{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,7]],"date-time":"2026-03-07T23:58:12Z","timestamp":1772927892607,"version":"3.50.1"},"reference-count":50,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2012,2,1]],"date-time":"2012-02-01T00:00:00Z","timestamp":1328054400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2012,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Host defense peptides are naturally occurring molecules that play essential roles in innate immunity to infection. Based on prior structure-function knowledge, we tested two synthetic peptides (RP-1 and AA-RP-1) modeled on the conserved, microbicidal \u03b1-helical domain of mammalian CXCL4 platelet kinocidins. These peptides were evaluated for efficacy against\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Leishmania<\/jats:named-content>\n            species, the causative agents of the group of diseases known as leishmaniasis.\n            <jats:italic>In vitro<\/jats:italic>\n            antileishmanial activity was assessed against three distinct\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Leishmania<\/jats:named-content>\n            strains by measuring proliferation, metabolic activity and parasite viability after exposure to various concentrations of peptides. We demonstrate that micromolar concentrations of RP-1 and AA-RP-1 caused dose-dependent growth inhibition of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Leishmania<\/jats:named-content>\n            promastigotes. This antileishmanial activity correlated with rapid membrane disruption, as well as with a loss of mitochondrial transmembrane potential. In addition, RP-1 and AA-RP-1 demonstrated distinct and significant\n            <jats:italic>in vivo<\/jats:italic>\n            antileishmanial activities in a mouse model of experimental visceral leishmaniasis after intravenous administration. These results establish efficacy of RP-1 lineage synthetic peptides against\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Leishmania<\/jats:named-content>\n            species\n            <jats:italic>in vitro<\/jats:italic>\n            and after intravenous administration\n            <jats:italic>in vivo<\/jats:italic>\n            and provide further validation of proof of concept for the development of these and related systemic anti-infective peptides targeting pathogens that are resistant to conventional antibiotics.\n          <\/jats:p>","DOI":"10.1128\/aac.05349-11","type":"journal-article","created":{"date-parts":[[2011,11,30]],"date-time":"2011-11-30T02:31:59Z","timestamp":1322620319000},"page":"658-665","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":25,"title":["Efficacy of Synthetic Peptides RP-1 and AA-RP-1 against Leishmania Species\n            <i>In Vitro<\/i>\n            and\n            <i>In Vivo<\/i>"],"prefix":"10.1128","volume":"56","author":[{"given":"Marie Crisel B.","family":"Erfe","sequence":"first","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Consuelo V.","family":"David","sequence":"additional","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"},{"name":"London School of Hygiene and Tropical Medicine, London, United Kingdom"},{"name":"University of Maryland School of Medicine, Baltimore, Maryland, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cher","family":"Huang","sequence":"additional","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Victoria","family":"Lu","sequence":"additional","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ana Claudia","family":"Maretti-Mira","sequence":"additional","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"},{"name":"Laboratory of Interdisciplinary Medical Research, Instituto Oswaldo Cruz at Fiocruz, Rio de Janeiro, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jacquelyn","family":"Haskell","sequence":"additional","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kevin W.","family":"Bruhn","sequence":"additional","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"},{"name":"David Geffen School of Medicine at the University of California, Los Angeles, Los Angeles, California, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael R.","family":"Yeaman","sequence":"additional","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"},{"name":"David Geffen School of Medicine at the University of