Cationic host defense peptides; novel antimicrobial therapeutics against Category A pathogens and emerging infections

References

• Zasloff M. Antimicrobial peptides of multicellular organisms. Nature. 2002;415(6870):389–395.10.1038/415389a
   PubMed Web of Science ®Google Scholar
• Doss M, White MR, Tecle T, Hartshorn KL. Human defensins and LL-37 in mucosal immunity. J Leukoc Biol. 2010;87(1):79–92.10.1189/jlb.0609382
   PubMed Web of Science ®Google Scholar
• De Y, Chen Q, Schmidt AP, Anderson GM, Wang JM, Wooters J, et al. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J Exp Med. 2000;192(7):1069–1074.
   PubMed Web of Science ®Google Scholar
• Dorschner RA, Pestonjamasp VK, Tamakuwala S, Ohtake T, Rudisill J, Nizet V, et al. Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A streptococcus. J Invest Dermatol. 2001;117(1):91–97.10.1046/j.1523-1747.2001.01340.x
   PubMed Web of Science ®Google Scholar
• Koczulla R, von Degenfeld G, Kupatt C, Krötz F, Zahler S, Gloe T, et al. An angiogenic role for the human peptide antibiotic LL-37/hCAP-18. J Clin Invest. 2003;111(11):1665–1672.10.1172/JCI17545
   PubMed Web of Science ®Google Scholar
• Davidson DJ, Currie AJ, Reid GS, Bowdish DM, MacDonald KL, Ma RC, et al. The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization. J Immunol. 2004;172(2):1146–1156.10.4049/jimmunol.172.2.1146
   PubMed Web of Science ®Google Scholar
• Barlow PG, Beaumont PE, Cosseau C, Mackellar A, Wilkinson TS, Hancock RE, et al. The human cathelicidin LL-37 preferentially promotes apoptosis of infected airway epithelium. Am J Respir Cell Mol Biol. 2010;43(6):692–702.10.1165/rcmb.2009-0250OC
   PubMed Web of Science ®Google Scholar
• Barlow PG, Li Y, Wilkinson TS, Bowdish DM, Lau YE, Cosseau C, et al. The human cationic host defense peptide LL-37 mediates contrasting effects on apoptotic pathways in different primary cells of the innate immune system. J Leukoc Biol. 2006;80(3):509–520.10.1189/jlb.1005560
   PubMed Web of Science ®Google Scholar
• Li HN, Barlow PG, Bylund J, Mackellar A, Bjorstad A, Conlon J, et al. Secondary necrosis of apoptotic neutrophils induced by the human cathelicidin LL-37 is not proinflammatory to phagocytosing macrophages. J Leukoc Biol. 2009;86(4):891–902.10.1189/jlb.0209050
   PubMed Web of Science ®Google Scholar
• Nizet V, Gallo RL. Cathelicidins and innate defense against invasive bacterial infection. Scand J Infect Dis. 2003;35(9):670–676.10.1080/00365540310015629
   PubMed Web of Science ®Google Scholar
• Auvynet C, Rosenstein Y. Multifunctional host defense peptides: antimicrobial peptides, the small yet big players in innate and adaptive immunity. FEBS J. 2009;276(22):6497–6508.10.1111/j.1742-4658.2009.07360.x
   PubMed Web of Science ®Google Scholar
• Lenarc̆ic̆ B, Ritonja A, Dolenc I, Stoka V, Berbic̆ S, Pungerc̆ar J, et al. Pig leukocyte cysteine proteinase inhibitor (PLCPI), a new member of the stefin family. FEBS Lett. 1993;336(2):289–292.10.1016/0014-5793(93)80822-C
   PubMed Web of Science ®Google Scholar
• Duplantier AJ, van Hoek ML. The human cathelicidin antimicrobial peptide LL-37 as a potential treatment for polymicrobial infected wounds. Front Immunol. 2013;4:1–14. Available from: http://www.ncbi.nlm.nih.gov/pubmed/23840194.
   PubMed Web of Science ®Google Scholar
• 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. 2001;58(7):978–989.10.1007/PL00000914
   PubMed Web of Science ®Google Scholar
• Brogden KA, Ackermann M, McCray PB, Tack BF. Antimicrobial peptides in animals and their role in host defences. Int J Antimicrob Agents. 2003;22(5):465–478.10.1016/S0924-8579(03)00180-8
   PubMed Web of Science ®Google Scholar
• Kokryakov VN, Harwig SS, Panyutich EA, Shevchenko AA, Aleshina GM, Shamova OV, et al. Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett. 1993;327(2):231–236.10.1016/0014-5793(93)80175-T
   PubMed Web of Science ®Google Scholar
• 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. 1998;421(3):263–267.10.1016/S0014-5793(97)01579-2
   PubMed Web of Science ®Google Scholar
• Sørensen O, Arnljots K, Cowland JB, Bainton DF, Borregaard N. The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils. Blood. 1997;90(7):2796–2803.
