{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T01:31:41Z","timestamp":1790818301257,"version":"4.1.0"},"reference-count":43,"publisher":"National Academy of Sciences","issue":"33","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2013,8,13]]},"abstract":"<jats:p>\n                    Leishmaniasis, a parasitic disease caused by protozoa of the genus\n                    <jats:italic>Leishmania<\/jats:italic>\n                    , affects millions of people worldwide. Aminoglycosides are mostly known as highly potent, broad-spectrum antibiotics that exert their antibacterial activity by selectively targeting the decoding A site of the bacterial ribosome, leading to aberrant protein synthesis. Recently, some aminoglycosides have been clinically approved and are currently used worldwide for the treatment of leishmaniasis; however the molecular details by which aminoglycosides induce their deleterious effect on\n                    <jats:italic>Leishmaina<\/jats:italic>\n                    is still rather obscure. Based on high conservation of the decoding site among all kingdoms, it is assumed that the putative binding site of these agents in\n                    <jats:italic>Leishmania<\/jats:italic>\n                    is the ribosomal A site. However, although recent X-ray crystal structures of the bacterial ribosome in complex with aminoglycosides shed light on the mechanism of aminoglycosides action as antibiotics, no such data are presently available regarding their binding site in\n                    <jats:italic>Leishmania<\/jats:italic>\n                    . We present crystal structures of two different aminoglycoside molecules bound to a model of the\n                    <jats:italic>Leishmania<\/jats:italic>\n                    ribosomal A site: Geneticin (G418), a potent aminoglycoside for the treatment of leishmaniasis at a 2.65-\u00c5 resolution, and Apramycin, shown to be a strong binder to the leishmanial ribosome lacking an antileishmanial activity at 1.4-\u00c5 resolution. The structural data, coupled with in vitro inhibition measurements on two strains of\n                    <jats:italic>Leishmania<\/jats:italic>\n                    , provide insight as to the source of the difference in inhibitory activity of different Aminoglycosides. The combined structural and physiological data sets the ground for rational design of new, and more specific, aminoglycoside derivatives as potential therapeutic agents against leishmaniasis.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1307365110","type":"journal-article","created":{"date-parts":[[2013,7,30]],"date-time":"2013-07-30T00:11:18Z","timestamp":1375143078000},"page":"13333-13338","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":36,"title":["Identification of the molecular attributes required for aminoglycoside activity against\n                    <i>Leishmania<\/i>"],"prefix":"10.1073","volume":"110","author":[{"given":"Moran","family":"Shalev","sequence":"first","affiliation":[{"name":"Schulich Faculty of Chemistry, Technion\u2013Israel Institute of Technology, Haifa 32000, Israel;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiro","family":"Kondo","sequence":"additional","affiliation":[{"name":"Department of Materials and Life Sciences, Faculty of Science and Technology, Sophia University, Tokyo 102-8554, Japan; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dmitry","family":"Kopelyanskiy","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Molecular Genetics, Institute for Medical Research Israel\u2013Canada, Hebrew University\u2013Hadassah Medical School, Jerusalem 91120, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles L.","family":"Jaffe","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Molecular Genetics, Institute for Medical Research Israel\u2013Canada, Hebrew University\u2013Hadassah Medical School, Jerusalem 91120, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noam","family":"Adir","sequence":"additional","affiliation":[{"name":"Schulich Faculty of Chemistry, Technion\u2013Israel Institute of Technology, Haifa 32000, Israel;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Timor","family":"Baasov","sequence":"additional","affiliation":[{"name":"Schulich Faculty of Chemistry, Technion\u2013Israel Institute of Technology, Haifa 32000, Israel;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2013,7,29]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1038\/35030019","article-title":"Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics","volume":"407","author":"Carter AP","year":"2000","unstructured":"AP Carter, et al., Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. 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Nucleic Acids Res 33, 5677\u20135690 (2005).