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Volumn 11, Issue 1, 1999, Pages 23-27

Antimicrobial peptides in mammalian and insect host defence

Author keywords

[No Author keywords available]

Indexed keywords

BACTERICIDAL ACTIVITY; CELL GRANULE; CYTOTOXIC T LYMPHOCYTE; DROSOPHILA; HUMAN; IMMUNITY; MYCOBACTERIUM TUBERCULOSIS; NATURAL KILLER CELL; NONHUMAN; PATHOGENESIS; RESPIRATORY TRACT INFECTION; REVIEW;

EID: 0033067196     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(99)80005-3     Document Type: Article
Times cited : (688)

References (54)
  • 1
    • 0031821708 scopus 로고    scopus 로고
    • Gene-encoded peptide antibiotics and the concept of innate immunity: An update review
    • This is an insightful and colorful review by a pioneer in the field.
    • Boman HG Gene-encoded peptide antibiotics and the concept of innate immunity: an update review. Scand J Immunol. 48:1998;15-25. This is an insightful and colorful review by a pioneer in the field.
    • (1998) Scand J Immunol , vol.48 , pp. 15-25
    • Boman, H.G.1
  • 2
    • 0031281940 scopus 로고    scopus 로고
    • Antimicrobial peptide defense in Drosophila
    • This is an insightful and comprehensive view of the antimicrobial peptide response in Drosophila. The spatzle/Toll/cactus regulatory systems of Drosophila are described and compared to cytokine-induced activation of the transcription factor NF-κB in mammalian cells.
    • Meister M, Lemaitre B, Hoffmann JA Antimicrobial peptide defense in Drosophila. Bioessays. 19:1997;1019-1026. This is an insightful and comprehensive view of the antimicrobial peptide response in Drosophila. The spatzle/Toll/cactus regulatory systems of Drosophila are described and compared to cytokine-induced activation of the transcription factor NF-κB in mammalian cells.
    • (1997) Bioessays , vol.19 , pp. 1019-1026
    • Meister, M.1    Lemaitre, B.2    Hoffmann, J.A.3
  • 3
    • 0032168228 scopus 로고    scopus 로고
    • Beta-defensins: Endogenous antibiotics of the innate host defense response
    • Diamond G, Bevins CL Beta-defensins: endogenous antibiotics of the innate host defense response. Clin Immunol Immunopathol. 88:1998;221-225.
    • (1998) Clin Immunol Immunopathol , vol.88 , pp. 221-225
    • Diamond, G.1    Bevins, C.L.2
  • 4
    • 0032484654 scopus 로고    scopus 로고
    • Localization and genomic organization of sheep antimicrobial peptide genes
    • Huttner KM, Lambeth MR, Burkin HR, Burkin DJ, Broad TE Localization and genomic organization of sheep antimicrobial peptide genes. Gene. 206:1998;85-91.
    • (1998) Gene , vol.206 , pp. 85-91
    • Huttner, K.M.1    Lambeth, M.R.2    Burkin, H.R.3    Burkin, D.J.4    Broad, T.E.5
  • 5
    • 0030728214 scopus 로고    scopus 로고
    • Structural organization of the bovine cathelicidin gene family and identification of a novel member
    • Scocchi M, Wang S, Zanetti M Structural organization of the bovine cathelicidin gene family and identification of a novel member. FEBS Lett. 417:1997;311-315.
    • (1997) FEBS Lett , vol.417 , pp. 311-315
    • Scocchi, M.1    Wang, S.2    Zanetti, M.3
  • 6
    • 0031882530 scopus 로고    scopus 로고
    • Expression of beta-defensin genes in bovine alveolar macrophages
    • Ryan LK, Rhodes J, Bhat M, Diamond G Expression of beta-defensin genes in bovine alveolar macrophages. Infect Immun. 66:1998;878-881.
    • (1998) Infect Immun , vol.66 , pp. 878-881
    • Ryan, L.K.1    Rhodes, J.2    Bhat, M.3    Diamond, G.4
  • 7
    • 0031756983 scopus 로고    scopus 로고
    • Timing, targeting and sorting of azurophil granule proteins in human myeloid cells
    • Arnljots K, Sorensen O, Lollike K, Borregaard N Timing, targeting and sorting of azurophil granule proteins in human myeloid cells. Leukemia. 12:1998;1789-1795.