California, Los Angeles, Los Angeles, California, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Noah","family":"Craft","sequence":"additional","affiliation":[{"name":"Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California, USA"},{"name":"David Geffen School of Medicine at the University of California, Los Angeles, Los Angeles, California, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.48.2.641-643.2004"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.cdd.4400951"},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.exppara.2009.03.019","article-title":"Leishmania donovani: thionins, plant antimicrobial peptides with leishmanicidal activity","volume":"122","author":"Berrocal-Lobo M","year":"2009","unstructured":"Berrocal-LoboM MolinaA Rodriguez-PalenzuelaP Garcia-OlmedoF RivasL. 2009. Leishmania donovani: thionins, plant antimicrobial peptides with leishmanicidal activity. Exp. Parasitol. 122: 247\u2013249.","journal-title":"Exp. Parasitol"},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1007\/s00436-006-0133-z","article-title":"In vitro leishmanicidal activity of Tityus discrepans scorpion venom","volume":"99","author":"Borges A","year":"2006","unstructured":"BorgesA. 2006. In vitro leishmanicidal activity of Tityus discrepans scorpion venom. Parasitol. Res. 99: 167\u2013173.","journal-title":"Parasitol. Res"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1002\/bip.21071"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pntd.0000886"},{"key":"e_1_3_2_8_2","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/S0020-7519(03)00008-0","article-title":"Programmed cell death in trypanosomatids and other unicellular organisms","volume":"33","author":"Debrabant A","year":"2003","unstructured":"DebrabantA LeeN BertholetS DuncanR NakhasiHL. 2003. Programmed cell death in trypanosomatids and other unicellular organisms. Int. J. Parasitol. 33: 257\u2013267.","journal-title":"Int. J. Parasitol"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cimid.2004.03.004"},{"issue":"1","key":"e_1_3_2_10_2","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1042\/bj3300453","article-title":"The plasma membrane of Leishmania donovani promastigotes is the main target for CA(1-8)M(1-18), a synthetic cecropin A-melittin hybrid peptide","volume":"330","author":"Diaz-Achirica P","year":"1998","unstructured":"Diaz-AchiricaP UbachJ GuineaA AndreuD RivasL. 1998. The plasma membrane of Leishmania donovani promastigotes is the main target for CA(1-8)M(1-18), a synthetic cecropin A-melittin hybrid peptide. Biochem. J. 330(Pt 1): 453\u2013460.","journal-title":"Biochem. J"},{"key":"e_1_3_2_11_2","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.parint.2005.01.001","article-title":"Development of a modified MTT assay for screening antimonial resistant field isolates of Indian visceral leishmaniasis","volume":"54","author":"Dutta A","year":"2005","unstructured":"DuttaA BandyopadhyayS MandalC ChatterjeeM. 2005. Development of a modified MTT assay for screening antimonial resistant field isolates of Indian visceral leishmaniasis. Parasitol. Int. 54: 119\u2013122.","journal-title":"Parasitol. Int"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00018-010-0306-x"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pntd.0000373"},{"key":"e_1_3_2_14_2","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/S1471-4922(02)02352-8","article-title":"Interaction of Leishmania with the host macrophage","volume":"18","author":"Handman E","year":"2002","unstructured":"HandmanE BullenDV. 2002. Interaction of Leishmania with the host macrophage. Trends Parasitol. 18: 332\u2013334.","journal-title":"Trends Parasitol"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.169.1.59"},{"key":"e_1_3_2_16_2","first-page":"414","article-title":"Functional and structural damage in Leishmania mexicana exposed to the cationic peptide dermaseptin","volume":"59","author":"Hernandez C","year":"1992","unstructured":"HernandezC. 1992. Functional and structural damage in Leishmania mexicana exposed to the cationic peptide dermaseptin. Eur. J. Cell Biol. 59: 414\u2013424.","journal-title":"Eur. J. Cell Biol"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(98)10178-2"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(09)60233-6"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00056-05"},{"key":"e_1_3_2_20_2","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1111\/j.1462-5822.2011.01589.x","article-title":"Mammalian antimicrobial peptide influences control of cutaneous Leishmania infection","volume":"13","author":"Kulkarni MM","year":"2011","unstructured":"KulkarniMM. 