Erratum: Up-regulation of silent information regulator 2 (Sir2) is associated with amphotericin B resistance in clinical isolates of Leishmania donovani (Journal of Antimicrobial Chemotherapy (2015) 70: 5 (1343-1356) DOI: 10.1093/jac/dku534);Up-regulation of silent information regulator 2 (Sir2) is associated with amphotericin B resistance in clinical isolates of Leishmania donovani

Journal of Antimicrobial Chemotherapy

Volumn 70, Issue 5, 2014, Pages 1343-1356

  Purkait, Bidyut ^a   Singh, Ruby ^a   Wasnik, Kirti ^b   Das, Sushmita ^c   Kumar, Ashish ^a   Paine, Mark ^d   Dikhit, Manas ^a   Singh, Dharmendra ^a   Sardar, Abul H ^a   Ghosh, Ayan K ^a   Das, Pradeep ^a  

^a INDIAN COUNCIL OF MEDICAL RESEARCH   (India)

^b National Institute of Pharmaceutical Education and Research (NIPER)   (India)

^c ALL INDIA INSTITUTE OF MEDICAL SCIENCES   (India)

^d LIVERPOOL SCHOOL OF TROPICAL MEDICINE   (United Kingdom)

Author keywords

AmB resistance; Apoptosis; MDR1; ROS; Sir2; Visceral leishmaniasis

Indexed keywords

AMPHOTERICIN B; MESSENGER RNA; MULTIDRUG RESISTANCE PROTEIN 1; NICOTINAMIDE ADENINE DINUCLEOTIDE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SILENT INFORMATION REGULATOR PROTEIN 2; SIRTINOL; ANTIPROTOZOAL AGENT; MULTIDRUG RESISTANCE PROTEIN; SIRTUIN;

ALLELE; ANTIBIOTIC RESISTANCE; APOPTOSIS; ARTICLE; BIOSYNTHESIS; CROSS RESISTANCE; DIALYSIS; DNA DEGRADATION; DNA FRAGMENTATION; DRUG SENSITIVITY; ENZYME ACTIVITY; GENETIC MANIPULATION; HYDROGEN BOND; LD50; LEISHMANIA DONOVANI; MACROPHAGE; MOLECULAR DYNAMICS; MTT ASSAY; PARASITE LOAD; PARASITE SURVIVAL; PHENOTYPE; PROTEIN EXPRESSION; PURIFICATION; REAL TIME POLYMERASE CHAIN REACTION; UPREGULATION; WESTERN BLOTTING; DRUG EFFECTS; DRUG RESISTANCE; GENE EXPRESSION; GENE EXPRESSION PROFILING; GENE INACTIVATION; GENETICS; METABOLISM;

AMPHOTERICIN B; ANTIPROTOZOAL AGENTS; APOPTOSIS; DRUG RESISTANCE; GENE EXPRESSION; GENE EXPRESSION PROFILING; GENE KNOCKOUT TECHNIQUES; LEISHMANIA DONOVANI; P-GLYCOPROTEIN; REACTIVE OXYGEN SPECIES; SIRTUINS; UP-REGULATION;

EID: 84929751492     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dkad023     Document Type: Erratum

References (46)

1. World Health Organization. The World Health Report. http://www.who.int/whr/1998/en/whr98_en.pdf.
2. Sinha PK, Bimal S, Singh SK et al. Pre- & post-treatment evaluation of immunological features in Indian visceral leishmaniasis (VL) patients with HIV co-infection. Indian J Med Res 2006; 123: 197-202.
3. Jha TK, Giri YN, Singh TK et al. Use of amphotericin B in drug-resistant cases of visceral leishmaniasis in north Bihar, India. Am J Trop Med Hyg 1995; 52: 536-38.
4. Lemke A, Kiderlen AF, Kayser O. Amphotericin B. Appl Microbiol Biotechnol 2005; 68: 151-62.
5. Dutcher JD, Gold W, Pagano JF et al. Amphotericin B, its production and its salts. US Pat 1959; 2.908.611
6. Urbina JA, Cohen BE, Perozo E et al. Spin-labeled amphotericin B: synthesis, characterization, biological and spectroscopic properties. Biochim Biophys Acta 1987; 897: 467-73.
7. Lamy-Freund MT, Ferreira VFN, Schreier S. Mechanism of inactivation of the polyene antibiotic amphotericin B: evidence for radical formation in the process of autooxidation. J Antibiot 1985; 38: 753-7.
8. Srivastava P, Prajapati VK, Rai M et al. Unusual case of resistance to amphotericin B in Visceral Leishmaniasis in a region in India where Leishmaniasis is not endemic. J Clin Microbiol 2011; 49: 3088-91.
9. Purkait B, Kumar A, Nandi N et al. Mechanism of amphotericin B resistance in clinical isolates of Leishmania donovani. Antimicrob Agents Chemother 2012; 56: 1031-41.
10. Moreira W, Leprohon P, Ouellette M. Tolerance to drug-induced cell death favours the acquisition of multidrug resistance in Leishmania. Cell Death Dis 2011; 2, e201; doi:10.1038/cddis.83.
11. Brachmann CB, Sherman JM, Devine SE et al. The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev 1995; 9: 2888-902.
12. Imai S, Armstrong CM, Kaeberlein M et al. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 2000; 403: 795-800.
13. Zemzoumi K, Sereno D, Francois C et al. Leishmania major: cell type dependent distribution of a 43 kDa antigen related to silent information regulatory-2 protein family. Biol Cell 1998; 90: 239-45.
14. Frye RA. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem Biophys Res Commun 1999; 260: 273-9.
15. Frye RA. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 2000; 273: 793-8.
16. Yoshida M, Horinouchi S, Beppu T. Tricostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function. Bioessays 1995; 17: 423-30.
17. Tanny JC, Moazed D. Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: evidence for acetyl transfer from substrate to an NAD breakdown product. Proc Natl Acad Sci USA 2001; 98: 415-20.
18. Sauve AA, Celic I, Avalos J et al. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reaction. Biochem 2001; 40: 15456-63.
19. Garcia-Salcedo JA, Gijon P, Nolan DP et al. A chromosomal SIR2 homologue with both histone NAD-dependent ADP-ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei. EMBO J 2003; 22: 5851-62.
20. Tavares J, Ouaissi A, Santar'Em N et al. The Leishmania infantum cytosolic Sir2-related protein 1 (Lisir2rp1) is an NAD+-dependent deacetylase and ADP-ribosyltransferase. Biochem J 2008; 415: 377-86.
21. Vergnes B, Sereno D, Madjidian-Sereno N et al. Cytoplasmic SIR2 homologue overexpression promotes survival of Leishmania parasites by preventing programmed cell death. Gene 2002; 296: 139-50.
22. Shieh WM, Ame JC, Wilson MV et al. Poly(ADP-ribose) polymerase null mouse cells synthesize ADP-ribose polymers. J Biol Chem 1998; 273: 30069-72.
23. Smith S. TheworldaccordingtoPARP. Trends BiochemSci 2001; 26: 174-9.
24. Zhang J. Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked? BioEssays 2003; 25: 808-14.
25. Reverter-Branchat G, Cabiscol E, Tamarit J et al. Chronological and replicative life-span extension in Saccharomyces cerevisiae by increased dosage of alcohol dehydrogenase 1. Microbiology 2007; 153: 3667-76.
26. Oh WK, Cho KB, Hien TT et al. Amurensin G, a potent natural SIRT1 inhibitor, rescues doxorubicin responsiveness via down-regulation of multidrug resistance 1. Mol Pharmacol 2010; 78: 855-64.
27. Chu F, Chou PM, Zheng X et al. Control of multidrug resistance gene mdr1 and cancer resistance to chemotherapy by the longevity gene sirt1. Cancer Res 2005; 22: 10183-7.
28. Ashutosh, Gupta S, Ramesh et al. Use of Leishmania donovani field isolates expressing the luciferase reporter gene in in-vitro drug screening. Antimicrob Agents Chemother 2005; 49, 3776-83.
29. Dolai S, Yadav RK, Pal S et al. Leishmania major ascorbate peroxidase overexpression protects cells against reactive oxygen species-mediated cardiolipin oxidation. Free Radic Biol Med 2008; 45: 1520-9.
30. Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993; 234: 779-815.
31. Wiederstein M, Sippl MJ. ProSA-web: interactiveweb service for the recognition of errors in three-dimensional structures of proteins. Nucl Acids Res 1996; 35: 407-10.
32. Van Der Spoel D, Lindahl E, Hess B et al. GROMACS: fast, flexible, and free. J Comput Chem 2005; 26: 1701-18.
33. Ewald PP. Die Berechnung optischer und elektrostatischer Gitterpotentiale. Ann Phys 1921; 369: 253-87.
34. Rarey M, Kramer B, Lengauer T et al. A fast flexible docking method using an incremental construction algorithm. J Mol Biol 1996; 261: 470-89.
35. Jones G, Willett P, Glen RC et al. Development and validation of a genetic algorithm for flexible docking. J Mol Biol 1997; 267: 727-48.
36. Dolai S, Pal S, Yadav RK et al. Endoplasmic reticulum stress-induced apoptosis in Leishmania through Ca-dependent and caspase-independent Mmechanism. J Biol Chem 2011; 286: 13638-46.
37. Sardar AH, Das S, Agnihorti S et al. Spinigerin induces apoptotic like cell death in a caspase independent manner in Leishmania donovani. Expt Parasitol 2013; 135: 715-25.
38. Ashutosh, Garg M, Sundar S et al. Downregulation of mitogenactivated protein kinase 1 of Leishmania donovani field isolates is associated with antimony resistance. Antimicrob Agents Chemother 2012; 56: 518-25.
39. Cruz A, Coburn CM, Beverley SM. Double targeted gene replacement for creating null mutants. Proc Natl Acad Sci USA 1991; 88: 7170-4.
40. Vergnes B, Sereno D, Tavares J et al. Targeted disruption of cytosolic SIR2 deacetylase discloses its essential role in Leishmania survival and proliferation. Gene 2005; 363: 85-96.
41. Vergnes B, Vanhille L, Ouaissi A et al. Stage-specific antileishmanial activity of an inhibitor of SIR2 histone deacetylase. Acta Tropica 2005; 94: 107-15.
42. Stewart BW. Mechanisms of apoptosis: integration of genetic, biochemical, and cellular indicators. J Natl Cancer Inst 1994; 86: 1286-96.
43. Schlegel RA, Williamson P. Phosphatidylserine, a death knell. Cell Death Differ 2001; 8: 551-63.
44. Mishra J, Singh S. Miltefosine resistance in Leishmania donovani involves suppression of oxidative stress-induced programmed cell death. Exp Parasitol 2013; 135: 397-406.
45. Rajamohan SB, Pillai VB, Gupta M et al. SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1. Mol Cellular Biol 2009; 29: 4116-29.
46. Quaissi M, Quaissi A. Histone deacetylase enzymes as potential drug targets in cancer and parasitic diseases. J Biomed Biotechnol 2006; 2006: 13474.