   PubMed Web of Science ®Google Scholar
• Gudmundsson GH, Agerberth B, Odeberg J, Bergman T, Olsson B, Salcedo R. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur J Biochem. 1996;238(2):325–332.10.1111/ejb.1996.238.issue-2
   PubMedGoogle Scholar
• Nijnik A, Hancock RE. The roles of cathelicidin LL-37 in immune defences and novel clinical applications. Curr Opin Hematol. 2009;16(1):41–47.10.1097/MOH.0b013e32831ac517
   PubMed Web of Science ®Google Scholar
• Bals R, Hiemstra PS. Innate immunity in the lung: how epithelial cells fight against respiratory pathogens. Eur Respir J. 2004;23(2):327–333.10.1183/09031936.03.00098803
   PubMed Web of Science ®Google Scholar
• Bowdish DM, Davidson DJ, Hancock RE. Immunomodulatory properties of defensins and cathelicidins. Curr Top Microbiol Immunol. 2006;306:27–66.
   PubMed Web of Science ®Google Scholar
• Frohm M, Agerberth B, Ahangari G, Stahle-Backdahl M, Liden S, Wigzell H, et al. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J Biol Chem. 1997;272(24):15258–15263.10.1074/jbc.272.24.15258
   PubMed Web of Science ®Google Scholar
• Agerberth B, Charo J, Werr J, Olsson B, Idali F, Lindbom L, et al. The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations. Blood. 2000;96(9):3086–3093.
   PubMed Web of Science ®Google Scholar
• Larrick JW, Lee J, Ma S, Li X, Francke U, Wright SC, et al. Structural, functional analysis and localization of the human CAP18 gene. FEBS Lett. 1996;398(1):74–80.10.1016/S0014-5793(96)01199-4
   PubMed Web of Science ®Google Scholar
• Bergman P, Johansson L, Wan H, Jones A, Gallo RL, Gudmundsson GH, et al. Induction of the antimicrobial peptide CRAMP in the blood-brain barrier and meninges after meningococcal infection. Infect Immun. 2006;74(12):6982–6991.10.1128/IAI.01043-06
   PubMed Web of Science ®Google Scholar
• Barlow PG, Findlay EG, Currie SM, Davidson DJ. Antiviral potential of cathelicidins. Future Microbiol. 2014;9(1):55–73.10.2217/fmb.13.135
   PubMed Web of Science ®Google Scholar
• Vandamme D, Landuyt B, Luyten W, Schoofs L. A comprehensive summary of LL-37, the factotum human cathelicidin peptide. Cell Immunol. 2012;280(1):22–35.10.1016/j.cellimm.2012.11.009
   PubMed Web of Science ®Google Scholar
• Bals R, Weiner DJ, Moscioni AD, Meegalla RL, Wilson JM. Augmentation of innate host defense by expression of a cathelicidin antimicrobial peptide. Infect Immun. 1999;67(11):6084–6089.
