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Volumn 5, Issue 1, 2010, Pages 99-113

Defensins as anti-inflammatory compounds and mucosal adjuvants

Author keywords

Adjuvant; Defensin; Innate immunity; Mucosal immunity; Oral inflammation

Indexed keywords

ALPHA DEFENSIN; ANTIINFLAMMATORY AGENT; BETA DEFENSIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; EPIDERMAL GROWTH FACTOR RECEPTOR; GRANULOCYTE COLONY STIMULATING FACTOR; HEAT SHOCK PROTEIN 70; HEMAGGLUTININ; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 10; INTERLEUKIN 13; INTERLEUKIN 1BETA; INTERLEUKIN 4; INTERLEUKIN 6; INTERLEUKIN 8; KEYHOLE LIMPET HEMOCYANIN; MELITTIN; MITOGEN ACTIVATED PROTEIN KINASE 3; PLASMID DNA; STAT1 PROTEIN; STAT6 PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING 1; SUPPRESSOR OF CYTOKINE SIGNALING 3; TETANUS TOXOID; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 5; TUMOR NECROSIS FACTOR ALPHA;

EID: 75849147159     PISSN: 17460913     EISSN: None     Source Type: Journal    
DOI: 10.2217/fmb.09.104     Document Type: Review
Times cited : (68)

References (118)
  • 1
    • 35948971396 scopus 로고    scopus 로고
    • Optimization of conditions for profiling bacterial populations in food by culture-independent methods
    • Cocolin L, Diez A, Urso R et al.: Optimization of conditions for profiling bacterial populations in food by culture-independent methods. Int. J. Food Microbiol. 120, 100-109 (2007).
    • (2007) Int. J. Food Microbiol. , vol.120 , pp. 100-109
    • Cocolin, L.1    Diez, A.2    Urso, R.3
  • 2
    • 33750528753 scopus 로고    scopus 로고
    • Development of a quantitative real-time PCR method to enumerate total bacterial counts in ready-to-eat fruits and vegetables
    • Takahashi H, Konuma H, Hara-Kudo Y: Development of a quantitative real-time PCR method to enumerate total bacterial counts in ready-to-eat fruits and vegetables. J. Food Prot. 69, 2504-2508 (2006).
    • (2006) J. Food Prot. , vol.69 , pp. 2504-2508
    • Takahashi, H.1    Konuma, H.2    Hara-Kudo, Y.3
  • 4
    • 68949212363 scopus 로고    scopus 로고
    • T-RFLP-based mcrA gene analysis of methanogenic archaea in association with oral infections and evidence of a novel Methanobrevibacter phylotype
    • Vianna ME, Conrads G, Gomes BP, Horz HP: T-RFLP-based mcrA gene analysis of methanogenic archaea in association with oral infections and evidence of a novel Methanobrevibacter phylotype. Oral Microbiol. Immunol. 24, 417-422 (2009).
    • (2009) Oral Microbiol. Immunol. , vol.24 , pp. 417-422
    • Vianna, M.E.1    Conrads, G.2    Gomes, B.P.3    Horz, H.P.4
  • 5
    • 33646337906 scopus 로고    scopus 로고
    • Subgingival and tongue microbiota during early periodontitis
    • Tanner AC, Paster BJ, Lu SC et al.: Subgingival and tongue microbiota during early periodontitis. J. Dent. Res. 85, 318-323 (2006).
    • (2006) J. Dent. Res. , vol.85 , pp. 318-323
    • Tanner, A.C.1    Paster, B.J.2    Lu, S.C.3
  • 6
    • 34249876626 scopus 로고    scopus 로고
    • Indigenous microflora and innate immunity of the head and neck
    • Hull MW, Chow AW: Indigenous microflora and innate immunity of the head and neck. Infect. Dis. Clin. North Am. 21, 265-282 (2007).
    • (2007) Infect. Dis. Clin. North Am. , vol.21 , pp. 265-282
    • Hull, M.W.1    Chow, A.W.2
  • 8
    • 30044441094 scopus 로고    scopus 로고
    • Limiting inflammatory responses during activation of innate immunity
    • Han J, Ulevitch RJ: Limiting inflammatory responses during activation of innate immunity. Nat. Immunol. 6, 1198-1205 (2005).
    • (2005) Nat. Immunol. , vol.6 , pp. 1198-1205
    • Han, J.1    Ulevitch, R.J.2
  • 9
    • 30044438392 scopus 로고    scopus 로고
    • Dampening inflammation
    • Henson PM: Dampening inflammation. Nat. Immunol. 6, 1179-1181 (2005).
    • (2005) Nat. Immunol. , vol.6 , pp. 1179-1181
    • Henson, P.M.1
  • 10
    • 2942620546 scopus 로고    scopus 로고
    • Therapeutic potential of oral tolerance
    • Mayer L, Shao L: Therapeutic potential of oral tolerance. Nat. Rev. Immunol. 4, 407-419 (2004).
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 407-419
    • Mayer, L.1    Shao, L.2
  • 11
    • 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: Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annu. Rev. Immunol. 22, 181-215 (2004).
    • (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
  • 12
    • 0036606951 scopus 로고    scopus 로고
    • Mammalian defensins in immunity: More than just microbicidal
    • Yang D, Biragyn A, Kwak LW, Oppenheim JJ: Mammalian defensins in immunity: more than just microbicidal. Trends Immunol. 23, 291-296 (2002).
    • (2002) Trends Immunol. , vol.23 , pp. 291-296
    • Yang, D.1    Biragyn, A.2    Kwak, L.W.3    Oppenheim, J.J.4
  • 13
    • 0034960109 scopus 로고    scopus 로고
    • The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity
    • Yang D, Chertov O, Oppenheim JJ: The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity. Cell. Mol. Life Sci. 58, 978-989. (2001).
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 978-989
    • Yang, D.1    Chertov, O.2    Oppenheim, J.J.3
  • 14
    • 65949105709 scopus 로고    scopus 로고
    • Reawakening retrocyclins: Ancestral human defensins active against HIV 1
    • Venkataraman N, Cole AL, Ruchala P et al.: Reawakening retrocyclins: ancestral human defensins active against HIV 1. PLoS Biol. 7, e95 (2009).