    • (1998) Leukemia , vol.12 , pp. 1789-1795
    • Arnljots, K.1    Sorensen, O.2    Lollike, K.3    Borregaard, N.4
  • 8
    • 0031898688 scopus 로고    scopus 로고
    • Gene expression, immunolocalization, and secretion of human defensin-5 in human female reproductive tract
    • This study localized this α-defensin to where it could defend against ascending bacterial infections, especially during portions of the menstrual cycle that are highly conducive to fertilization.
    • Quayle AJ, Porter EM, Nussbaum AA, Wang YM, Brabec C, Yip KP, Mok SC Gene expression, immunolocalization, and secretion of human defensin-5 in human female reproductive tract. Am J Pathol. 152:1998;1247-1258. This study localized this α-defensin to where it could defend against ascending bacterial infections, especially during portions of the menstrual cycle that are highly conducive to fertilization.
    • (1998) Am J Pathol , vol.152 , pp. 1247-1258
    • Quayle, A.J.1    Porter, E.M.2    Nussbaum, A.A.3    Wang, Y.M.4    Brabec, C.5    Yip, K.P.6    Mok, S.C.7
  • 9
    • 0031863272 scopus 로고    scopus 로고
    • RK-2: A novel rabbit kidney defensin and its implications for renal host defense
    • Wu ER, Daniel R, Bateman A RK-2: a novel rabbit kidney defensin and its implications for renal host defense. Peptides. 19:1998;793-799.
    • (1998) Peptides , vol.19 , pp. 793-799
    • Wu, E.R.1    Daniel, R.2    Bateman, A.3
  • 10
    • 0032523214 scopus 로고    scopus 로고
    • Human beta-defensin-1: An antimicrobial peptide of urogenital tissues
    • In this paper the processing, localization and function of hBD-1 are characterized. The peptide is especially well placed to protect the upper nephron from infection by bacteria ascending from the bladder.
    • Valore EV, Park CH, Quayle AJ, Wiles KR, McCray PB Jr., Ganz T Human beta-defensin-1: an antimicrobial peptide of urogenital tissues. J Clin Invest. 101:1998;1633-1642. In this paper the processing, localization and function of hBD-1 are characterized. The peptide is especially well placed to protect the upper nephron from infection by bacteria ascending from the bladder.
    • (1998) J Clin Invest , vol.101 , pp. 1633-1642
    • Valore, E.V.1    Park, C.H.2    Quayle, A.J.3    Wiles, K.R.4    McCray P.B., Jr.5    Ganz, T.6
  • 13
    • 0031913244 scopus 로고    scopus 로고
    • Mouse β-defensin 1 is a salt-sensitive antimicrobrial peptide present in epithelia of the lung and urogenital tract
    • Bals R, Goldman MJ, Wilson JM Mouse β-defensin 1 is a salt-sensitive antimicrobrial peptide present in epithelia of the lung and urogenital tract. Infect Immun. 66:1998;1225-1232.
    • (1998) Infect Immun , vol.66 , pp. 1225-1232
    • Bals, R.1    Goldman, M.J.2    Wilson, J.M.3
  • 14
    • 0031662487 scopus 로고    scopus 로고
    • Expression of the peptide antibiotic human beta-defensin 1 in cultured gingival epithelial cells and gingival tissue
    • Krisanaprakornkit S, Weinberg A, Perez CN, Dale BA Expression of the peptide antibiotic human beta-defensin 1 in cultured gingival epithelial cells and gingival tissue. Infect Immun. 66:1998;4222-4228.
    • (1998) Infect Immun , vol.66 , pp. 4222-4228
    • Krisanaprakornkit, S.1    Weinberg, A.2    Perez, C.N.3    Dale, B.A.4
  • 15
    • 0031925507 scopus 로고    scopus 로고
    • Beta-sheet antibiotic peptides as potential dental therapeutics
    • Miyasaki KT, Lehrer RI Beta-sheet antibiotic peptides as potential dental therapeutics. Int J Antimicrob Agents. 9:1998;269-280.