   PubMed Web of Science ®Google Scholar
• Barlow PG, Svoboda P, Mackellar A, Nash AA, York IA, Pohl J, et al. Antiviral activity and increased host defense against influenza infection elicited by the human cathelicidin LL-37. PLoS One. 2011;6(10):e25333.10.1371/journal.pone.0025333
   PubMed Web of Science ®Google Scholar
• Pütsep K, Carlsson G, Boman HG, Andersson M. Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet. 2002;360(9340):1144–1149.10.1016/S0140-6736(02)11201-3
   PubMed Web of Science ®Google Scholar
• Iimura M, Gallo RL, Hase K, Miyamoto Y, Eckmann L, Kagnoff MF. Cathelicidin mediates innate intestinal defense against colonization with epithelial adherent bacterial pathogens. J Immunol. 2005;174(8):4901–4907.10.4049/jimmunol.174.8.4901
   PubMed Web of Science ®Google Scholar
• Nizet V, Ohtake T, Lauth X, Trowbridge J, Rudisill J, Dorschner RA, et al. Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature. 2001;414(6862):454–457.10.1038/35106587
   PubMed Web of Science ®Google Scholar
• Yu FS, Cornicelli MD, Kovach MA, Newstead MW, Zeng X, Kumar A, et al. Flagellin stimulates protective lung mucosal immunity: role of cathelicidin-related antimicrobial peptide. J Immunol. 2010;185(2):1142–1149.10.4049/jimmunol.1000509
   PubMed Web of Science ®Google Scholar
• Chromek M, Slamová Z, Bergman P, Kovács L, Podracká L, Ehrén I, et al. The antimicrobial peptide cathelicidin protects the urinary tract against invasive bacterial infection. Nat Med. 2006;12(6):636–641.10.1038/nm1407
   PubMed Web of Science ®Google Scholar
• Oren Z, Shai Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry. 1997;36(7):1826–1835.10.1021/bi962507l
   PubMed Web of Science ®Google Scholar
• Xhindoli D, Pacor S, Benincasa M, Scocchi M, Gennaro R, Tossi A. The human cathelicidin LL-37 – a pore-forming antibacterial peptide and host-cell modulator. Biochim Biophys Acta. 2016;1858(3):546–566.10.1016/j.bbamem.2015.11.003
   PubMed Web of Science ®Google Scholar
• Mardirossian M, Grzela R, Giglione C, Meinnel T, Gennaro R, Mergaert P, et al. The host antimicrobial peptide bac71-35 binds to bacterial ribosomal proteins and inhibits protein synthesis. Chem Biol. 2014;21(12):1639–1647.10.1016/j.chembiol.2014.10.009
   PubMed Web of Science ®Google Scholar
• Tripathi S, Tecle T, Verma A, Crouch E, White M, Hartshorn KL. The human cathelicidin LL-37 inhibits influenza A viruses through a mechanism distinct from that of surfactant protein D or defensins. J Gen Virol. 2013;94(Pt_1):40–49.10.1099/vir.0.045013-0
   PubMed Web of Science ®Google Scholar
• Wong JH, Legowska A, Rolka K, Ng TB, Hui M, Cho CH, et al. Effects of cathelicidin and its fragments on three key enzymes of HIV-1. Peptides. 2011;32(6):1117–1122.10.1016/j.peptides.2011.04.017
   PubMed Web of Science ®Google Scholar
• Beaumont PE, Li H, Davidson DJ. LL-37: an immunomodulatory antimicrobial host defence peptide. In: Hiemstra PS, Zaat S, editors. Antimicrobial peptides and innate immunity. Basel: Springer; 2013. p. 97–121.10.1007/978-3-0348-0541-4
   Google Scholar
• Pazgier M, Li X, Lu W, Lubkowski J. Human defensins: synthesis and structural properties. Curr Pharm Des. 2007;13(30):3096–3118.10.2174/138161207782110381
   PubMed Web of Science ®Google Scholar
• Mangoni ML. Host-defense peptides: from biology to therapeutic strategies. Cell Mol Life Sci. 2011;68(13):2157–2159.10.1007/s00018-011-0709-3
   PubMed Web of Science ®Google Scholar
• Schutte BC, Mitros JP, Bartlett JA, Walters JD, Jia HP, Welsh MJ, et al. Discovery of five conserved beta -defensin gene clusters using a computational search strategy. Proc Nat Acad Sci USA. 2002;99(4):2129–2133.10.1073/pnas.042692699
   PubMed Web of Science ®Google Scholar
• Ericksen B, Wu Z, Lu W, Lehrer RI. Antibacterial activity and specificity of the six human α-defensins. Antimicrob Agents Chemother. 2005;49(1):269–275.10.1128/AAC.49.1.269-275.2005
   PubMed Web of Science ®Google Scholar
• Semple F, Dorin JR. ß-Defensins: multifunctional modulators of infection, inflammation and more? J Innate Immun. 2012;4(4):337–348.10.1159/000336619
   PubMed Web of Science ®Google Scholar
• Wilson SS, Wiens ME, Smith JG. Antiviral mechanisms of human defensins. J Mol Biol. 2013;425(24):4965–4980.10.1016/j.jmb.2013.09.038
   PubMed Web of Science ®Google Scholar
• Selsted ME, Ouellette AJ. Mammalian defensins in the antimicrobial immune response. Nat Immunol. 2005;6(6):551–557.10.1038/ni1206
   PubMed Web of Science ®Google Scholar
• Bevins CL, Salzman NH. Paneth cells, antimicrobial peptides and maintenance of intestinal homeostasis. Nat Rev Microbiol. 2011;9(5):356–368.10.1038/nrmicro2546
   PubMed Web of Science ®Google Scholar
• Ouellette AJ. Paneth cell α-defensins in enteric innate immunity. Cell Mol Life Sci. 2011;68(13):2215–2229.10.1007/s00018-011-0714-6
   PubMed Web of Science ®Google Scholar
• Com E, Bourgeon F, Evrard B, Ganz T, Colleu D, Jegou B, et al. Expression of antimicrobial defensins in the male reproductive tract of rats, mice, and humans. Biol Reprod. 2003;68(1):95–104.
