{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,15]],"date-time":"2026-04-15T20:02:50Z","timestamp":1776283370410,"version":"3.50.1"},"reference-count":36,"publisher":"Springer Science and Business Media LLC","issue":"11","license":[{"start":{"date-parts":[[2016,4,6]],"date-time":"2016-04-06T00:00:00Z","timestamp":1459900800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2016,4,6]],"date-time":"2016-04-06T00:00:00Z","timestamp":1459900800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Antibiot"],"published-print":{"date-parts":[[2016,11]]},"DOI":"10.1038\/ja.2016.16","type":"journal-article","created":{"date-parts":[[2016,4,6]],"date-time":"2016-04-06T06:21:47Z","timestamp":1459923707000},"page":"783-790","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Frog skin cultures secrete anti-yellow fever compounds"],"prefix":"10.1038","volume":"69","author":[{"given":"Carolina","family":"Mu\u00f1oz-Camargo","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Margarita Correa","family":"M\u00e9ndez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vivian","family":"Salazar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Johanna","family":"Moscoso","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Diana","family":"Narv\u00e1ez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria Mercedes","family":"Torres","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Franz Kaston","family":"Florez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Helena","family":"Groot","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eduardo","family":"Mitrani","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2016,4,6]]},"reference":[{"key":"BFja201616_CR1","doi-asserted-by":"publisher","first-page":"1154","DOI":"10.1093\/nar\/gkt1157","volume":"42","author":"FH Waghu","year":"2014","unstructured":"Waghu, F. H. et al. CAMP: collection of sequences and structures of antimicrobial peptides. Nucleic Acids Res. 42, 1154\u20131158 (2014).","journal-title":"Nucleic Acids Res."},{"key":"BFja201616_CR2","doi-asserted-by":"publisher","first-page":"58","DOI":"10.3390\/ph7010058","volume":"7","author":"JM Conlon","year":"2014","unstructured":"Conlon, J. M. & Mechkarska, M. Host-defense peptides with therapeutic potential from skin secretions of frogs from the family pipidae. Pharmaceuticals (Basel) 7, 58\u201377 (2014).","journal-title":"Pharmaceuticals (Basel)"},{"key":"BFja201616_CR3","doi-asserted-by":"publisher","first-page":"2068","DOI":"10.1046\/j.1432-1033.2003.03584.x","volume":"270","author":"D Vanhoye","year":"2003","unstructured":"Vanhoye, D., Bruston, F., Nicolas, P. & Amiche, M. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. Eur. J. Biochem. 270, 2068\u20132081 (2003).","journal-title":"Eur. J. Biochem."},{"key":"BFja201616_CR4","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1007\/s00441-010-1014-4","volume":"343","author":"JM Conlon","year":"2011","unstructured":"Conlon, J. M. The contribution of skin antimicrobial peptides to the system of innate immunity in anurans. Cell Tissue Res. 343, 201\u2013212 (2011).","journal-title":"Cell Tissue Res."},{"key":"BFja201616_CR5","doi-asserted-by":"publisher","first-page":"132","DOI":"10.1016\/j.peptides.2014.03.020","volume":"56","author":"JM Conlon","year":"2014","unstructured":"Conlon, J. M. et al. A family of antimicrobial and immunomodulatory peptides related to the frenatins from skin secretions of the Orinoco lime frog Sphaenorhynchus lacteus (Hylidae). Peptides 56, 132\u2013140 (2014).","journal-title":"Peptides"},{"key":"BFja201616_CR6","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1016\/j.peptides.2013.10.015","volume":"50","author":"M Mechkarska","year":"2013","unstructured":"Mechkarska, M. et al. An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties. Peptides 50, 153\u2013159 (2013).","journal-title":"Peptides"},{"key":"BFja201616_CR7","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1034\/j.1399-3011.2003.00090.x","volume":"62","author":"JM Conlon","year":"2003","unstructured":"Conlon, J. M. et al. Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii. J. Pept. Res. 62, 207\u2013213 (2003).","journal-title":"J. Pept. Res."},{"key":"BFja201616_CR8","doi-asserted-by":"publisher","first-page":"797","DOI":"10.1007\/s10886-013-0294-z","volume":"39","author":"JM Conlon","year":"2013","unstructured":"Conlon, J. M. et al. Evaluation of the Skin Peptide Defenses of the Oregon Spotted Frog Rana pretiosa Against Infection by the Chytrid Fungus Batrachochytrium dendrobatidis. J. Chem. Ecol. 39, 797\u2013805 (2013).","journal-title":"J. Chem. Ecol."},{"key":"BFja201616_CR9","doi-asserted-by":"publisher","first-page":"272","DOI":"10.1002\/jmv.23450","volume":"85","author":"I Bergaoui","year":"2013","unstructured":"Bergaoui, I. et al. In vitro antiviral activity of dermaseptin S4 and derivatives from amphibian skin against herpes simplex virus type 2. J. Med. Virol. 85, 272\u2013281 (2013).","journal-title":"J. Med. Virol."},{"key":"BFja201616_CR10","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1002\/jmv.2134","volume":"66","author":"A Belaid","year":"2002","unstructured":"Belaid, A. et al. In vitro antiviral activity of dermaseptins against herpes simplex virus type 1. J. Med. Virol. 66, 229\u2013234 (2002).","journal-title":"J. Med. Virol."},{"key":"BFja201616_CR11","doi-asserted-by":"publisher","first-page":"11598","DOI":"10.1128\/JVI.79.18.11598-11606.2005","volume":"79","author":"SE Vancompernolle","year":"2005","unstructured":"Vancompernolle, S. E. et al. Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells. J. Virol. 79, 11598\u201311606 (2005).","journal-title":"J. Virol."},{"key":"BFja201616_CR12","first-page":"11","volume":"80","author":"P Rushika","year":"2009","unstructured":"Rushika, P., Mansoora, K. & Richard, J. K. Closing the door on flaviviruses: entry as a target for antiviral drug design. Antiviral Res. 80, 11\u201322 (2009).","journal-title":"Antiviral Res."},{"key":"BFja201616_CR13","doi-asserted-by":"publisher","first-page":"64","DOI":"10.1007\/s12539-011-0064-y","volume":"3","author":"A Umamaheswari","year":"2011","unstructured":"Umamaheswari, A., Kumar, M., Pradhan, D. & Marisetty, H. Docking studies towards exploring antiviral compounds against envelope protein of yellow fever virus. Interdiscip. Sci. Comput. Life Sci. 3, 64\u201377 (2011).","journal-title":"Interdiscip. Sci. Comput. Life Sci."},{"key":"BFja201616_CR14","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/S1473-3099(01)00016-0","volume":"1","author":"TP Monath","year":"2015","unstructured":"Monath, T. P. Yellow fever: an update. Lancet Infect. Dis. 1, 11\u201320 (2015).","journal-title":"Lancet Infect. Dis."},{"key":"BFja201616_CR15","doi-asserted-by":"publisher","first-page":"960","DOI":"10.1001\/jama.300.8.960","volume":"300","author":"J Staples","year":"2008","unstructured":"Staples, J. & Monath, T. Yellow fever: 100 years of discovery. J. Am. Med. Assoc. 300, 960\u2013962 (2008).","journal-title":"J. Am. Med. Assoc."},{"key":"BFja201616_CR16","doi-asserted-by":"publisher","first-page":"1884","DOI":"10.1093\/jac\/dks147","volume":"67","author":"E Mastrangelo","year":"2012","unstructured":"Mastrangelo, E. et al. Ivermectin is a potent inhibitor of flavivirus replication specifically targeting NS3 helicase activity: new prospects for an old drug. J. Antimicrob. Chemother. 67, 1884\u20131894 (2012).","journal-title":"J. Antimicrob. Chemother."},{"key":"BFja201616_CR17","doi-asserted-by":"publisher","first-page":"246","DOI":"10.1007\/s11908-012-0256-6","volume":"14","author":"D Hill","year":"2012","unstructured":"Hill, D. Mapping the risk of yellow fever infection. Curr. Infect. Dis. Rep. 14, 246\u2013255 (2012).","journal-title":"Curr. Infect. Dis. Rep."