A powerful yeast-based screening assay for the identification of inhibitors of indoleamine 2,3-dioxygenase

Journal of Biomolecular Screening

Volumn 17, Issue 10, 2012, Pages 1362-1371

  Cerejo, Marta ^a,b   Andrade, Gonçalo ^a   Roca, Christophe ^b   Sousa, José ^c   Rodrigues, Cátia ^a   Pinheiro, Ricardo ^a   Chatterjee, Sukalyan ^a,d   Vieira, Helena ^a   Calado, Patrícia ^a  

^a UNIVERSITY OF LISBON   (Portugal)

^b UNIVERSIDADE NOVA DE LISBOA   (Portugal)

^c Universidade Nova de Lisboa ^*  (Portugal)

^d UNIVERSITY OF COIMBRA   (Portugal)

Author keywords

high throughput screen; IDO inhibitors; predictivity; stringency; yeast based assay

Indexed keywords

INDOLEAMINE 2,3 DIOXYGENASE INHIBITOR; KYNURENINE; TRYPTOPHAN;

ARTICLE; AUTOMATION; CELL ACTIVITY; CELL DEATH; CELL GROWTH; CELL METABOLISM; CONTROLLED STUDY; DRUG DEVELOPMENT; DRUG POTENCY; DRUG SCREENING; ENZYME ACTIVITY; ENZYME INHIBITION; FUNGAL STRAIN; HUMAN; HUMAN CELL; IN VITRO STUDY; LIVER TOXICITY; PEPTIDE LIBRARY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; YEAST;

ANIMALS; CELL LINE, TUMOR; CERCOPITHECUS AETHIOPS; COS CELLS; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME INHIBITORS; GENE EXPRESSION; HIGH-THROUGHPUT SCREENING ASSAYS; HUMANS; INDOLEAMINE-PYRROLE 2,3,-DIOXYGENASE; SACCHAROMYCES CEREVISIAE;

EUKARYOTA; MAMMALIA;

EID: 84869071830     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057112452595     Document Type: Article

References (30)