   PubMed Web of Science ®Google Scholar
• Quayle AJ, Porter EM, Nussbaum AA, Wang YM, Brabec C, Yip KP, et al. Gene expression, immunolocalization, and secretion of human defensin-5 in human female reproductive tract. Am J Pathol. 1998;152(5):1247–1258.
   PubMed Web of Science ®Google Scholar
• Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, et al. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. J Biol Chem. 1993;268(9):6641–6648.
   PubMed Web of Science ®Google Scholar
• Bals R, Goldman MJ, Wilson JM. Mouse beta-defensin 1 is a salt-sensitive antimicrobial peptide present in epithelia of the lung and urogenital tract. Infect Immun. 1998;66(3):1225–1232.
   PubMed Web of Science ®Google Scholar
• Bals R, Wang X, Wu Z, Freeman T, Bafna V, Zasloff M, et al. Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung. J Clin Invest. 1998;102(5):874–880.10.1172/JCI2410
   PubMed Web of Science ®Google Scholar
• Sorensen OE, Thapa DR, Rosenthal A, Liu L, Roberts AA, Ganz T. Differential regulation of beta-defensin expression in human skin by microbial stimuli. J Immunol. 2005;174(8):4870–4879.10.4049/jimmunol.174.8.4870
   PubMed Web of Science ®Google Scholar
• Yang D, Chertov O, Bykovskaia SN, Chen Q, Buffo MJ, Shogan J, et al. Beta-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6. Science. 1999;286(5439):525–528.10.1126/science.286.5439.525
   PubMed Web of Science ®Google Scholar
• Taylor K, Clarke DJ, McCullough B, Chin W, Seo E, Yang D, et al. Analysis and separation of residues important for the chemoattractant and antimicrobial activities of beta-defensin 3. J Biol Chem. 2008;283(11):6631–6639.10.1074/jbc.M709238200
   PubMed Web of Science ®Google Scholar
• Taylor K, Rolfe M, Reynolds N, Kilanowski F, Pathania U, Clarke D, et al. Defensin-related peptide 1 (Defr1) is allelic to Defb8 and chemoattracts immature DC and CD4+ T cells independently of CCR6. Eur J Immunol. 2009;39(5):1353–1360.10.1002/eji.200838566
   PubMed Web of Science ®Google Scholar
• Wu Z, Hoover DM, Yang D, Boulegue C, Santamaria F, Oppenheim JJ, et al. Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human beta-defensin 3. Proc Nat Acad Sci USA. 2003;100(15):8880–8885.10.1073/pnas.1533186100
   PubMed Web of Science ®Google Scholar
• Jin G, Kawsar HI, Hirsch SA, Zeng C, Jia X, Feng Z, et al. An antimicrobial peptide regulates tumor-associated macrophage trafficking via the chemokine receptor CCR2, a model for tumorigenesis. PLoS One. 2010;5(6):e10993.10.1371/journal.pone.0010993
   PubMed Web of Science ®Google Scholar
• Niyonsaba F, Ushio H, Hara M, Yokoi H, Tominaga M, Takamori K, et al. Antimicrobial peptides human beta-defensins and cathelicidin LL-37 induce the secretion of a pruritogenic cytokine IL-31 by human mast cells. J Immunol. 2010;184(7):3526–3534.10.4049/jimmunol.0900712
   PubMed Web of Science ®Google Scholar
• Niyonsaba F, Ushio H, Nakano N, Ng W, Sayama K, Hashimoto K, et al. Antimicrobial peptides human beta-defensins stimulate epidermal keratinocyte migration, proliferation and production of proinflammatory cytokines and chemokines. J Invest Dermatol. 2007;127(3):594–604.10.1038/sj.jid.5700599
   PubMed Web of Science ®Google Scholar
• Nagaoka I, Niyonsaba F, Tsutsumi-Ishii Y, Tamura H, Hirata M. Evaluation of the effect of human beta-defensins on neutrophil apoptosis. Int Immunol. 2008;20(4):543–553.10.1093/intimm/dxn012
   PubMed Web of Science ®Google Scholar
• Chen Q, Jin Y, Zhang K, Li H, Chen W, Meng G, et al. Alarmin HNP-1 promotes pyroptosis and IL-1beta release through different roles of NLRP3 inflammasome via P2X7 in LPS-primed macrophages. Innate Immun. 2013;20(3):290–300. Available from: http://www.ncbi.nlm.nih.gov/pubmed/23792296.