},{"key":"BFja201616_CR18","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1186\/1756-3305-5-175","volume":"5","author":"C Ngoagouni","year":"2012","unstructured":"Ngoagouni, C. et al. Entomological profile of yellow fever epidemics in the Central African Republic, 2006\u20132010. Parasit. Vectors 5, 175 (2012).","journal-title":"Parasit. Vectors"},{"key":"BFja201616_CR19","doi-asserted-by":"publisher","first-page":"461","DOI":"10.1038\/ja.2012.50","volume":"65","author":"H Groot","year":"2012","unstructured":"Groot, H. et al. Skin micro-organs from several frog species secrete a repertoire of powerful antimicrobials in culture. J. Antibiot. 65, 461\u2013467 (2012).","journal-title":"J. Antibiot."},{"key":"BFja201616_CR20","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1016\/S0145-305X(01)00088-X","volume":"26","author":"LA Rollins-Smith","year":"2002","unstructured":"Rollins-Smith, L. A. et al. Activity of antimicrobial skin peptides from ranid frogs against Batrachochytrium dendrobatidis, the chytrid fungus associated with global amphibian declines. Dev. Comp. Immunol. 26, 471\u2013479 (2002).","journal-title":"Dev. Comp. Immunol."},{"key":"BFja201616_CR21","doi-asserted-by":"publisher","first-page":"156","DOI":"10.1016\/0003-2697(87)90021-2","volume":"162","author":"P Chomczynski","year":"1987","unstructured":"Chomczynski, P. & Sacchi, N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156\u2013159 (1987).","journal-title":"Anal. Biochem."},{"key":"BFja201616_CR22","doi-asserted-by":"publisher","first-page":"2129","DOI":"10.1016\/j.peptides.2006.04.006","volume":"27","author":"T Chen","year":"2006","unstructured":"Chen, T., Zhou, M., Gagliardo, R., Walker, B. & Shaw, C. Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis. Peptides 27, 2129\u20132136 (2006).","journal-title":"Peptides"},{"key":"BFja201616_CR23","doi-asserted-by":"publisher","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","volume":"25","author":"SF Altschul","year":"1997","unstructured":"Altschul, S. F. et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389\u20133402 (1997).","journal-title":"Nucleic Acids Res."},{"key":"BFja201616_CR24","volume-title":"Multiple Sequence Alignment Using ClustalW and ClustalX. Current Protocols in Bioinformatics","author":"JD Thompson","year":"2002","unstructured":"Thompson, J. D., Gibson, T. J. & Higgins, D. G. Multiple Sequence Alignment Using ClustalW and ClustalX. Current Protocols in Bioinformatics. (John Wiley & Sons, Inc., (2002)."},{"key":"BFja201616_CR25","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1016\/0166-3542(96)89697-5","volume":"30","author":"J Neyts","year":"1996","unstructured":"Neyts, J., Meerbach, A., Mckenna, P. & Declercq, E. Use of the yellow fever virus vaccine strain 17D for the study of strategies for the treatment of yellow fever virus infections. Antiviral Res. 30, 125\u2013132 (1996).","journal-title":"Antiviral Res."},{"key":"BFja201616_CR26","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1620\/tjem.176.163","volume":"176","author":"K Sudo","year":"1995","unstructured":"Sudo, K., Konno, K., Yokota, T. & Shigeta, S. A screening system for antiviral compounds against Herpes Simplex Virus type 1 using the MTT method with L929 cells. Tohoku J. Exp. Med. 176, 163\u2013171 (1995).","journal-title":"Tohoku J. Exp. Med."},{"key":"BFja201616_CR27","doi-asserted-by":"publisher","first-page":"1461","DOI":"10.1124\/mol.105.020057","volume":"69","author":"P Leyssen","year":"2006","unstructured":"Leyssen, P., De Clercq, E. & Neyts, J. The anti-yellow fever virus activity of ribavirin is independent of error-prone replication. Mol. Pharmacol. 69, 1461\u20131467 (2006).","journal-title":"Mol. Pharmacol."},{"key":"BFja201616_CR28","doi-asserted-by":"publisher","first-page":"2445","DOI":"10.1016\/j.peptides.2005.05.019","volume":"26","author":"M Zhou","year":"2005","unstructured":"Zhou, M., Chen, T., Walker, B. & Shaw, C. Novel frenatins from the skin of the Australasian giant white-lipped tree frog, Litoria infrafrenata: cloning of precursor cDNAs and identification in defensive skin secretion. Peptides 26, 2445\u20132451 (2005).","journal-title":"Peptides"},{"key":"BFja201616_CR29","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1017\/S0006323197005045","volume":"72","author":"BT Clarke","year":"1997","unstructured":"Clarke, B. T. The natural history of amphibian skin secretions, their normal functioning and potential medical applications. Biol. Rev. Camb. Philos. Soc. 72, 365\u2013379 (1997).","journal-title":"Biol. Rev. Camb. Philos. Soc."