    • (1998) Int J Antimicrob Agents , vol.9 , pp. 269-280
    • Miyasaki, K.T.1    Lehrer, R.I.2
  • 16
    • 0032169557 scopus 로고    scopus 로고
    • Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung
    • The demonstration of the inducible expression of this peptide is of particular interest. Its inhibition by high salt is a typical defensin feature.
    • Bals R, Wang X, Wu Z, Freeman T, Bafna V, Zasloff M, Wilson JM Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung. J Clin Invest. 102:1998;874-880. The demonstration of the inducible expression of this peptide is of particular interest. Its inhibition by high salt is a typical defensin feature.
    • (1998) J Clin Invest , vol.102 , pp. 874-880
    • Bals, R.1    Wang, X.2    Wu, Z.3    Freeman, T.4    Bafna, V.5    Zasloff, M.6    Wilson, J.M.7
  • 17
    • 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 NY Acad Sci. 832:1997;147-162.
    • (1997) Ann NY Acad Sci , vol.832 , pp. 147-162
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 18
    • 0032482980 scopus 로고    scopus 로고
    • The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface
    • The authors show that this LPS-binding, α-helical peptide can act directly or synergistically to kill or detoxify bacteria entering the airways.
    • Bals R, Wang X, Zasloff M, Wilson JM The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface. Proc Natl Acad Sci USA. 95:1998;9541-9546. The authors show that this LPS-binding, α-helical peptide can act directly or synergistically to kill or detoxify bacteria entering the airways.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9541-9546
    • Bals, R.1    Wang, X.2    Zasloff, M.3    Wilson, J.M.4
  • 19
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Potent, salt-independent antimicrobial activity and co-operative binding of lipopolysaccharide by this human peptide were shown in this paper.
    • Turner J, Cho Y, Dinh NN, Waring AJ, Lehrer RI Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob Agents Chemother. 42:1998;2206-2214. Potent, salt-independent antimicrobial activity and co-operative binding of lipopolysaccharide by this human peptide were shown in this paper.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 20
    • 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. 273:1998;3718-3724.
    • (1998) J Biol Chem , vol.273 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 21
    • 0031925180 scopus 로고    scopus 로고
    • Protective effects of a human 18-kilodalton cationic antimicrobial protein (CAP18)-derived peptide against murine endotoxemia
    • Kirikae T, Hirata M, Yamasu H, Kirikae F, Tamura H, Kayama F, Nakatsuka K, Yokochi T, Nakano M Protective effects of a human 18-kilodalton cationic antimicrobial protein (CAP18)-derived peptide against murine endotoxemia. Infect Immun. 66:1998;1861-1868.
    • (1998) Infect Immun , vol.66 , pp. 1861-1868
    • Kirikae, T.1    Hirata, M.2    Yamasu, H.3    Kirikae, F.4    Tamura, H.5    Kayama, F.6    Nakatsuka, K.7    Yokochi, T.8    Nakano, M.9
  • 22
    • 0031870993 scopus 로고    scopus 로고
    • The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids
    • The authors provide evidence that protegrins contribute substantially in vivo to the antimicrobial properties of porcine exudate fluids. Previous studies suggest that LL-37 may play a similar role in humans.
    • Shi J, Ganz T The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids. Infect Immun. 66:1998;3611-3617. The authors provide evidence that protegrins contribute substantially in vivo to the antimicrobial properties of porcine exudate fluids. Previous studies suggest that LL-37 may play a similar role in humans.
    • (1998) Infect Immun , vol.66 , pp. 3611-3617
    • Shi, J.1    Ganz, T.2
  • 23
    • 0031842041 scopus 로고    scopus 로고
    • Activity of protegrins against yeast-phase Candida albicans
    • Cho Y, Turner JS, Dinh NN, Lehrer RI Activity of protegrins against yeast-phase Candida albicans. Infect Immun. 66:1998;2486-2493.