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.1002\/cmdc.200700113","article-title":"Crystal structure of the bacterial ribosomal decoding site complexed with a synthetic doubly functionalized paromomycin derivative: A new specific binding mode to an a-minor motif enhances in vitro antibacterial activity","volume":"2","author":"Kondo J","year":"2007","unstructured":"J Kondo, et al., Crystal structure of the bacterial ribosomal decoding site complexed with a synthetic doubly functionalized paromomycin derivative: A new specific binding mode to an a-minor motif enhances in vitro antibacterial activity. ChemMedChem 2, 1631\u20131638 (2007).","journal-title":"ChemMedChem"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1002\/cbic.200700271","article-title":"Differential selectivity of natural and synthetic aminoglycosides towards the eukaryotic and prokaryotic decoding A sites","volume":"8","author":"Kondo J","year":"2007","unstructured":"J Kondo, et al., Differential selectivity of natural and synthetic aminoglycosides towards the eukaryotic and prokaryotic decoding A sites. 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Blood Cells Mol Dis 38, 193\u2013198 (2007).","journal-title":"Blood Cells Mol Dis"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.jmb.2004.11.073","article-title":"Mutagenesis of 16S rRNA C1409-G1491 base-pair differentiates between 6\u2019OH and 6\u2019NH3+ aminoglycosides","volume":"346","author":"Pfister P","year":"2005","unstructured":"P Pfister, et al., Mutagenesis of 16S rRNA C1409-G1491 base-pair differentiates between 6\u2019OH and 6\u2019NH3+ aminoglycosides. J Mol Biol 346, 467\u2013475 (2005).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"2836","DOI":"10.1021\/jm801640k","article-title":"Development of novel aminoglycoside (NB54) with reduced toxicity and enhanced suppression of disease-causing premature stop mutations","volume":"52","author":"Nudelman I","year":"2009","unstructured":"I Nudelman, et al., Development of novel aminoglycoside (NB54) with reduced toxicity and enhanced suppression of disease-causing premature stop mutations. 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J Med Chem 52, 2243\u20132254 (2009).","journal-title":"J Med Chem"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"3735","DOI":"10.1016\/j.bmc.2010.03.060","article-title":"Repairing faulty genes by aminoglycosides: Development of new derivatives of geneticin (G418) with enhanced suppression of diseases-causing nonsense mutations","volume":"18","author":"Nudelman I","year":"2010","unstructured":"I Nudelman, et al., Repairing faulty genes by aminoglycosides: Development of new derivatives of geneticin (G418) with enhanced suppression of diseases-causing nonsense mutations. 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Exp Parasitol 130, 200\u2013204 (2012).","journal-title":"Exp Parasitol"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.molbiopara.2008.12.007","article-title":"Paromomycin: Uptake and resistance in Leishmania donovani","volume":"164","author":"Jhingran A","year":"2009","unstructured":"A Jhingran, B Chawla, S Saxena, MP Barrett, R Madhubala, Paromomycin: Uptake and resistance in Leishmania donovani. Mol Biochem Parasitol 164, 111\u2013117 (2009).","journal-title":"Mol Biochem Parasitol"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"e35671","DOI":"10.1371\/journal.pone.0035671","article-title":"Leishmaniasis worldwide and global estimates of its incidence","volume":"7","author":"Alvar J","year":"2012","unstructured":"J Alvar, et al., Leishmaniasis worldwide and global estimates of its incidence. PLoS ONE; WHO Leishmaniasis Control Team 7, e35671 (2012).","journal-title":"PLoS ONE"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"6265","DOI":"10.1093\/nar\/13.17.6265","article-title":"Suppression of a nonsense mutation in mammalian cells in vivo by the aminoglycoside antibiotics G-418 and paromomycin","volume":"13","author":"Burke JF","year":"1985","unstructured":"JF Burke, AE Mogg, Suppression of a nonsense mutation in mammalian cells in vivo by the aminoglycoside antibiotics G-418 and paromomycin. Nucleic Acids Res 13, 6265\u20136272 (1985).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"10630","DOI":"10.1021\/jm3012992","article-title":"Increased selectivity toward cytoplasmic versus mitochondrial ribosome confers improved efficiency of synthetic aminoglycosides in fixing damaged genes: A strategy for treatment of genetic diseases caused by nonsense mutations","volume":"55","author":"Kandasamy J","year":"2012","unstructured":"J Kandasamy, et al., Increased selectivity toward cytoplasmic versus mitochondrial ribosome confers improved efficiency of synthetic aminoglycosides in fixing damaged genes: A strategy for treatment of genetic diseases caused by nonsense mutations. 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