    • (2009) PLoS Biol. , vol.7
    • Venkataraman, N.1    Cole, A.L.2    Ruchala, P.3
  • 15
    • 34548039239 scopus 로고    scopus 로고
    • Defensins in the immunology of bacterial infections
    • Menendez A, Finlay B: Defensins in the immunology of bacterial infections. Curr. Opin. Immunol. 19, 385-391 (2007).
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 385-391
    • Menendez, A.1    Finlay, B.2
  • 16
    • 34748844591 scopus 로고    scopus 로고
    • Antimicrobial peptides: Natural effectors of the innate immune system
    • Radek K, Gallo R: Antimicrobial peptides: natural effectors of the innate immune system. Semin. Immunopathol. 29, 27-43 (2007).
    • (2007) Semin. Immunopathol. , vol.29 , pp. 27-43
    • Radek, K.1    Gallo, R.2
  • 17
    • 58149252357 scopus 로고    scopus 로고
    • Host defense peptides in the oral cavity and the lung: Similarities and differences
    • Diamond G, Beckloff N, Ryan LK: Host defense peptides in the oral cavity and the lung: similarities and differences. J. Dent. Res. 87, 915-927 (2008).
    • (2008) J. Dent. Res. , vol.87 , pp. 915-927
    • Diamond, G.1    Beckloff, N.2    Ryan, L.K.3
  • 18
    • 50249123189 scopus 로고    scopus 로고
    • Neutrophil-derived defensins as modulators of innate immune function
    • Rehaume LM, Hancock RE: Neutrophil-derived defensins as modulators of innate immune function. Crit. Rev. Immunol. 28, 185-200 (2008).
    • (2008) Crit. Rev. Immunol. , vol.28 , pp. 185-200
    • Rehaume, L.M.1    Hancock, R.E.2
  • 20
    • 20644462344 scopus 로고    scopus 로고
    • Mammalian defensins in the antimicrobial immune response
    • Selsted ME, Ouellette AJ: Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6, 551-557 (2005).
    • (2005) Nat. Immunol. , vol.6 , pp. 551-557
    • Selsted, M.E.1    Ouellette, A.J.2
  • 21
    • 2342589520 scopus 로고    scopus 로고
    • Expression of b defensins in gingival health and in periodontal disease
    • Bissell J, Joly S, Johnson GK et al.: Expression of b defensins in gingival health and in periodontal disease. J. Oral Pathol. Med. 33, 278-285 (2004).
    • (2004) J. Oral Pathol. Med. , vol.33 , pp. 278-285
    • Bissell, J.1    Joly, S.2    Johnson, G.K.3
  • 22
    • 33745851881 scopus 로고    scopus 로고
    • Cutting edge: Human b defensin 3 - A novel antagonist of the HIV 1 coreceptor CXCR4
    • Feng Z, Dubyak GR, Lederman MM, Weinberg A: Cutting edge: human b defensin 3 - a novel antagonist of the HIV 1 coreceptor CXCR4. J. Immunol. 177, 782-786 (2006).
    • (2006) J. Immunol. , vol.177 , pp. 782-786
    • Feng, Z.1    Dubyak, G.R.2    Lederman, M.M.3    Weinberg, A.4
  • 23
    • 33845401745 scopus 로고    scopus 로고
    • Human a- and b defensins block multiple steps in herpes simplex virus infection
    • Hazrati E, Galen B, Lu W et al.: Human a- and b defensins block multiple steps in herpes simplex virus infection. J. Immunol. 177, 8658-8666 (2006).
    • (2006) J. Immunol. , vol.177 , pp. 8658-8666
    • Hazrati, E.1    Galen, B.2    Lu, W.3
  • 24
    • 1542513868 scopus 로고    scopus 로고
    • Human b defensins 2 and 3 demonstrate strain-selective activity against oral microorganisms
    • Joly S, Maze C, McCray PB Jr, Guthmiller JM: Human b defensins 2 and 3 demonstrate strain-selective activity against oral microorganisms. J. Clin. Microbiol. 42, 1024-1029 (2004).
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 1024-1029
    • Joly, S.1    Maze, C.2    McCray Jr., P.B.3    Guthmiller, J.M.4
  • 25
    • 25144453335 scopus 로고    scopus 로고
    • Regulation of mammalian defensin expression by Toll-like receptor-dependent and independent signalling pathways
    • Froy O: Regulation of mammalian defensin expression by Toll-like receptor-dependent and independent signalling pathways. Cell. Microbiol. 7, 1387-1397 (2005).
    • (2005) Cell. Microbiol. , vol.7 , pp. 1387-1397
    • Froy, O.1
  • 26
    • 6344225825 scopus 로고    scopus 로고
    • β defensin-2 expression is regulated by TLR signaling in intestinal epithelial cells
    • Vora P, Youdim A, Thomas LS et al.: β defensin-2 expression is regulated by TLR signaling in intestinal epithelial cells. J. Immunol. 173, 5398-5405 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 5398-5405
    • Vora, P.1    Youdim, A.2    Thomas, L.S.3
  • 27
    • 4644249955 scopus 로고    scopus 로고
    • NF-kB- and AP-1-mediated induction of human b defensin-2 in intestinal epithelial cells by Escherichia coli Nissle 1917: A novel effect of a probiotic bacterium
    • Wehkamp J, Harder J, Wehkamp K et al.: NF-kB- and AP-1-mediated induction of human b defensin-2 in intestinal epithelial cells by Escherichia coli Nissle 1917: a novel effect of a probiotic bacterium. Infect. Immun. 72, 5750-5758 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 5750-5758
    • Wehkamp, J.1    Harder, J.2    Wehkamp, K.3
  • 28
    • 11144355933 scopus 로고    scopus 로고
    • Gangliosides act as co-receptors for Salmonella enteritidis FliC and promote FliC induction of human b defensin-2 expression in Caco-2 cells
    • Ogushi K, Wada A, Niidome T et al.: Gangliosides act as co-receptors for Salmonella enteritidis FliC and promote FliC induction of human b defensin-2 expression in Caco-2 cells. J. Biol. Chem. 279, 12213-12219 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 12213-12219
    • Ogushi, K.1    Wada, A.2    Niidome, T.3
  • 29
    • 0036136328 scopus 로고    scopus 로고
    • Regulation of human b defensin-2 in gingival epithelial cells: The involvement of mitogen-activated protein kinase pathways, but not the NF-kB transcription factor family
    • Krisanaprakornkit S, Kimball JR, Dale BA: Regulation of human b defensin-2 in gingival epithelial cells: the involvement of mitogen-activated protein kinase pathways, but not the NF-kB transcription factor family. J. Immunol. 168, 316-324 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 316-324
    • Krisanaprakornkit, S.1    Kimball, J.R.2    Dale, B.A.3
  • 30
    • 34548721076 scopus 로고    scopus 로고
    • IL-4 and IL-13 negatively regulate TNF a- and IFN g-induced b defensin expression through STAT 6, suppressor of cytokine signaling (SOCS)-1, and SOCS-3
    • Albanesi C, Fairchild HR, Madonna S et al.: IL-4 and IL-13 negatively regulate TNF a- and IFN g-induced b defensin expression through STAT 6, suppressor of cytokine signaling (SOCS)-1, and SOCS-3. J. Immunol. 179, 984-992 (2007).