    • (1998) Infect Immun , vol.66 , pp. 2486-2493
    • Cho, Y.1    Turner, J.S.2    Dinh, N.N.3    Lehrer, R.I.4
  • 24
    • 0032536098 scopus 로고    scopus 로고
    • Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study
    • This reports that oligomerization, previously shown for defensins, is probably even more important in allowing smaller β-sheet peptides to form membrane-perturbing assemblies.
    • Roumestand C, Louis V, Aumelas A, Grassy G, Calas B, Chavanieu A Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study. FEBS Lett. 421:1998;263-267. This reports that oligomerization, previously shown for defensins, is probably even more important in allowing smaller β-sheet peptides to form membrane-perturbing assemblies.
    • (1998) FEBS Lett , vol.421 , pp. 263-267
    • Roumestand, C.1    Louis, V.2    Aumelas, A.3    Grassy, G.4    Calas, B.5    Chavanieu, A.6
  • 25
    • 0032475823 scopus 로고    scopus 로고
    • An antimicrobial activity of cytolytic T cells mediated by granulysin
    • This paper shows how polypeptides equip cytolytic lymphocytes (T cells and natural killer cells) to participate in direct host defense against intracellular micro-organisms.
    • Stenger S, Hanson DA, Teitelbaum R, Dewan P, Niazi KR, Froelich CJ, Ganz T, Thoma-Uszynski S, Melian A, Bogdan Cet al. An antimicrobial activity of cytolytic T cells mediated by granulysin. Science. 282:1998;121-125. This paper shows how polypeptides equip cytolytic lymphocytes (T cells and natural killer cells) to participate in direct host defense against intracellular micro-organisms.
    • (1998) Science , vol.282 , pp. 121-125
    • Stenger, S.1    Hanson, D.A.2    Teitelbaum, R.3    Dewan, P.4    Niazi, K.R.5    Froelich, C.J.6    Ganz, T.7    Thoma-Uszynski, S.8    Melian, A.9    Bogdan, C.10
  • 26
    • 0032319580 scopus 로고    scopus 로고
    • Human salivary histatins: Promising anti-fungal therapeutic agents
    • Tsai H, Bobek LA Human salivary histatins: promising anti-fungal therapeutic agents. Crit Rev Oral Biol Med. 9:1998;480-497.
    • (1998) Crit Rev Oral Biol Med , vol.9 , pp. 480-497
    • Tsai, H.1    Bobek, L.A.2
  • 27
    • 0032493760 scopus 로고    scopus 로고
    • Candidacidal activity of salivary histatins. Identification of a histatin 5-binding protein on Candida albicans
    • Edgerton M, Koshlukova SE, Lo TE, Chrzan BG, Straubinger RM, Raj PA Candidacidal activity of salivary histatins. Identification of a histatin 5-binding protein on Candida albicans. J Biol Chem. 273:1998;20438-20447.
    • (1998) J Biol Chem , vol.273 , pp. 20438-20447
    • Edgerton, M.1    Koshlukova, S.E.2    Lo, T.E.3    Chrzan, B.G.4    Straubinger, R.M.5    Raj, P.A.6
  • 28
    • 0032544326 scopus 로고    scopus 로고
    • Histatin 5 is a substrate and not an inhibitor of the Arg- And Lys-specific proteinases of Porphyromonas gingivalis
    • O'Brien-Simpson NM, Dashper SG, Reynolds EC Histatin 5 is a substrate and not an inhibitor of the Arg- and Lys-specific proteinases of Porphyromonas gingivalis. Biochem Biophys Res Commun. 250:1998;474-478.
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 474-478
    • O'Brien-Simpson, N.M.1    Dashper, S.G.2    Reynolds, E.C.3
  • 29
    • 0000463507 scopus 로고    scopus 로고
    • Antileukoprotease: An endogenous protein in the innate mucosal defense against fungi
    • Tomee JF, Hiemstra PS, Heinzel-Wieland R, Kauffman HF Antileukoprotease: an endogenous protein in the innate mucosal defense against fungi. J Infect Dis. 176:1997;740-747.