   PubMed Web of Science ®Google Scholar
• Miles K, Clarke DJ, Lu W, Sibinska Z, Beaumont PE, Davidson DJ, et al. Dying and necrotic neutrophils are anti-inflammatory secondary to the release of alpha-defensins. J Immunol. 2009;183(3):2122–2132.10.4049/jimmunol.0804187
   PubMed Web of Science ®Google Scholar
• Semple F, Webb S, Li HN, Patel HB, Perretti M, Jackson IJ, et al. Human beta-defensin 3 has immunosuppressive activity in vitro and in vivo. Eur J Immunol. 2010;40(4):1073–1078.10.1002/eji.200940041
   PubMed Web of Science ®Google Scholar
• Wilson CL, Ouellette AJ, Satchell DP, Ayabe T, Lopez-Boado YS, Stratman JL, et al. Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense. Science. 1999;286(5437):113–117.10.1126/science.286.5437.113
   PubMed Web of Science ®Google Scholar
• Moser C, Weiner DJ, Lysenko E, Bals R, Weiser JN, Wilson JM. beta-defensin 1 contributes to pulmonary innate immunity in mice. Infect Immun. 2002;70(6):3068–3072.10.1128/IAI.70.6.3068-3072.2002
   PubMed Web of Science ®Google Scholar
• Peyrin-Biroulet L, Beisner J, Wang G, Nuding S, Oommen ST, Kelly D, et al. Peroxisome proliferator-activated receptor gamma activation is required for maintenance of innate antimicrobial immunity in the colon. Proc Nat Acad Sci USA. 2010;107(19):8772–8777.10.1073/pnas.0905745107
   PubMed Web of Science ®Google Scholar
• Salzman NH, Hung K, Haribhai D, Chu H, Karlsson-Sjöberg J, Amir E, et al. Enteric defensins are essential regulators of intestinal microbial ecology. Nat Immunol. 2010;11(1):76–82.10.1038/ni.1825
   PubMed Web of Science ®Google Scholar
• Morrison G, Kilanowski F, Davidson D, Dorin J. Characterization of the mouse beta defensin 1, Defb1, mutant mouse model. Infect Immun. 2002;70(6):3053–3060.10.1128/IAI.70.6.3053-3060.2002
   PubMed Web of Science ®Google Scholar
• Mock M, Fouet A. Anthrax. Ann Rev Microbiol. 2001;55:647–671.10.1146/annurev.micro.55.1.647
   PubMed Web of Science ®Google Scholar
• Ringertz SH, Hoiby EA, Jensenius M, Maehlen J, Caugant DA, Myklebust A, et al. Injectional anthrax in a heroin skin-popper. Lancet. 2000;356(9241):1574–1575.10.1016/S0140-6736(00)03133-0
   PubMed Web of Science ®Google Scholar
• Athamna A, Massalha M, Athamna M, Nura A, Medlej B, Ofek I, et al. In vitro susceptibility of Bacillus anthracis to various antibacterial agents and their time-kill activity. J Antimicrob Chemother. 2004;53(2):247–251.10.1093/jac/dkh016
   PubMed Web of Science ®Google Scholar
• Radyuk SN, Mericko PA, Popova TG, Grene E, Alibek K. In vitro-generated respiratory mucosa: a new tool to study inhalational anthrax. Biochem Biophys Res Commun. 2003;305(3):624–632.10.1016/S0006-291X(03)00830-1
   PubMed Web of Science ®Google Scholar
• Wang W, Mulakala C, Ward SC, Jung G, Luong H, Pham D, et al. Retrocyclins kill bacilli and germinating spores of Bacillus anthracis and inactivate anthrax lethal toxin. J Biol Chem. 2006;281(43):32755–32764.10.1074/jbc.M603614200
   PubMed Web of Science ®Google Scholar
• Thwaite JE, Hibbs S, Titball RW, Atkins TP. Proteolytic degradation of human antimicrobial peptide LL-37 by Bacillus anthracis may contribute to virulence. Antimicrob Agents Chemother. 2006;50(7):2316–2322.10.1128/AAC.01488-05
   PubMed Web of Science ®Google Scholar
• Lisanby MW, Swiecki MK, Dizon BL, Pflughoeft KJ, Koehler TM, Kearney JF. Cathelicidin administration protects mice from Bacillus anthracis spore challenge. J Immunol. 2008;181(7):4989–5000.10.4049/jimmunol.181.7.4989
   PubMed Web of Science ®Google Scholar
• McGillivray SM, Ebrahimi CM, Fisher N, Sabet M, Zhang DX, Chen Y, et al. ClpX contributes to innate defense peptide resistance and virulence phenotypes of Bacillus anthracis. J Innate Immun. 2009;1(5):494–506.10.1159/000225955