    • (2007) J. Immunol. , vol.179 , pp. 984-992
    • Albanesi, C.1    Fairchild, H.R.2    Madonna, S.3
  • 31
    • 33845476244 scopus 로고    scopus 로고
    • Signal transduction and nuclear responses in Staphylococcus aureus-induced expression of human β defensin 3 in skin keratinocytes
    • Menzies BE, Kenoyer A: Signal transduction and nuclear responses in Staphylococcus aureus-induced expression of human β defensin 3 in skin keratinocytes. Infect. Immun. 74, 6847-6854 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 6847-6854
    • Menzies, B.E.1    Kenoyer, A.2
  • 32
    • 17044367481 scopus 로고    scopus 로고
    • Differential regulation of b defensin expression in human skin by microbial stimuli
    • Sorensen OE, Thapa DR, Rosenthal A, Liu L, Roberts AA, Ganz T: Differential regulation of b defensin expression in human skin by microbial stimuli. J. Immunol. 174, 4870-4879 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 4870-4879
    • Sorensen, O.E.1    Thapa, D.R.2    Rosenthal, A.3    Liu, L.4    Roberts, A.A.5    Ganz, T.6
  • 33
    • 33744965671 scopus 로고    scopus 로고
    • Nucleotide-binding oligomerization domain-1 and epidermal growth factor receptor: Critical regulators of b defensins during Helicobacter pylori infection
    • Boughan PK, Argent RH, Body-Malapel M et al.: Nucleotide-binding oligomerization domain-1 and epidermal growth factor receptor: critical regulators of b defensins during Helicobacter pylori infection. J. Biol. Chem. 281, 11637-11648 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 11637-11648
    • Boughan, P.K.1    Argent, R.H.2    Body-Malapel, M.3
  • 34
    • 0036829687 scopus 로고    scopus 로고
    • Toll-like receptor 4-dependent activation of dendritic cells by b defensin 2
    • Biragyn A, Ruffini PA, Leifer CA et al.: Toll-like receptor 4-dependent activation of dendritic cells by b defensin 2. Science 298, 1025-1029 (2002).
    • (2002) Science , vol.298 , pp. 1025-1029
    • Biragyn, A.1    Ruffini, P.A.2    Leifer, C.A.3
  • 36
    • 25644438337 scopus 로고    scopus 로고
    • Modulation of Toll-like receptor 7 and LL-37 expression in colon and breast epithelial cells by human β defensin-2
    • Stroinigg N, Srivastava MD: Modulation of Toll-like receptor 7 and LL-37 expression in colon and breast epithelial cells by human β defensin-2. Allergy Asthma Proc. 26, 299-309 (2005).
    • (2005) Allergy Asthma Proc. , vol.26 , pp. 299-309
    • Stroinigg, N.1    Srivastava, M.D.2
  • 37
    • 22544457464 scopus 로고    scopus 로고
    • The human β defensins (-1, -2, -3, -4) and cathelicidin LL-37 induce IL-18 secretion through p38 and ERK MAPK activation in primary human keratinocytes
    • Niyonsaba F, Ushio H, Nagaoka I, Okumura K, Ogawa H: The human βdefensins (-1, -2, -3, -4) and cathelicidin LL-37 induce IL-18 secretion through p38 and ERK MAPK activation in primary human keratinocytes. J. Immunol. 175, 1776-1784 (2005).
    • (2005) J. Immunol. , vol.175 , pp. 1776-1784
    • Niyonsaba, F.1    Ushio, H.2    Nagaoka, I.3    Okumura, K.4    Ogawa, H.5
  • 38
    • 34548810954 scopus 로고    scopus 로고
    • A novel role for defensins in intestinal homeostasis: Regulation of IL-1b secretion.
    • Shi J, Aono S, Lu W et al.: A novel role for defensins in intestinal homeostasis: regulation of IL-1b secretion. J. Immunol. 179, 1245-1253 (2007).
    • (2007) J. Immunol. , vol.179 , pp. 1245-1253
    • Shi, J.1    Aono, S.2    Lu, W.3
  • 39
    • 68149125185 scopus 로고    scopus 로고
    • Dying and necrotic neutrophils are anti-inflammatory secondary to the release of a defensins
    • Miles K, Clarke DJ, Lu W et al.: Dying and necrotic neutrophils are anti-inflammatory secondary to the release of a defensins. J. Immunol. 183, 2122-2132 (2009).
    • (2009) J. Immunol. , vol.183 , pp. 2122-2132
    • Miles, K.1    Clarke, D.J.2    Lu, W.3
  • 40
    • 56249122900 scopus 로고    scopus 로고
    • Human β 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 et al.: Human b 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).