    • (1997) J Infect Dis , vol.176 , pp. 740-747
    • Tomee, J.F.1    Hiemstra, P.S.2    Heinzel-Wieland, R.3    Kauffman, H.F.4
  • 30
    • 0032581354 scopus 로고    scopus 로고
    • Antileukoprotease in human skin: An antibiotic peptide constitutively produced by keratinocytes
    • Wiedow O, Harder J, Bartels J, Streit V, Christophers E Antileukoprotease in human skin: an antibiotic peptide constitutively produced by keratinocytes. Biochem Biophys Res Commun. 248:1998;904-909.
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 904-909
    • Wiedow, O.1    Harder, J.2    Bartels, J.3    Streit, V.4    Christophers, E.5
  • 31
    • 0031865628 scopus 로고    scopus 로고
    • Lipopolysaccharide-related stimuli induce expression of the secretory leukocyte protease inhibitor, a macrophage-derived lipopolysaccharide inhibitor
    • Jin F, Nathan CF, Radzioch D, Ding A Lipopolysaccharide-related stimuli induce expression of the secretory leukocyte protease inhibitor, a macrophage-derived lipopolysaccharide inhibitor. Infect Immun. 66:1998;2447-2452.
    • (1998) Infect Immun , vol.66 , pp. 2447-2452
    • Jin, F.1    Nathan, C.F.2    Radzioch, D.3    Ding, A.4
  • 32
    • 84903421873 scopus 로고    scopus 로고
    • Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin
    • Hwang PM, Zhou N, Shan X, Arrowsmith CH, Vogel HJ Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry. 37:1998;4288-4298.
    • (1998) Biochemistry , vol.37 , pp. 4288-4298
    • Hwang, P.M.1    Zhou, N.2    Shan, X.3    Arrowsmith, C.H.4    Vogel, H.J.5
  • 33
    • 0031690098 scopus 로고    scopus 로고
    • Antimicrobial peptides derived from pepsinogens in the stomach of the bullfrog, Rana catesbeiana
    • Minn I, Kim HS, Kim SC Antimicrobial peptides derived from pepsinogens in the stomach of the bullfrog, Rana catesbeiana. Biochim Biophys Acta. 1407:1998;31-39.
    • (1998) Biochim Biophys Acta , vol.1407 , pp. 31-39
    • Minn, I.1    Kim, H.S.2    Kim, S.C.3
  • 34
    • 0031446642 scopus 로고    scopus 로고
    • Drosophila host defense: Differential induction of antimicrobial peptide genes after infection by various classes of microorganisms
    • This reports that bacterial and fungal infections elicited selective expression of antimicrobial peptides appropriate to the inciting stimulus.
    • Lemaitre B, Reichhart JM, Hoffmann JA Drosophila host defense: differential induction of antimicrobial peptide genes after infection by various classes of microorganisms. Proc Natl Acad Sci USA. 94:1997;14614-14619. This reports that bacterial and fungal infections elicited selective expression of antimicrobial peptides appropriate to the inciting stimulus.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14614-14619
    • Lemaitre, B.1    Reichhart, J.M.2    Hoffmann, J.A.3
  • 35
    • 0032496389 scopus 로고    scopus 로고
    • Two distinct pathways can control expression of the gene encoding the Drosophila antimicrobial peptide metchnikowin
    • The authors show that expression of metchnikowin, a proline-rich peptide with antibacterial and antifungal activity, was regulated by two systems which allowed it to be expressed after challenge by bacteria or fungi.
    • Levashina EA, Ohresser S, Lemaitre B, Imler JL Two distinct pathways can control expression of the gene encoding the Drosophila antimicrobial peptide metchnikowin. J Mol Biol. 278:1998;515-527. The authors show that expression of metchnikowin, a proline-rich peptide with antibacterial and antifungal activity, was regulated by two systems which allowed it to be expressed after challenge by bacteria or fungi.
    • (1998) J Mol Biol , vol.278 , pp. 515-527
    • Levashina, E.A.1    Ohresser, S.2    Lemaitre, B.3    Imler, J.L.4
  • 36
    • 0030845264 scopus 로고    scopus 로고
    • Midgut-specific immune molecules are produced by the blood-sucking insect Stomoxys calcitrans
    • Lehane MJ, Wu D, Lehane SM Midgut-specific immune molecules are produced by the blood-sucking insect Stomoxys calcitrans. Proc Natl Acad Sci USA. 94:1997;11502-11507.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11502-11507
    • Lehane, M.J.1    Wu, D.2    Lehane, S.M.3
  • 37
    • 0032473360 scopus 로고    scopus 로고
    • A drosomycin-GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the Toll pathway
    • This technically and conceptually elegant study demonstrates the local production of antimicrobial peptides in salivary glands and in epithelial cells that line the respiratory, digestive and genital tracts. These phenomena have direct counterparts in mammals.