},{"key":"BFja201616_CR30","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1016\/j.peptides.2012.12.012","volume":"40","author":"JM Conlon","year":"2013","unstructured":"Conlon, J. M. et al. An immunomodulatory peptide related to frenatin 2 from skin secretions of the Tyrrhenian painted frog Discoglossus sardus (Alytidae). Peptides 40, 65\u201371 (2013).","journal-title":"Peptides"},{"key":"BFja201616_CR31","doi-asserted-by":"publisher","first-page":"268","DOI":"10.1016\/j.virol.2004.02.029","volume":"323","author":"VG Chinchar","year":"2004","unstructured":"Chinchar, V. G. et al. Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. Virology 323, 268\u2013275 (2004).","journal-title":"Virology"},{"key":"BFja201616_CR32","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1016\/j.ijantimicag.2003.07.022","volume":"23","author":"V Albiol Matanic","year":"2004","unstructured":"Albiol Matanic, V. & Castilla, V. Antiviral activity of antimicrobial cationic peptides against Junin virus and herpes simplex virus. J. Antimicrob. Agents 23, 382\u2013389 (2004).","journal-title":"J. Antimicrob. Agents"},{"key":"BFja201616_CR33","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1128\/MMBR.00016-10","volume":"74","author":"J Davies","year":"2010","unstructured":"Davies, J. & Davies, D. Origins and evolution of antibiotic resistance. Microbiol. Mol. Biol. Rev. 74, 417\u2013433 (2010).","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"BFja201616_CR34","doi-asserted-by":"publisher","first-page":"447","DOI":"10.1038\/nri1860","volume":"6","author":"ME Klotman","year":"2006","unstructured":"Klotman, M. E. & Chang, T. L. Defensins in innate antiviral immunity. Nat. Rev. Immunol. 6, 447\u2013456 (2006).","journal-title":"Nat. Rev. Immunol."},{"key":"BFja201616_CR35","doi-asserted-by":"crossref","first-page":"31635","DOI":"10.1016\/S0021-9258(18)31742-3","volume":"269","author":"A Mor","year":"1994","unstructured":"Mor, A., Hani, K. & Nicolas, P. The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms. J. Biol. Chem. 269, 31635\u201331641 (1994).","journal-title":"J. Biol. Chem."},{"key":"BFja201616_CR36","doi-asserted-by":"publisher","first-page":"703","DOI":"10.1586\/eri.10.38","volume":"8","author":"M Cassone","year":"2010","unstructured":"Cassone, M. & Otvos, L. Synergy among antibacterial peptides and between peptides and small-molecule antibiotics. Expert Rev. Anti. Infect. Ther. 8, 703\u2013716 (2010).","journal-title":"Expert Rev. Anti. Infect. Ther."}],"container-title":["The Journal of Antibiotics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/ja201616.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/ja201616","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/ja201616.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T17:23:14Z","timestamp":1684430594000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/ja201616"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,4,6]]},"references-count":36,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2016,11]]}},"alternative-id":["BFja201616"],"URL":"https:\/\/doi.org\/10.1038\/ja.2016.16","relation":{},"ISSN":["0021-8820","1881-1469"],"issn-type":[{"value":"0021-8820","type":"print"},{"value":"1881-1469","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,4,6]]},"assertion":[{"value":"20 May 2015","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"11 January 2016","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"20 January 2016","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"6 April 2016","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no conflict of interest.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}},{"value":"This content has been made available to all.","name":"free","label":"Free to read"}]}}