   PubMed Web of Science ®Google Scholar
• McGillivray SM, Tran DN, Ramadoss NS, Alumasa JN, Okumura CY, Sakoulas G, et al. Pharmacological inhibition of the ClpXP protease increases bacterial susceptibility to host cathelicidin antimicrobial peptides and cell envelope-active antibiotics. Antimicrob Agents Chemother. 2012;56(4):1854–1861.10.1128/AAC.05131-11
   PubMed Web of Science ®Google Scholar
• Franks SE, Ebrahimi C, Hollands A, Okumura CY, Aroian RV, Nizet V, et al. Novel role for the yceGH tellurite resistance genes in the pathogenesis of Bacillus anthracis. Infect Immun. 2014;82(3):1132–1140.10.1128/IAI.01614-13
   PubMed Web of Science ®Google Scholar
• Samant S, Hsu FF, Neyfakh AA, Lee H. The Bacillus anthracis protein MprF is required for synthesis of lysylphosphatidylglycerols and for resistance to cationic antimicrobial peptides. J Bacteriol. 2009;191(4):1311–1319.10.1128/JB.01345-08
   PubMed Web of Science ®Google Scholar
• Molhoek EM, van Dijk A, Veldhuizen EJ, Dijk-Knijnenburg H, Mars-Groenendijk RH, Boele LC, et al. Chicken cathelicidin-2-derived peptides with enhanced immunomodulatory and antibacterial activities against biological warfare agents. Int J Antimicrob Agents. 2010;36(3):271–274.10.1016/j.ijantimicag.2010.06.001
   PubMed Web of Science ®Google Scholar
• Fox MA, Thwaite JE, Ulaeto DO, Atkins TP, Atkins HS. Design and characterization of novel hybrid antimicrobial peptides based on cecropin A, LL-37 and magainin II. Peptides. 2012;33(2):197–205.10.1016/j.peptides.2012.01.013
   PubMed Web of Science ®Google Scholar
• Kim C, Gajendran N, Mittrucker HW, Weiwad M, Song YH, Hurwitz R, et al. Human alpha-defensins neutralize anthrax lethal toxin and protect against its fatal consequences. Proc Nat Acad Sci USA. 2005;102(13):4830–4835.10.1073/pnas.0500508102
   PubMed Web of Science ®Google Scholar
• Mayer-Scholl A, Hurwitz R, Brinkmann V, Schmid M, Jungblut P, Weinrauch Y, et al. Human neutrophils kill Bacillus anthracis. PLoS Pathog. 2005;1(3):e23.10.1371/journal.ppat.0010023
   Google Scholar
• Pazgier M, Wei G, Ericksen B, Jung G, Wu Z, de Leeuw E, et al. Sometimes it takes two to tango: contributions of dimerization to functions of human alpha-defensin HNP1 peptide. J Biol Chem. 2012;287(12):8944–8953.10.1074/jbc.M111.332205
   PubMed Web of Science ®Google Scholar
• Zhao L, Tolbert WD, Ericksen B, Zhan C, Wu X, Yuan W, et al. Single, double and quadruple alanine substitutions at oligomeric interfaces identify hydrophobicity as the key determinant of human neutrophil alpha defensin hnp1 function. PLoS One. 2013;8(11):e78937.10.1371/journal.pone.0078937
   Google Scholar
• Welkos S, Cote CK, Hahn U, Shastak O, Jedermann J, Bozue J, et al. Humanized theta-defensins (retrocyclins) enhance macrophage performance and protect mice from experimental anthrax infections. Antimicrob Agents Chemother. 2011;55(9):4238–4250.10.1128/AAC.00267-11
   PubMed Web of Science ®Google Scholar
• Galimand M, Carniel E, Courvalin P. Resistance of Yersinia pestis to Antimicrobial Agents. Antimicrobial Agents Chemother. 2006;50(10):3233–3236.10.1128/AAC.00306-06
   PubMed Web of Science ®Google Scholar
• Klein KA, Fukuto HS, Pelletier M, Romanov G, Grabenstein JP, Palmer LE, et al. A transposon site hybridization screen identifies galU and wecBC as important for survival of Yersinia pestis in murine macrophages. J Bacteriol. 2012;194(3):653–662.10.1128/JB.06237-11
   PubMed Web of Science ®Google Scholar
• WHO. Human plague: review of regional morbidity and mortality. Wkly Epidemiol Rec. 2010;85(6):40–45.