    • (2008) Immunol. Cell Biol. , vol.86 , pp. 643-649
    • Pingel, L.C.1    Kohlgraf, K.G.2    Hansen, C.J.3
  • 41
    • 13844308074 scopus 로고    scopus 로고
    • Defensins - Non-antibiotic use for vaccine development
    • Biragyn A: Defensins - non-antibiotic use for vaccine development. Curr. Protein Pept. Sci. 6, 53-60 (2005).
    • (2005) Curr. Protein Pept. Sci. , vol.6 , pp. 53-60
    • Biragyn, A.1
  • 42
    • 33749006591 scopus 로고    scopus 로고
    • The human b defensin-3, an antibacterial peptide with multiple biological functions
    • Dhople V, Krukemeyer A, Ramamoorthy A: The human b defensin-3, an antibacterial peptide with multiple biological functions. Biochim. Biophys. Acta 1758, 1499-1512 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1499-1512
    • Dhople, V.1    Krukemeyer, A.2    Ramamoorthy, A.3
  • 43
    • 33646380105 scopus 로고    scopus 로고
    • Lipid-specific membrane activity of human β defensin-3
    • Bohling A, Hagge SO, Roes S et al.: Lipid-specific membrane activity of human β defensin-3. Biochemistry (Mosc.) 45, 5663-5670 (2006).
    • (2006) Biochemistry (Mosc. , vol.45 , pp. 5663-5670
    • Bohling, A.1    Hagge, S.O.2    Roes, S.3
  • 44
    • 57349161186 scopus 로고    scopus 로고
    • Human a- And b defensins bind to immobilized adhesins from Porphyromonas gingivalis
    • Dietrich DE, Xiao X, Dawson DV et al.: Human a- and b defensins bind to immobilized adhesins from Porphyromonas gingivalis. Infect. Immun. 76, 5714-5720 (2008).
    • (2008) Infect. Immun. , vol.76 , pp. 5714-5720
    • Dietrich, D.E.1    Xiao, X.2    Dawson, D.V.3
  • 45
    • 33845682462 scopus 로고    scopus 로고
    • The novel β defensin DEFB123 prevents lipopolysaccharide-mediated effects in vitro and in vivo
    • Motzkus D, Schulz-Maronde S, Heitland A et al.: The novel b defensin DEFB123 prevents lipopolysaccharide-mediated effects in vitro and in vivo. FASEB J. 20, 1701-1702 (2006).
    • (2006) FASEB J. , vol.20 , pp. 1701-1702
    • Motzkus, D.1    Schulz-Maronde, S.2    Heitland, A.3
  • 46
    • 44649117522 scopus 로고    scopus 로고
    • Human a defensins inhibit Clostridium difficile toxin B
    • Giesemann T, Guttenberg G, Aktories K: Human a defensins inhibit Clostridium difficile toxin B. Gastroenterology 134, 2049-2058 (2008).
    • (2008) Gastroenterology , vol.134 , pp. 2049-2058
    • Giesemann, T.1    Guttenberg, G.2    Aktories, K.3
  • 48
    • 33749989623 scopus 로고    scopus 로고
    • Human a defensins neutralize toxins of the mono-ADP-ribosyltransferase family
    • Kim C, Slavinskaya Z, Merrill AR, Kaufmann SH: Human a defensins neutralize toxins of the mono-ADP-ribosyltransferase family. Biochem. J. 399, 225-229 (2006).
    • (2006) Biochem. J. , vol.399 , pp. 225-229
    • Kim, C.1    Slavinskaya, Z.2    Merrill, A.R.3    Kaufmann, S.H.4
  • 49
    • 33845354241 scopus 로고    scopus 로고
    • Retrocyclins kill bacilli and germinating spores of Bacillus anthracis and inactivate anthrax lethal toxin
    • Wang W, Mulakala C, Ward SC et al.: Retrocyclins kill bacilli and germinating spores of Bacillus anthracis and inactivate anthrax lethal toxin. J. Biol. Chem. 281, 32755-32764 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 32755-32764
    • Wang, W.1    Mulakala, C.2    Ward, S.C.3
  • 50
  • 51
    • 9344221638 scopus 로고    scopus 로고
    • RC-101, a retrocyclin-1 analogue with enhanced activity against primary HIV type 1 isolates
    • Owen SM, Rudolph DL, Wang W et al.: RC-101, a retrocyclin-1 analogue with enhanced activity against primary HIV type 1 isolates. AIDS Res. Hum. Retroviruses 20, 1157-1165 (2004).
    • (2004) AIDS Res. Hum. Retroviruses , vol.20 , pp. 1157-1165
    • Owen, S.M.1    Rudolph, D.L.2    Wang, W.3
  • 52
    • 3042640897 scopus 로고    scopus 로고
    • A θ defensin composed exclusively of d-amino acids is active against HIV 1
    • Owen SM, Rudolph D, Wang W et al.: A θ defensin composed exclusively of d-amino acids is active against HIV 1. J. Pept. Res. 63, 469-476 (2004).
    • (2004) J. Pept. Res. , vol.63 , pp. 469-476
    • Owen, S.M.1    Rudolph, D.2    Wang, W.3
  • 53
    • 33745691892 scopus 로고    scopus 로고
    • θ defensins prevent HIV 1 Env-mediated fusion by binding gp41 and blocking 6-helix bundle formation
    • Gallo SA, Wang W, Rawat SS et al.: θ defensins prevent HIV 1 Env-mediated fusion by binding gp41 and blocking 6-helix bundle formation. J. Biol. Chem. 281, 18787-18792 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 18787-18792
    • Gallo, S.A.1    Wang, W.2    Rawat, S.S.3
  • 55
    • 75849123960 scopus 로고    scopus 로고
    • HBD3 inhibits Porphyromonas gingivalis Hemagglutinin B binding to dendritic cells
    • Presented at, Miami Beach Convention Center, FL, USA, 1-4 April
    • Dietrich DE, Belanger M, Progluske-Fox A, Kurago Z, Brogden KA: HBD3 inhibits Porphyromonas gingivalis Hemagglutinin B binding to dendritic cells. Presented at: 87th General Session IADR/AADR/CADR. Miami Beach Convention Center, FL, USA, 1-4 April 2009.