2011. Mammalian antimicrobial peptide influences control of cutaneous Leishmania infection. Cell Microbiol. 13: 913\u2013923.","journal-title":"Cell Microbiol"},{"key":"e_1_3_2_21_2","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1111\/j.1365-2958.2006.05459.x","article-title":"The major surface-metalloprotease of the parasitic protozoan, Leishmania, protects against antimicrobial peptide-induced apoptotic killing","volume":"62","author":"Kulkarni MM","year":"2006","unstructured":"KulkarniMM. 2006. The major surface-metalloprotease of the parasitic protozoan, Leishmania, protects against antimicrobial peptide-induced apoptotic killing. Mol. Microbiol. 62: 1484\u20131497.","journal-title":"Mol. Microbiol"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M809079200"},{"key":"e_1_3_2_23_2","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.exppara.2007.07.011","article-title":"Trypanocidal and leishmanicidal activities of different antimicrobial peptides (AMPs) isolated from aquatic animals","volume":"118","author":"Lofgren SE","year":"2008","unstructured":"LofgrenSE MilettiLC SteindelM BachereE BarraccoMA. 2008. Trypanocidal and leishmanicidal activities of different antimicrobial peptides (AMPs) isolated from aquatic animals. Exp. Parasitol. 118: 197\u2013202.","journal-title":"Exp. Parasitol"},{"key":"e_1_3_2_24_2","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1007\/978-1-60761-594-1_25","article-title":"Characterization of the leishmanicidal activity of antimicrobial peptides","volume":"618","author":"Luque-Ortega JR","year":"2010","unstructured":"Luque-OrtegaJR RivasL. 2010. Characterization of the leishmanicidal activity of antimicrobial peptides. Methods Mol. Biol. 618: 393\u2013420.","journal-title":"Methods Mol. Biol"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1096\/fj.07-096081"},{"key":"e_1_3_2_26_2","doi-asserted-by":"crossref","first-page":"e1141","DOI":"10.1371\/journal.pntd.0001141","article-title":"Effect of BMAP-28 antimicrobial peptides on Leishmania major promastigote and amastigote growth: role of leishmanolysin in parasite survival","volume":"5","author":"Lynn MA","year":"2011","unstructured":"LynnMA. 2011. Effect of BMAP-28 antimicrobial peptides on Leishmania major promastigote and amastigote growth: role of leishmanolysin in parasite survival. PLoS Negl. Trop. Dis. 5: e1141.","journal-title":"PLoS Negl. Trop. Dis"},{"key":"e_1_3_2_27_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M410795200"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0169-4758(00)01637-9"},{"key":"e_1_3_2_29_2","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.exppara.2010.02.006","article-title":"Interactions of antimicrobial peptides with Leishmania and trypanosomes and their functional role in host parasitism","volume":"126","author":"McGwire BS","year":"2010","unstructured":"McGwireBS KulkarniMM. 2010. Interactions of antimicrobial peptides with Leishmania and trypanosomes and their functional role in host parasitism. Exp. Parasitol. 126: 397\u2013405.","journal-title":"Exp. Parasitol"},{"key":"e_1_3_2_30_2","doi-asserted-by":"publisher","DOI":"10.1086\/375747"},{"key":"e_1_3_2_31_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1742-4658.2009.07358.x"},{"key":"e_1_3_2_32_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-1759(83)90303-4"},{"key":"e_1_3_2_33_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(05)67629-5"},{"key":"e_1_3_2_34_2","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1016\/j.peptides.2011.01.011","article-title":"Leishmanicidal activity of synthetic antimicrobial peptides in an infection model with human dendritic cells","volume":"32","author":"Perez-Cordero JJ","year":"2011","unstructured":"Perez-CorderoJJ LozanoJM CortesJ DelgadoG. 2011. Leishmanicidal activity of synthetic antimicrobial peptides in an infection model with human dendritic cells. Peptides 32: 683\u2013690.","journal-title":"Peptides"},{"key":"e_1_3_2_35_2","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1093\/ecam\/neh033","article-title":"Antiprotozoan and antiviral activities of non-cytotoxic truncated and variant analogues of mussel defensin","volume":"1","author":"Roch P","year":"2004","unstructured":"RochP BeschinA BernardE. 