    • Ferrandon D, Jung AC, Criqui M, Lemaitre B, Uttenweiler-Joseph S, Michaut L, Reichhart J, Hoffmann JA A drosomycin-GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the Toll pathway. EMBO J. 17:1998;1217-1227. This technically and conceptually elegant study demonstrates the local production of antimicrobial peptides in salivary glands and in epithelial cells that line the respiratory, digestive and genital tracts. These phenomena have direct counterparts in mammals.
    • (1998) EMBO J , vol.17 , pp. 1217-1227
    • Ferrandon, D.1    Jung, A.C.2    Criqui, M.3    Lemaitre, B.4    Uttenweiler-Joseph, S.5    Michaut, L.6    Reichhart, J.7    Hoffmann, J.A.8
  • 38
    • 18144452207 scopus 로고    scopus 로고
    • Presence of antibacterial peptides on the laid egg chorion of the medfly Ceratitis capitata
    • This paper demonstrates that ceratotoxin peptides that are secreted by accessory female reproductive glands form a protective antibacterial coating on the surface of newly laid eggs. Antimicrobial peptides are also found in the seeds of plants and the genitourinary tract of mammals.
    • Marchini D, Marri L, Rosetto M, Manetti AG, Dallai R Presence of antibacterial peptides on the laid egg chorion of the medfly Ceratitis capitata. Biochem Biophys Res Commun. 240:1997;657-663. This paper demonstrates that ceratotoxin peptides that are secreted by accessory female reproductive glands form a protective antibacterial coating on the surface of newly laid eggs. Antimicrobial peptides are also found in the seeds of plants and the genitourinary tract of mammals.
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 657-663
    • Marchini, D.1    Marri, L.2    Rosetto, M.3    Manetti, A.G.4    Dallai, R.5
  • 39
    • 0030684057 scopus 로고    scopus 로고
    • Plasmodium activates the innate immune response of Anopheles gambiae mosquitoes
    • Richman AM, Dimopoulos G, Seeley D, Kafatos FC Plasmodium activates the innate immune response of Anopheles gambiae mosquitoes. EMBO J. 16:1997;6114-6119.
    • (1997) EMBO J , vol.16 , pp. 6114-6119
    • Richman, A.M.1    Dimopoulos, G.2    Seeley, D.3    Kafatos, F.C.4
  • 40
    • 0032079138 scopus 로고    scopus 로고
    • Plasmodium gallinaceum: Differential killing of some mosquito stages of the parasite by insect defensin
    • Shahabuddin M, Fields I, Bulet P, Hoffmann JA, Miller LH Plasmodium gallinaceum: differential killing of some mosquito stages of the parasite by insect defensin. Exp Parasitol. 89:1998;103-112.
    • (1998) Exp Parasitol , vol.89 , pp. 103-112
    • Shahabuddin, M.1    Fields, I.2    Bulet, P.3    Hoffmann, J.A.4    Miller, L.H.5
  • 41
    • 0030750976 scopus 로고    scopus 로고
    • Solution structure of drosomycin, the first inducible antifungal protein from insects
    • Landon C, Sodano P, Hetru C, Hoffmann J, Ptak M Solution structure of drosomycin, the first inducible antifungal protein from insects. Protein Sci. 6:1997;1878-1884.
    • (1997) Protein Sci , vol.6 , pp. 1878-1884
    • Landon, C.1    Sodano, P.2    Hetru, C.3    Hoffmann, J.4    Ptak, M.5
  • 42
    • 0032052256 scopus 로고    scopus 로고
    • A novel insect defensin from the ant Formica rufa
    • Taguchi S, Bulet P, Hoffmann JA A novel insect defensin from the ant Formica rufa. Biochimie. 80:1998;343-346.