    • (2009) 87th General Session IADR/AADR/CADR
    • Dietrich, D.E.1    Belanger, M.2    Progluske-Fox, A.3    Kurago, Z.4    Brogden, K.A.5
  • 56
    • 75849130132 scopus 로고    scopus 로고
    • Defensins attenuate cytokine responses yet enhance antibody responses to Porphyromonas gingivalis adhesins in mice
    • Kohlgraf KG, Ackermann A, Lu X et al.: Defensins attenuate cytokine responses yet enhance antibody responses to Porphyromonas gingivalis adhesins in mice. Future Microbiol. 5(1), 115-125 (2010).
    • (2010) Future Microbiol. , vol.5 , Issue.1 , pp. 115-125
    • Kohlgraf, K.G.1    Ackermann, A.2    Lu, X.3
  • 58
    • 75849162647 scopus 로고    scopus 로고
    • Antimicrobial peptides as mucosal adjuvants
    • Brogden KA, Stanton TB, Cornick N et al. (Eds). ASM Press, DC, USA
    • Pingel L, Lu X, Brogden KA: Antimicrobial peptides as mucosal adjuvants. In: Virulence Mechanisms of Bacterial Pathogens. Brogden KA, Stanton TB, Cornick N et al. (Eds). ASM Press, DC, USA, 281-295 (2007).
    • (2007) Virulence Mechanisms of Bacterial Pathogens , pp. 281-295
    • Pingel, L.1    Lu, X.2    Brogden, K.A.3
  • 59
    • 34250331531 scopus 로고    scopus 로고
    • The perfect mix: Recent progress in adjuvant research
    • Guy B: The perfect mix: recent progress in adjuvant research. Nat. Rev. Microbiol. 5, 505-517 (2007).
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 505-517
    • Guy, B.1
  • 60
    • 33645228369 scopus 로고    scopus 로고
    • The use of soluble polymers and polymer microparticles to provide improved vaccine responses after parenteral and mucosal delivery
    • Davis SS: The use of soluble polymers and polymer microparticles to provide improved vaccine responses after parenteral and mucosal delivery. Vaccine 24(Suppl. 2), S2-S10 (2006).
    • (2006) Vaccine , vol.24 , Issue.SUPPL. 2
    • Davis, S.S.1
  • 61
    • 33645225168 scopus 로고    scopus 로고
    • The use of oil adjuvants in therapeutic vaccines
    • Aucouturier J, Ascarateil S, Dupuis L: The use of oil adjuvants in therapeutic vaccines. Vaccine 24(Suppl. 2), S2-S45 (2006).
    • (2006) Vaccine , vol.24 , Issue.SUPPL. 2
    • Aucouturier, J.1    Ascarateil, S.2    Dupuis, L.3
  • 64
    • 33745221673 scopus 로고    scopus 로고
    • Of mice, men, and elephants: Mycobacterium tuberculosis cell envelope lipids and pathogenesis
    • Riley LW: Of mice, men, and elephants: Mycobacterium tuberculosis cell envelope lipids and pathogenesis. J. Clin. Invest. 116, 1475-1478 (2006).
    • (2006) J. Clin. Invest. , vol.116 , pp. 1475-1478
    • Riley, L.W.1
  • 66
  • 67
    • 11144302533 scopus 로고    scopus 로고
    • γ interferon and monophosphoryl lipid A-trehalose dicorynomycolate are efficient adjuvants for Mycobacterium tuberculosis multivalent acellular vaccine
    • Hovav AH, Fishman Y, Bercovier H: γ interferon and monophosphoryl lipid A-trehalose dicorynomycolate are efficient adjuvants for Mycobacterium tuberculosis multivalent acellular vaccine. Infect. Immun. 73, 250-257 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 250-257
    • Hovav, A.H.1    Fishman, Y.2    Bercovier, H.3
  • 68
    • 33645215961 scopus 로고    scopus 로고
    • Co-stimulatory agonists as immunological adjuvants
    • Barr TA, Carlring J, Heath AW: Co-stimulatory agonists as immunological adjuvants. Vaccine 24, 3399-3407 (2006).
    • (2006) Vaccine , vol.24 , pp. 3399-3407
    • Barr, T.A.1    Carlring, J.2    Heath, A.W.3
  • 70
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown KL, Hancock RE: Cationic host defense (antimicrobial) peptides. Curr. Opin. Immunol. 18, 24-30 (2006).
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 71
    • 0036947672 scopus 로고    scopus 로고
    • Lactoferrin and immunologic dissonance: Clinical implications
    • Kruzel ML, Zimecki M: Lactoferrin and immunologic dissonance: clinical implications. Arch. Immunol. Ther. Exp. (Warsz.) 50, 399-410 (2002).
    • (2002) Arch. Immunol. Ther. Exp. (Warsz. , vol.50 , pp. 399-410
    • Kruzel, M.L.1    Zimecki, M.2
  • 72
    • 33750183408 scopus 로고    scopus 로고
    • A complex of lactoferrin with monophosphoryl lipid A is an efficient adjuvant of the humoral and cellular immune response in mice
    • Chodaczek G, Zimecki M, Lukasiewicz J, Lugowski C: A complex of lactoferrin with monophosphoryl lipid A is an efficient adjuvant of the humoral and cellular immune response in mice. Med. Microbiol. Immunol. (Berl.) 195, 207-216 (2006).
    • (2006) Med. Microbiol. Immunol. (Berl. , vol.195 , pp. 207-216
    • Chodaczek, G.1    Zimecki, M.2    Lukasiewicz, J.3    Lugowski, C.4
  • 73
    • 18644363054 scopus 로고    scopus 로고
    • Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant
    • Kurosaka K, Chen Q, Yarovinsky F, Oppenheim JJ, Yang D: Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant. J. Immunol. 174, 6257-6265 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 6257-6265
    • Kurosaka, K.1    Chen, Q.2    Yarovinsky, F.3    Oppenheim, J.J.4    Yang, D.5
  • 74
    • 1942475289 scopus 로고    scopus 로고
    • Adjuvant action of melittin following intranasal immunisation with tetanus and diphtheria toxoids.