1. Shimizu T., Nomiyama S., Hirata F., Hayaishi O.. Indoleamine 2,3-Dioxygenase: Purification and Some Properties. J. Biol. Chem. 1978 ; 253: 4700-4706
2. Dai X., Zhu B.T.. Indoleamine 2,3-Dioxygenase Tissue Distribution and Cellular Localization in Mice: Implications for Its Biological Functions. J. Histochem. Cytochem. 2010 ; 58: 17-28
3. Tan P.H., Bharath A.K.. Manipulation of Indoleamine 2,3 Dioxygenase: A Novel Therapeutic Target for Treatment of Diseases. Expert. Opin. Ther. Targets. 2009 ; 13: 987-1012
4. Prendergast G.C., Chang M.Y., Mandik-Nayak L., Metz R., Muller A.J.. Indoleamine 2,3-Dioxygenase as a Modifier of Pathogenic Inflammation in Cancer and Other Inflammation-Associated Diseases. Curr. Med. Chem. 2011 ; 18: 2257-2262
5. Di PucchioT.DaneseS.De CristofaroR.RutellaS.Inhibitors of Indoleamine 2,3-Dioxygenase: A Review of Novel Patented Lead Compounds. Expert Opin. Ther. Pat. 2010, 20, 229-250.
6. Scott G.N., DuHadaway J., Pigott E., Ridge N., Prendergast G.C., Muller A.J., Mandik-Nayak L.. The Immunoregulatory Enzyme IDO Paradoxically Drives B Cell-Mediated Autoimmunity. J. Immunol. 2009 ; 182: 7509-7517
7. Mohib K., Wang S., Guan Q., Mellor A.L., Sun H., Du C., Jevnikar A.M.. Indoleamine 2,3-Dioxygenase Expression Promotes Renal Ischemia-Reperfusion Injury. Am. J. Physiol. Renal Physiol. 2008 ; 295: F226 - F234
8. Jung I.D., Lee M.G., Chang J.H., Lee J.S., Jeong Y.I., Lee C.M., Park W.S., Han J., Seo S.K., Lee S.Y., et al. Blockade of Indoleamine 2,3-Dioxygenase Protects Mice against Lipopolysaccharide-Induced Endotoxin Shock. J. Immunol. 2009 ; 182: 3146-3154
9. Boasso A., Vaccari M., Fuchs D., Hardy A.W., Tsai W.P., Tryniszewska E., Shearer G.M., Franchini G.. Combined Effect of Antiretroviral Therapy and Blockade of IDO in SIV-Infected Rhesus Macaques. J. Immunol. 2009 ; 182: 4313-4320
10. Xu H., Oriss T.B., Fei M., Henry A.C., Melgert B.N., Chen L., Mellor A.L., Munn D.H., Irvin C.G., Ray P., et al. Indoleamine 2,3-Dioxygenase in Lung Dendritic Cells Promotes Th2 Responses and Allergic Inflammation. Proc. Natl. Acad. Sci. U. S. A. 2008 ; 105: 6690-6695
11. Muller A.J., DuHadaway J.B., Donover P.S., Sutanto-Ward E., Prendergast G.C.. Inhibition of Indoleamine 2,3-Dioxygenase, an Immunoregulatory Target of the Cancer Suppression Gene Bin1, Potentiates Cancer Chemotherapy. Nat. Med. 2005 ; 11: 312-319
12. Baban B., Chandler P., McCool D., Marshall B., Munn D.H., Mellor A.L.. Indoleamine 2,3-Dioxygenase Expression Is Restricted to Fetal Trophoblast Giant Cells during Murine Gestation and Is Maternal Genome Specific. J. Reprod. Immunol. 2004 ; 61: 67-77
13. Jia L., Schweikart K., Tomaszewski J., Page J.G., Noker P.E., Buhrow S.A., Reid J.M., Ames M.M., Munn D.H.. Toxicology and Pharmacokinetics of 1-Methyl-d-tryptophan: Absence of Toxicity Due to Saturating Absorption. Food Chem. Toxicol. 2008 ; 46: 203-211
14. Littlejohn T.K., Takikawa O., Skylas D., Jamie J.F., Walker M.J., Truscott R.J.. Expression and Purification of Recombinant Human Indoleamine 2, 3-Dioxygenase. Protein Expr. Purif. 2000 ; 19: 22-29
15. Tenreiro S., Outeiro T.F.. Simple Is Good: Yeast Models of Neurodegeneration. FEMS Yeast Res. 2010 ; 10: 970-979
16. Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Bécam A.M., Rytka J., Herbert C.J.. Aerobic and Anaerobic NAD+ Metabolism in Saccharomyces cerevisiae. FEBS Lett. 2002 ; 517: 97-102
17. Gietz R.D., Schiestl R.H.. Applications of High Efficiency Lithium Acetate Transformation of Intact Yeast Cells Using Single-Stranded Nucleic Acids as Carrier. Yeast. 1991 ; 7: 253-263
18. Scherer S., Davis R. W.. Replacement of Chromosome Segments with Altered DNA Sequences Constructed In Vitro. Proc. Natl. Acad. Sci. U.S.A. 1979 ; 76: 4951-4955
19. Zhang J.H., Chung T.D., Oldenburg K.R.. A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays. J. Biomol. Screen. 1999 ; 4: 67-73
20. Sanni L.A., Thomas S.R., Tattam B.N., Moore D.E., Chaudhri G., Stocker R., Hunt N.H.. Dramatic Changes in Oxidative Tryptophan Metabolism along the Kynurenine Pathway in Experimental Cerebral and Noncerebral Malaria. Am. J. Pathol. 1998 ; 152: 611-619
21. Vottero E., Balgi A., Woods K., Tugendreich S., Melese T., Andersen R.J., Mauk A.G., Roberge M.. Inhibitors of Human Indoleamine 2,3-Dioxygenase Identified with a Target-Based Screen in Yeast. Biotechnol. J. 2006 ; 1: 282-288
22. Delle Fratte S., Piubelli C., Domenici E.. Development of a High-Throughput Scintillation Proximity Assay for the Identification of C-domain Translational Initiation Factor 2 Inhibitors. J. Biomol. Screen. 2002 ; 7: 541-546
23. Sun C., Newbatt Y., Douglas L., Workman P., Aherne W., Linardopoulos S.. High-Throughput Screening Assay for Identification of Small Molecule Inhibitors of Aurora2/STK15 Kinase. J. Biomol. Screen. 2004 ; 9: 391-397
24. Kolaczkowski M., Kolaczowska A., Luczynski J., Witek S., Goffeau A.. n Vivo Characterization of the Drug Resistance Profile of the Major ABC Transporters and Other Components of the Yeast Pleiotropic Drug Resistance Network. Microb. Drug Resist. 1998 ; 4: 143-158
25. Kaur R., Bachhawat A.K.. The Yeast Multidrug Resistance Pump, Pdr5p, Confers Reduced Drug Resistance in erg Mutants of Saccharomyces cerevisiae. Microbiology. 1999 ; 145: 809-818
26. Perkins E., Sun D., Nguyen A., Tulac S., Francesco M., Tavana H., Nguyen H., Tugendreich S., Barthmaier P., Couto J., et al. Novel Inhibitors of Poly(ADP-ribose) Polymerase/PARP1 and PARP2 Identified Using a Cell-Based Screen in Yeast. Cancer Res. 2001 ; 61: 4175-4183
27. Gutierrez-Lugo M.T., Baker H., Shiloach J., Boshoff H., Bewley C.A.. Dequalinium, a New Inhibitor of Mycobacterium tuberculosis Mycothiol Ligase Identified by High-Throughput Screening. J. Biomol. Screen. 2009 ; 14: 643-652
28. Falk H., Connor T., Yang H., Loft K.J., Alcindor J.L., Nikolakopoulos G., Surjadi R.N., Bentley J.D., Hattarki M.K., Dolezal O., et al. An Efficient High-Throughput Screening Method for MYST Family Acetyltransferases, a New Class of Epigenetic Drug Targets. J. Biomol. Screen. 2011 ; 16: 1196-1205
29. Mezna M., Wong A.C., Ainger M., Scott R.W., Hammonds T., Olson M.F.. Development of a High-Throughput Screening Method for LIM Kinase 1 Using a Luciferase-Based Assay of ATP Consumption. J. Biomol. Screen. 2012 ; 17 (4). 460-468
30. Andrews B.J., Turchi J.J.. Development of a High-Throughput Screen for Inhibitors of Replication Protein A and Its Role in Nucleotide Excision Repair. Mol. