, M.3    Olin, A.I.4    Janjusevic, R.5
  • 54
    • 56249122900 scopus 로고    scopus 로고
    • Human beta-defensin 3 binds to hemagglutinin B (rHagB), a non-fimbrial adhesin from Porphyromonas gingivalis, and attenuates a pro-inflammatory cytokine response
    • Pingel LC, Kohlgraf KG, Hansen CJ, Eastman CG, Dietrich DE, et al. (2008) Human beta-defensin 3 binds to hemagglutinin B (rHagB), a non-fimbrial adhesin from Porphyromonas gingivalis, and attenuates a pro-inflammatory cytokine response. Immunol Cell Biol 86: 643-649.
    • (2008) Immunol Cell Biol , vol.86 , pp. 643-649
    • Pingel, L.C.1    Kohlgraf, K.G.2    Hansen, C.J.3    Eastman, C.G.4    Dietrich, D.E.5
  • 55
    • 57349161186 scopus 로고    scopus 로고
    • Human alpha- and beta-defensins bind to immobilized adhesins from Porphyromonas gingivalis
    • Dietrich DE, Xiao X, Dawson DV, Belanger M, Xie H, et al. (2008) Human alpha- and beta-defensins bind to immobilized adhesins from Porphyromonas gingivalis. Infect Immun 76: 5714-5720.
    • (2008) Infect Immun , vol.76 , pp. 5714-5720
    • Dietrich, D.E.1    Xiao, X.2    Dawson, D.V.3    Belanger, M.4    Xie, H.5
  • 56
    • 0019523437 scopus 로고
    • Role of Surface Mannan in the Adherence of Candida-Albicans to Fibrin-Platelet Clots Formed Invitro
    • Maisch PA, Calderone RA, (1981) Role of Surface Mannan in the Adherence of Candida-Albicans to Fibrin-Platelet Clots Formed Invitro. Infection and Immunity 32: 92-97.
    • (1981) Infection and Immunity , vol.32 , pp. 92-97
    • Maisch, P.A.1    Calderone, R.A.2
  • 57
    • 65649114368 scopus 로고    scopus 로고
    • Loss of mannosylphosphate from Candida albicans cell wall proteins results in enhanced resistance to the inhibitory effect of a cationic antimicrobial peptide via reduced peptide binding to the cell surface
    • Harris M, Mora-Montes HM, Gow NA, Coote PJ, (2009) Loss of mannosylphosphate from Candida albicans cell wall proteins results in enhanced resistance to the inhibitory effect of a cationic antimicrobial peptide via reduced peptide binding to the cell surface. Microbiology 155: 1058-1070.
    • (2009) Microbiology , vol.155 , pp. 1058-1070
    • Harris, M.1    Mora-Montes, H.M.2    Gow, N.A.3    Coote, P.J.4
  • 58
    • 77955343248 scopus 로고    scopus 로고
    • Inhibition of adherence of Corynebacterium diphtheriae to human buccal epithelium by glycoside hydrolases from marine hydrobiontes
    • Zaporozhets TS, Makarenkova ID, Bakunina I, Burtseva Iu V, Kusaikin MI, et al. (2010) [Inhibition of adherence of Corynebacterium diphtheriae to human buccal epithelium by glycoside hydrolases from marine hydrobiontes]. Biomed Khim 56: 351-359.
    • (2010) Biomed Khim , vol.56 , pp. 351-359
    • Zaporozhets, T.S.1    Makarenkova, I.D.2    Bakunina, I.3    Burtseva Iu, V.4    Kusaikin, M.I.5
  • 59
    • 58149269544 scopus 로고    scopus 로고
    • Dynamic, morphotype-specific Candida albicans beta-glucan exposure during infection and drug treatment
    • Wheeler RT, Kombe D, Agarwala SD, Fink GR, (2008) Dynamic, morphotype-specific Candida albicans beta-glucan exposure during infection and drug treatment. PLoS Pathog 4: e1000227.
    • (2008) PLoS Pathog , vol.4
    • Wheeler, R.T.1    Kombe, D.2    Agarwala, S.D.3    Fink, G.R.4
  • 60
    • 33646242974 scopus 로고    scopus 로고
    • A drug-sensitive genetic network masks fungi from the immune system
    • Wheeler RT, Fink GR, (2006) A drug-sensitive genetic network masks fungi from the immune system. PLoS Pathog 2: e35.
    • (2006) PLoS Pathog , vol.2
    • Wheeler, R.T.1    Fink, G.R.2
  • 61
    • 76749084670 scopus 로고    scopus 로고
    • Synthetic antimicrobial peptide L8 (MHLHKTSRVTLYLL) has membrane permeabilisation and bacterial aggregation activity
    • Loit E, Hincke MT, Altosaar I, (2010) Synthetic antimicrobial peptide L8 (MHLHKTSRVTLYLL) has membrane permeabilisation and bacterial aggregation activity. Int J Antimicrob Agents 35: 410-411.
    • (2010) Int J Antimicrob Agents , vol.35 , pp. 410-411
    • Loit, E.1    Hincke, M.T.2    Altosaar, I.3
  • 62
    • 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
  • 63
    • 2542480000 scopus 로고    scopus 로고
    • Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense
    • Yang D, Biragyn A, Hoover DM, Lubkowski J, Oppenheim JJ, (2004) Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annu Rev Immunol 22: 181-215.
    • (2004) Annu Rev Immunol , vol.22 , pp. 181-215
    • Yang, D.1    Biragyn, A.2    Hoover, D.M.3    Lubkowski, J.4    Oppenheim, J.J.5
  • 64
    • 0021742042 scopus 로고
    • Isolation of the Candida albicans gene for orotidine-5′-phosphate decarboxylase by complementation of S. cerevisiae ura3 and E. coli pyrF mutations
    • Gillum AM, Tsay EY, Kirsch DR, (1984) Isolation of the Candida albicans gene for orotidine-5′-phosphate decarboxylase by complementation of S. cerevisiae ura3 and E. coli pyrF mutations. Mol Gen Genet 198: 179-182.
    • (1984) Mol Gen Genet , vol.198 , pp. 179-182
    • Gillum, A.M.1    Tsay, E.Y.2    Kirsch, D.R.3
  • 66
    • 33947273030 scopus 로고    scopus 로고
    • Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells
    • Phan QT, Myers CL, Fu Y, Sheppard DC, Yeaman MR, et al. (2007) Als3 is a Candida albicans invasin that binds to cadherins and induces endocytosis by host cells. PLoS Biol 5: e64.
    • (2007) PLoS Biol , vol.5
    • Phan, Q.T.1    Myers, C.L.2    Fu, Y.3    Sheppard, D.C.4    Yeaman, M.R.5
  • 67
  • 68
    • 40049083456 scopus 로고    scopus 로고
    • A short-form C-type lectin from amphioxus acts as a direct microbial killing protein via interaction with peptidoglycan and glucan
    • Yu Y, Huang H, Feng K, Pan M, Yuan S, et al. (2007) A short-form C-type lectin from amphioxus acts as a direct microbial killing protein via interaction with peptidoglycan and glucan. J Immunol 179: 8425-8434.
    • (2007) J Immunol , vol.179 , pp. 8425-8434
    • Yu, Y.1    Huang, H.2    Feng, K.3    Pan, M.4    Yuan, S.5
  • 69
    • 35148818645 scopus 로고    scopus 로고
    • Quantitative measurements of vancomycin binding to self-assembled peptide monolayers on chips by quartz crystal microbalance
    • Tseng MC, Chang YP, Chu YH, (2007) Quantitative measurements of vancomycin binding to self-assembled peptide monolayers on chips by quartz crystal microbalance. Anal Biochem 371: 1-9.
    • (2007) Anal Biochem , vol.371 , pp. 1-9
    • Tseng, M.C.1    Chang, Y.P.2    Chu, Y.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.