    • Bramwell VW, Somavarapu S, Outschoorn I, Alpar HO: Adjuvant action of melittin following intranasal immunisation with tetanus and diphtheria toxoids. J. Drug Target. 11, 525-530 (2003).
    • (2003) J. Drug Target. , vol.11 , pp. 525-530
    • Bramwell, V.W.1    Somavarapu, S.2    Outschoorn, I.3    Alpar, H.O.4
  • 75
    • 4043049496 scopus 로고    scopus 로고
    • The artificial antimicrobial peptide KLKLLLLLKLK induces predominantly a TH2-type immune response to co-injected antigens
    • Fritz JH, Brunner S, Birnstiel ML et al.: The artificial antimicrobial peptide KLKLLLLLKLK induces predominantly a TH2-type immune response to co-injected antigens. Vaccine 22, 3274-3284 (2004).
    • (2004) Vaccine , vol.22 , pp. 3274-3284
    • Fritz, J.H.1    Brunner, S.2    Birnstiel, M.L.3
  • 76
    • 14744273623 scopus 로고    scopus 로고
    • LL-37 enhances adaptive antitumor immune response in a murine model when genetically fused with M-CSFR (J6-1) DNA vaccine
    • An LL, Yang YH, Ma XT et al.: LL-37 enhances adaptive antitumor immune response in a murine model when genetically fused with M-CSFR (J6-1) DNA vaccine. Leuk. Res. 29, 535-543 (2005).
    • (2005) Leuk. Res. , vol.29 , pp. 535-543
    • An, L.L.1    Yang, Y.H.2    Ma, X.T.3
  • 77
    • 0035576242 scopus 로고    scopus 로고
    • Mediators of innate immunity that target immature, but not mature, dendritic cells induce antitumor immunity when genetically fused with nonimmunogenic tumor antigens
    • Biragyn A, Surenhu M, Yang D et al.: Mediators of innate immunity that target immature, but not mature, dendritic cells induce antitumor immunity when genetically fused with nonimmunogenic tumor antigens. J. Immunol. 167, 6644-6653 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 6644-6653
    • Biragyn, A.1    Surenhu, M.2    Yang, D.3
  • 78
    • 0034061579 scopus 로고    scopus 로고
    • Defensins act as potent adjuvants that promote cellular and humoral immune responses in mice to a lymphoma idiotype and carrier antigens
    • Tani K, Murphy WJ, Chertov O et al.: Defensins act as potent adjuvants that promote cellular and humoral immune responses in mice to a lymphoma idiotype and carrier antigens. Int. Immunol. 12, 691-700 (2000).
    • (2000) Int. Immunol. , vol.12 , pp. 691-700
    • Tani, K.1    Murphy, W.J.2    Chertov, O.3
  • 79
    • 31544445750 scopus 로고    scopus 로고
    • An LL et al.: Vaccine with b defensin 2-transduced leukemic cells activates innate and adaptive immunity to elicit potent antileukemia responses
    • Ma XT, Xu B, An LL et al.: Vaccine with b defensin 2-transduced leukemic cells activates innate and adaptive immunity to elicit potent antileukemia responses. Cancer Res. 66, 1169-1176 (2006).
    • (2006) Cancer Res. , vol.66 , pp. 1169-1176
    • Ma, X.T.1    Xu, B.2
  • 81
    • 0037911520 scopus 로고    scopus 로고
    • Defensin-induced adaptive immunity in mice and its potential in preventing periodontal disease
    • Brogden KA, Heidari M, Sacco RE et al.: Defensin-induced adaptive immunity in mice and its potential in preventing periodontal disease. Oral Microbiol. Immunol. 18, 95-99 (2003).
    • (2003) Oral Microbiol. Immunol. , vol.18 , pp. 95-99
    • Brogden, K.A.1    Heidari, M.2    Sacco, R.E.3
  • 82
    • 0037911520 scopus 로고    scopus 로고
    • Defensin-induced adaptive immunity in mice and its potential in preventing periodontal disease
    • Brogden KA, Heidari M, Sacco RE et al.: Defensin-induced adaptive immunity in mice and its potential in preventing periodontal disease. Oral Microbiol. Immunol. 18, 95-99 (2003).
    • (2003) Oral Microbiol. Immunol. , vol.18 , pp. 95-99
    • Brogden, K.A.1    Heidari, M.2    Sacco, R.E.3
  • 83
    • 29144483937 scopus 로고    scopus 로고
    • Reduced Paneth cell a defensins in ileal Crohn's disease
    • USA
    • Wehkamp J, Salzman NH, Porter E et al.: Reduced Paneth cell a defensins in ileal Crohn's disease. Proc. Natl Acad. Sci. USA 102, 18129-18134 (2005).
    • (2005) Proc. Natl Acad. Sci. , vol.102 , pp. 18129-18134
    • Wehkamp, J.1    Salzman, N.H.2    Porter, E.3
  • 84
    • 70350454810 scopus 로고    scopus 로고
    • Susceptibility to infectious diseases based on antimicrobial peptide production
    • Rivas-Santiago B, Serrano CJ, Enciso Moreno JA: Susceptibility to infectious diseases based on antimicrobial peptide production. Infect. Immun. 77, 4690-4695 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 4690-4695
    • Rivas-Santiago, B.1    Serrano, C.J.2    Enciso Moreno, J.A.3
  • 85
    • 26444577882 scopus 로고    scopus 로고
    • Copy number polymorphism and expression level variation of the human a defensin genes
    • Aldred PM, Hollox EJ, Armour JA: Copy number polymorphism and expression level variation of the human a defensin genes DEFA1 and DEFA3. Hum. Mol. Genet. 14, 2045-2052 (2005).
    • (2005) DEFA1 and DEFA3. Hum. Mol. Genet. , vol.14 , pp. 2045-2052
    • Aldred, P.M.1    Hollox, E.J.2    Armour, J.A.3
  • 86
    • 16844382886 scopus 로고    scopus 로고
    • Defensin deficiency, intestinal microbes, and the clinical phenotypes of Crohn's disease
    • Wehkamp J, Schmid M, Fellermann K, Stange EF: Defensin deficiency, intestinal microbes, and the clinical phenotypes of Crohn's disease. J. Leukoc. Biol. 77, 460-465 (2005).
    • (2005) J. Leukoc. Biol. , vol.77 , pp. 460-465
    • Wehkamp, J.1    Schmid, M.2    Fellermann, K.3    Stange, E.F.4
  • 87
    • 0344505756 scopus 로고    scopus 로고
    • Polymorphisms of the human β defensin-1 gene
    • Dork T, Stuhrmann M: Polymorphisms of the human β defensin-1 gene. Mol. Cell. Probes 12, 171-173 (1998).
    • (1998) Mol. Cell. Probes , vol.12 , pp. 171-173
    • Dork, T.1    Stuhrmann, M.2
  • 88
    • 29144457296 scopus 로고    scopus 로고
    • Human defensin gene copy number polymorphisms: Comprehensive analysis of independent variation in a- And β defensin regions at 8p22-p23
    • Linzmeier RM, Ganz T: Human defensin gene copy number polymorphisms: comprehensive analysis of independent variation in a- and β defensin regions at 8p22-p23. Genomics 86, 423-430 (2005).
    • (2005) Genomics , vol.86 , pp. 423-430
    • Linzmeier, R.M.1    Ganz, T.2
  • 90
    • 3242723228 scopus 로고    scopus 로고
    • Novel hairpin-shaped primer assay to study the association of the -44 single-nucleotide polymorphism of the DEFB1 gene with early-onset periodontal disease
    • Boniotto M, Hazbon MH, Jordan WJ et al.: Novel hairpin-shaped primer assay to study the association of the -44 single-nucleotide polymorphism of the DEFB1 gene with early-onset periodontal disease. Clin. Diagn. Lab. Immunol. 11, 766-769 (2004).
    • (2004) Clin. Diagn. Lab. Immunol. , vol.11 , pp. 766-769
    • Boniotto, M.1    Hazbon, M.H.2    Jordan, W.J.3
  • 91
    • 20144389041 scopus 로고    scopus 로고
    • Distribution of human β defensin polymorphisms in various control and cystic fibrosis populations
    • Vankeerberghen A, Scudiero O, De Boeck K et al.: Distribution of human β defensin polymorphisms in various control and cystic fibrosis populations. Genomics 85, 574-581 (2005).
    • (2005) Genomics , vol.85 , pp. 574-581
    • Vankeerberghen, A.1    Scudiero, O.2    De Boeck, K.3
  • 92
    • 30844472619 scopus 로고    scopus 로고
    • Screening of copy number polymorphisms in human β defensin genes using modified real-time quantitative PCR
    • Chen Q, Book M, Fang X, Hoeft A, Stuber F: Screening of copy number polymorphisms in human β defensin genes using modified real-time quantitative PCR. J. Immunol. Methods 308, 231-240 (2006).
    • (2006) J. Immunol. Methods , vol.308 , pp. 231-240
    • Chen, Q.1    Book, M.2    Fang, X.3    Hoeft, A.4    Stuber, F.5
  • 93
    • 58149187882 scopus 로고    scopus 로고
    • APD2: The updated antimicrobial peptide database and its application in peptide design
    • Wang G, Li X, Wang Z: APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 37, D933-D937 (2009).
    • (2009) Nucleic Acids Res. , vol.37
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 94
    • 0347755460 scopus 로고    scopus 로고
    • APD: The antimicrobial peptide database
    • Wang Z, Wang G: APD: the antimicrobial peptide database. Nucleic Acids Res. 32, D590-D592 (2004).
    • (2004) Nucleic Acids Res. , vol.32
    • Wang, Z.1    Wang, G.2
  • 95
    • 0031662487 scopus 로고    scopus 로고
    • Expression of the peptide antibiotic human β defensin 1 in cultured gingival epithelial cells and gingival tissue
    • Krisanaprakornkit S, Weinberg A, Perez CN, Dale BA: Expression of the peptide antibiotic human β defensin 1 in cultured gingival epithelial cells and gingival tissue. Infect. Immun. 66, 4222-4228 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 4222-4228
    • Krisanaprakornkit, S.1    Weinberg, A.2    Perez, C.N.3    Dale, B.A.4
  • 96
  • 98
    • 0042371615 scopus 로고    scopus 로고
    • Localization of human β defensin 3 mRNA in normal oral epithelium, leukoplakia, and lichen planus: An in situ hybridization study
    • Nishimura M, Abiko Y, Kusano K et al.: Localization of human b defensin 3 mRNA in normal oral epithelium, leukoplakia, and lichen planus: an in situ hybridization study. Med. Electron. Microsc. 36, 94-97 (2003).
    • (2003) Med. Electron. Microsc. , vol.36 , pp. 94-97
    • Nishimura, M.1    Abiko, Y.2    Kusano, K.3
  • 99
    • 0344483901 scopus 로고    scopus 로고
    • Production of β defensin antimicrobial peptides by the oral mucosa and salivary glands
    • Mathews M, Jia HP, Guthmiller JM et al.: Production of b defensin antimicrobial peptides by the oral mucosa and salivary glands. Infect. Immun. 67, 2740-2745 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 2740-2745
    • Mathews, M.1    Jia, H.P.2    Guthmiller, J.M.3
  • 101
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human β defensin-3, a novel human inducible peptide antibiotic
    • Harder J, Bartels J, Christophers E, Schroder JM: Isolation and characterization of human b defensin-3, a novel human inducible peptide antibiotic. J. Biol. Chem. 276, 5707-5713 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schroder, J.M.4
  • 103
    • 0042672616 scopus 로고    scopus 로고
    • Human b defensins and Toll-like receptors in the upper airway
    • Claeys S, de Belder T, Holtappels G et al.: Human b defensins and Toll-like receptors in the upper airway. Allergy 58, 748-753 (2003).
    • (2003) Allergy , vol.58 , pp. 748-753
    • Claeys, S.1    De Belder, T.2    Holtappels, G.3
  • 104
    • 0036320726 scopus 로고    scopus 로고
    • The human false vocal folds - An analysis of antimicrobial defense mechanisms
    • Kutta H, Steven P, Kohla G, Tillmann B, Paulsen F: The human false vocal folds - an analysis of antimicrobial defense mechanisms. Anat. Embryol. (Berl.) 205, 315-323 (2002).