   Google Scholar
• Galimand M, Guiyoule A, Gerbaud G, Rasoamanana B, Chanteau S, Carniel E, et al. Multidrug resistance in Yersinia pestis mediated by a transferable plasmid. N Engl J Med. 1997;337(10):677–681.10.1056/NEJM199709043371004
   PubMed Web of Science ®Google Scholar
• Guiyoule A, Gerbaud G, Buchrieser C, Galimand M, Rahalison L, Chanteau S, et al. Transferable plasmid-mediated resistance to streptomycin in a clinical isolate of Yersinia pestis. Emerg Infect Diseases. 2001;7(1):43–48.10.3201/eid0701.010106
   PubMed Web of Science ®Google Scholar
• Chanteau S, Ratsitorahina M, Rahalison L, Rasoamanana B, Chan F, Boisier P, et al. Current epidemiology of human plague in Madagascar. Microb Infect. 2000;2(1):25–31.10.1016/S1286-4579(00)00289-6
   PubMed Web of Science ®Google Scholar
• Hinnebusch BJ, Rosso ML, Schwan TG, Carniel E. High-frequency conjugative transfer of antibiotic resistance genes to Yersinia pestis in the flea midgut. Mol Microbiol. 2002;46(2):349–354.10.1046/j.1365-2958.2002.03159.x
   PubMed Web of Science ®Google Scholar
• Abdelbaqi S, Deslouches B, Steckbeck J, Montelaro R, Reed DS. Novel engineered cationic antimicrobial peptides display broad-spectrum activity against Francisella tularensis, Yersinia pestis and Burkholderia pseudomallei. J Med Microbiol. 2016;65(2):188–194.10.1099/jmm.0.000209
   PubMed Web of Science ®Google Scholar
• Guo J, Nair MK, Galván EM, Liu SL, Schifferli DM. Tn5AraOut mutagenesis for the identification of Yersinia pestis genes involved in resistance towards cationic antimicrobial peptides. Microb Pathog. 2011;51(3):121–132.10.1016/j.micpath.2011.04.010
   PubMed Web of Science ®Google Scholar
• Galvan EM, Lasaro MA, Schifferli DM. Capsular antigen fraction 1 and Pla modulate the susceptibility of Yersinia pestis to pulmonary antimicrobial peptides such as cathelicidin. Infect Immun. 2008;76(4):1456–1464.10.1128/IAI.01197-07
   PubMed Web of Science ®Google Scholar
• Flick-Smith HC, Fox MA, Hamblin KA, Richards MI, Jenner DC, Laws TR, et al. Assessment of antimicrobial peptide LL-37 as a post-exposure therapy to protect against respiratory tularemia in mice. Peptides. 2013;43:96–101.10.1016/j.peptides.2013.02.024
   PubMed Web of Science ®Google Scholar
• Amer LS, Bishop BM, van Hoek ML. Antimicrobial and antibiofilm activity of cathelicidins and short, synthetic peptides against Francisella. Biochem Biophys Res Commun. 2010;396(2):246–251.10.1016/j.bbrc.2010.04.073
   PubMed Web of Science ®Google Scholar
• Han S, Bishop BM, van Hoek ML. Antimicrobial activity of human beta-defensins and induction by Francisella. Biochem Biophys Res Commun. 2008;371(4):670–674.10.1016/j.bbrc.2008.04.092
   PubMed Web of Science ®Google Scholar
• 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 Nat Acad Sci USA. 1998;95(16):9541–9546.10.1073/pnas.95.16.9541
   PubMed Web of Science ®Google Scholar
• Bowdish DM, Davidson DJ, Lau YE, Lee K, Scott MG, Hancock RE. Impact of LL-37 on anti-infective immunity. J Leukoc Biol. 2005;77(4):451–459.