2004. Antiprotozoan and antiviral activities of non-cytotoxic truncated and variant analogues of mussel defensin. Evidence Based Complement Alternat. Med. 1: 167\u2013174.","journal-title":"Evidence Based Complement Alternat. Med"},{"key":"e_1_3_2_36_2","first-page":"233","article-title":"Apoptosis in Leishmania species and its relevance to disease pathogenesis","volume":"123","author":"Shaha C","year":"2006","unstructured":"ShahaC. 2006. Apoptosis in Leishmania species and its relevance to disease pathogenesis. Indian J. Med. Res. 123: 233\u2013244.","journal-title":"Indian J. Med. Res"},{"key":"e_1_3_2_37_2","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1007\/978-0-387-76717-8_3","volume-title":"Programmed cell death in protozoa","author":"Soeiro MN","year":"2008","unstructured":"SoeiroMN SouzaEM. 2008. Programmed cell death and trypanosomatids: a brief review, p 24\u201338. In MartinJP (ed), Programmed cell death in protozoa. Landes Bioscience\/Springer Science\/Business Media, Rio de Janeiro, Brazil."},{"key":"e_1_3_2_38_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.64.5.1810-1818.1996"},{"key":"e_1_3_2_39_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.70.12.6524-6533.2002"},{"key":"e_1_3_2_40_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00935-08"},{"key":"e_1_3_2_41_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00018-010-0291-0"},{"key":"e_1_3_2_42_2","unstructured":"WHO. 2010. WHO technical report series: control of the leishmaniases.  Document 949. World Health Organization Geneva Switzerland."},{"key":"e_1_3_2_43_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.micpath.2004.11.002"},{"key":"e_1_3_2_44_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.00038-06"},{"key":"e_1_3_2_45_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0166-6851(03)00211-1"},{"key":"e_1_3_2_46_2","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.molbiopara.2004.03.010","article-title":"Multiple products of the Leishmania chagasi major surface protease (MSP or GP63) gene family","volume":"135","author":"Yao C","year":"2004","unstructured":"YaoC LuoJ StorlieP DonelsonJE WilsonME. 2004. Multiple products of the Leishmania chagasi major surface protease (MSP or GP63) gene family. Mol. Biochem. Parasitol. 135: 171\u2013183.","journal-title":"Mol. Biochem. Parasitol"},{"key":"e_1_3_2_47_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.46.12.3883-3891.2002"},{"key":"e_1_3_2_48_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.36.8.1665"},{"key":"e_1_3_2_49_2","doi-asserted-by":"publisher","DOI":"10.1124\/pr.55.1.2"},{"key":"e_1_3_2_50_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.48.11.4395-4404.2004"},{"key":"e_1_3_2_51_2","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1038\/sj.cdd.4401071","article-title":"Cell death in Leishmania induced by stress and differentiation: programmed cell death or necrosis?","volume":"9","author":"Zangger H","year":"2002","unstructured":"ZanggerH MottramJC FaselN. 2002. Cell death in Leishmania induced by stress and differentiation: programmed cell death or necrosis? Cell Death. Differ. 9: 1126\u20131139.","journal-title":"Cell Death. Differ"}],"container-title":["Antimicrobial Agents and Chemotherapy"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.05349-11","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/AAC.05349-11","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,21]],"date-time":"2022-02-21T22:26:20Z","timestamp":1645482380000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/AAC.05349-11"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,2]]},"references-count":50,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2012,2]]}},"alternative-id":["10.1128\/AAC.05349-11"],"URL":"https:\/\/doi.org\/10.1128\/aac.05349-11","relation":{},"ISSN":["0066-4804","1098-6596"],"issn-type":[{"value":"0066-4804","type":"print"},{"value":"1098-6596","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,2]]},"assertion":[{"value":"2011-07-21","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2011-11-16","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2012-01-20","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}