    • (1998) Biochimie , vol.80 , pp. 343-346
    • Taguchi, S.1    Bulet, P.2    Hoffmann, J.A.3
  • 43
    • 0032528858 scopus 로고    scopus 로고
    • Identification and characterization of the antimicrobial peptide corresponding to C-terminal beta-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor
    • Lee KH, Hong SY, Oh JE, Kwon M, Yoon JH, Lee J, Lee BL, Moon HM Identification and characterization of the antimicrobial peptide corresponding to C-terminal beta-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor. Biochem J. 334:1998;99-105.
    • (1998) Biochem J , vol.334 , pp. 99-105
    • Lee, K.H.1    Hong, S.Y.2    Oh, J.E.3    Kwon, M.4    Yoon, J.H.5    Lee, J.6    Lee, B.L.7    Moon, H.M.8
  • 45
    • 0030734903 scopus 로고    scopus 로고
    • Penetration of the insect defensin A into phospholipid monolayers and formation of defensin A-lipid complexes
    • Maget-Dana R, Ptak M Penetration of the insect defensin A into phospholipid monolayers and formation of defensin A-lipid complexes. Biophys J. 73:1997;2527-2533.
    • (1997) Biophys J , vol.73 , pp. 2527-2533
    • Maget-Dana, R.1    Ptak, M.2
  • 48
    • 0032539553 scopus 로고    scopus 로고
    • Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family
    • Shafer WM, Qu X, Waring AJ, Lehrer RI Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family. Proc Natl Acad Sci USA. 95:1998;1829-1833.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.2    Waring, A.J.3    Lehrer, R.I.4
  • 49
    • 0032577940 scopus 로고    scopus 로고
    • Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria
    • Zhang L, Falla T, Wu M, Fidai S, Burian J, Kay W, Hancock RE Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria. Biochem Biophys Res Commun. 247:1998;674-680.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 674-680
    • Zhang, L.1    Falla, T.2    Wu, M.3    Fidai, S.4    Burian, J.5    Kay, W.6    Hancock, R.E.7
  • 50
    • 0032006495 scopus 로고    scopus 로고
    • Acidic peptide-mediated expression of the antimicrobial peptide buforin II as tandem repeats in Escherichia coli
    • This promising strategy produced high yields of a recombinant, 21-residue, α-helical, antimicrobial peptide in E. coli by using a construct that contained tandem repeats of the peptide separated by an acidic, cysteine-containing propiece.
    • Lee JH, Minn I, Park CB, Kim SC Acidic peptide-mediated expression of the antimicrobial peptide buforin II as tandem repeats in Escherichia coli. Protein Expr Purif. 12:1998;53-60. This promising strategy produced high yields of a recombinant, 21-residue, α-helical, antimicrobial peptide in E. coli by using a construct that contained tandem repeats of the peptide separated by an acidic, cysteine-containing propiece.
    • (1998) Protein Expr Purif , vol.12 , pp. 53-60
    • Lee, J.H.1    Minn, I.2    Park, C.B.3    Kim, S.C.4
  • 51
    • 0031451521 scopus 로고    scopus 로고
    • Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity
    • Tossi A, Tarantino C, Romeo D Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. Eur J Biochem. 250:1997;549-558.
    • (1997) Eur J Biochem , vol.250 , pp. 549-558
    • Tossi, A.1    Tarantino, C.2    Romeo, D.3
  • 52
    • 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. 16:1998;82-88.
    • (1998) Trends Biotechnol , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 54
    • 0031753591 scopus 로고    scopus 로고
    • Experimental infections of Rana esculenta with Aeromonas hydrophila: A molecular mechanism for the control of the normal flora
    • Simmaco M, Mangoni ML, Boman A, Barra D, Boman HG Experimental infections of Rana esculenta with Aeromonas hydrophila: a molecular mechanism for the control of the normal flora. Scand J Immunol. 48:1998;357-363.
    • (1998) Scand J Immunol , vol.48 , pp. 357-363
    • Simmaco, M.1    Mangoni, M.L.2    Boman, A.3    Barra, D.4    Boman, H.G.5


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