   PubMed Web of Science ®Google Scholar
• Howell MD, Jones JF, Kisich KO, Streib JE, Gallo RL, Leung DY. Selective killing of vaccinia virus by LL-37: implications for eczema vaccinatum. J Immunol. 2004;172(3):1763–1767.10.4049/jimmunol.172.3.1763
   PubMed Web of Science ®Google Scholar
• Dean RE, O’Brien LM, Thwaite JE, Fox MA, Atkins H, Ulaeto DO. A carpet-based mechanism for direct antimicrobial peptide activity against vaccinia virus membranes. Peptides. 2010;31(11):1966–1972.10.1016/j.peptides.2010.07.028
   PubMed Web of Science ®Google Scholar
• Barton D, HogenEsch H, Weih F. Mice lacking the transcription factor RelB develop T cell-dependent skin lesions similar to human atopic dermatitis. Eur J Immunol. 2000;30(8):2323–2332.10.1002/(ISSN)1521-4141
   PubMed Web of Science ®Google Scholar
• Kawakami Y, Tomimori Y, Yumoto K, Hasegawa S, Ando T, Tagaya Y, et al. Inhibition of NK cell activity by IL-17 allows vaccinia virus to induce severe skin lesions in a mouse model of eczema vaccinatum. J Exp Med. 2009;206(6):1219–1225.10.1084/jem.20082835
   PubMed Web of Science ®Google Scholar
• Oyoshi MK, Elkhal A, Kumar L, Scott JE, Koduru S, He R, et al. Vaccinia virus inoculation in sites of allergic skin inflammation elicits a vigorous cutaneous IL-17 response. Proc Nat Acad Sci USA. 2009;106(35):14954–14959.10.1073/pnas.0904021106
   PubMed Web of Science ®Google Scholar
• Laughter D, Istvan JA, Tofte SJ, Hanifin JM. The prevalence of atopic dermatitis in Oregon schoolchildren. J Am Acad Dermatol. 2000;43(4):649–655.10.1067/mjd.2000.107773
   PubMed Web of Science ®Google Scholar
• Wollenberg A, Engler R. Smallpox, vaccination and adverse reactions to smallpox vaccine. Curr Opin Allergy Clin Immunol. 2004;4(4):271–275.10.1097/01.all.0000136758.66442.28
   PubMedGoogle Scholar
• Domenico J, Lucas JJ, Fujita M, Gelfand EW. Susceptibility to vaccinia virus infection and spread in mice is determined by age at infection, allergen sensitization and mast cell status. Int Arch Allergy Immunol. 2012;158(2):196–205.10.1159/000330647
   PubMed Web of Science ®Google Scholar
• Di Nardo A, Vitiello A, Gallo RL. Cutting edge: mast cell antimicrobial activity is mediated by expression of cathelicidin antimicrobial peptide. J Immunol. 2003;170(5):2274–2278.10.4049/jimmunol.170.5.2274
   PubMed Web of Science ®Google Scholar
• Wang Z, Lai Y, Bernard JJ, MacLeod DT, Cogen AL, Moss B, et al. Skin mast cells protect mice against vaccinia virus by triggering mast cell receptor S1PR2 and releasing antimicrobial peptides. J Immunol. 2012;188(1):345–357.10.4049/jimmunol.1101703
   PubMed Web of Science ®Google Scholar
• Garrison AR, Giomarelli BG, Lear-Rooney CM, Saucedo CJ, Yellayi S, Krumpe LR, et al. The cyanobacterial lectin scytovirin displays potent in vitro and in vivo activity against Zaire Ebola virus. Antiviral Res. 2014;112:1–7.10.1016/j.antiviral.2014.09.012
   PubMed Web of Science ®Google Scholar
• Vanheule V, Vervaeke P, Mortier A, Noppen S, Gouwy M, Snoeck R, et al. Basic chemokine-derived glycosaminoglycan binding peptides exert antiviral properties against dengue virus serotype 2, herpes simplex virus-1 and respiratory syncytial virus. Biochem Pharmacol. 2015;100:73–85. Available from: http://www.ncbi.nlm.nih.gov/pubmed/26551597.
   PubMed Web of Science ®Google Scholar
• Fox JL. Antimicrobial peptides stage a comeback. Nat Biotechnol. 2013;31(5):379–382.10.1038/nbt.2572
   PubMed Web of Science ®Google Scholar
• Mendez-Samperio P. Recent advances in the field of antimicrobial peptides in inflammatory diseases. Adv Biomed Res. 2013;2:50.10.4103/2277-9175.114192
   PubMedGoogle Scholar
• Bauer ME, Shafer WM. On the in vivo significance of bacterial resistance to antimicrobial peptides. Biochim Biophys Acta. 2015;1848(11):3101–3111.10.1016/j.bbamem.2015.02.012
   PubMed Web of Science ®Google Scholar
• Wang G, Hanke ML, Mishra B, Lushnikova T, Heim CE, Chittezham Thomas V, et al. Transformation of human cathelicidin LL-37 into selective, stable, and potent antimicrobial compounds. ACS Chem Biol. 2014;9(9):1997–2002.10.1021/cb500475y
   PubMed Web of Science ®Google Scholar