    • (2002) Anat. Embryol. (Berl. , vol.205 , pp. 315-323
    • Kutta, H.1    Steven, P.2    Kohla, G.3    Tillmann, B.4    Paulsen, F.5
  • 105
    • 54149110348 scopus 로고    scopus 로고
    • Nuclear hBD-1 accumulation in malignant salivary gland tumours
    • Wenghoefer M, Pantelis A, Dommisch H et al.: Nuclear hBD-1 accumulation in malignant salivary gland tumours. BMC Cancer 8, 290 (2008).
    • (2008) BMC Cancer , vol.8 , pp. 290
    • Wenghoefer, M.1    Pantelis, A.2    Dommisch, H.3
  • 107
    • 0141918814 scopus 로고    scopus 로고
    • Antimicrobial peptides in defence of the oral and respiratory tracts
    • Devine DA: Antimicrobial peptides in defence of the oral and respiratory tracts. Mol. Immunol. 40, 431-443 (2003).
    • (2003) Mol. Immunol. , vol.40 , pp. 431-443
    • Devine, D.A.1
  • 109
    • 34147222846 scopus 로고    scopus 로고
    • Quantification of human β defensin-2 and -3 in body fluids: Application for studies of innate immunity
    • Ghosh SK, Gerken TA, Schneider KM, Feng Z, McCormick TS, Weinberg A: Quantification of human β defensin-2 and -3 in body fluids: application for studies of innate immunity. Clin. Chem. 53, 757-765 (2007).
    • (2007) Clin. Chem. , vol.53 , pp. 757-765
    • Ghosh, S.K.1    Gerken, T.A.2    Schneider, K.M.3    Feng, Z.4    McCormick, T.S.5    Weinberg, A.6
  • 110
    • 69149102398 scopus 로고    scopus 로고
    • Antimicrobial peptides of the oral cavity
    • Gorr SU: Antimicrobial peptides of the oral cavity. Periodontol. 2000 51, 152-180 (2009).
    • (2000) Periodontol , vol.51 , pp. 152-180
    • Gorr, S.U.1
  • 111
    • 0032407465 scopus 로고    scopus 로고
    • Defensin-1, a peptide detected in the saliva of oral squamous cell carcinoma patients
    • Mizukawa N, Sugiyama K, Fukunaga J et al.: Defensin-1, a peptide detected in the saliva of oral squamous cell carcinoma patients. Anticancer Res. 18, 4645-4649 (1998).
    • (1998) Anticancer Res. , vol.18 , pp. 4645-4649
    • Mizukawa, N.1    Sugiyama, K.2    Fukunaga, J.3
  • 112
    • 28944451656 scopus 로고    scopus 로고
    • Peptides of human gingival crevicular fluid determined by HPLC-ESI-MS
    • Pisano E, Cabras T, Montaldo C et al.: Peptides of human gingival crevicular fluid determined by HPLC-ESI-MS. Eur. J. Oral Sci. 113, 462-468 (2005).
    • (2005) Eur. J. Oral Sci. , vol.113 , pp. 462-468
    • Pisano, E.1    Cabras, T.2    Montaldo, C.3
  • 113
    • 24144432828 scopus 로고    scopus 로고
    • Salivary antimicrobial peptide expression and dental caries experience in children
    • Tao R, Jurevic RJ, Coulton KK et al.: Salivary antimicrobial peptide expression and dental caries experience in children. Antimicrob. Agents Chemother. 49, 3883-3888 (2005).
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3883-3888
    • Tao, R.1    Jurevic, R.J.2    Coulton, K.K.3
  • 115
    • 45149091570 scopus 로고    scopus 로고
    • Analysis of neutrophil-derived antimicrobial peptides in gingival crevicular fluid suggests importance of cathelicidin LL-37 in the innate immune response against periodontogenic bacteria
    • Puklo M, Guentsch A, Hiemstra PS, Eick S, Potempa J: Analysis of neutrophil-derived antimicrobial peptides in gingival crevicular fluid suggests importance of cathelicidin LL-37 in the innate immune response against periodontogenic bacteria. Oral Microbiol. Immunol. 23, 328-335 (2008).
    • (2008) Oral Microbiol. Immunol. , vol.23 , pp. 328-335
    • Puklo, M.1    Guentsch, A.2    Hiemstra, P.S.3    Eick, S.4    Potempa, J.5
  • 116
    • 0032968506 scopus 로고    scopus 로고
    • Innate antimicrobial activity of nasal secretions
    • Cole AM, Dewan P, Ganz T: Innate antimicrobial activity of nasal secretions. Infect. Immun. 67, 3267-3275 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 3267-3275
    • Cole, A.M.1    Dewan, P.2    Ganz, T.3
  • 117
    • 67349133120 scopus 로고    scopus 로고
    • Discovery of Anas platyrhynchos avian β defensin 2 (Apl-AvBD2) with antibacterial and chemotactic functions
    • Soman SS, Arathy DS, Sreekumar E: Discovery of Anas platyrhynchos avian β defensin 2 (Apl-AvBD2) with antibacterial and chemotactic functions. Mol. Immunol. 46, 2029-2038 (2009).
    • (2009) Mol. Immunol. , vol.46 , pp. 2029-2038
    • Soman, S.S.1    Arathy, D.S.2    Sreekumar, E.3
  • 118
    • 68749109270 scopus 로고    scopus 로고
    • Immunomodulation by duck defensin, Apl-AvBD2: In vitro dendritic cell immunoreceptor (DCIR) mRNA suppression, and B- and T-lymphocyte chemotaxis
    • Soman SS, Nair S, Issac A et al.: Immunomodulation by duck defensin, Apl-AvBD2: in vitro dendritic cell immunoreceptor (DCIR) mRNA suppression, and B- and T-lymphocyte chemotaxis. Mol. Immunol. 46(15) 3070-3075 (2009).
    • (2009) Mol. Immunol. , vol.46 , Issue.15 , pp. 3070-3075
    • Soman, S.S.1    Nair, S.2    Issac, A.3


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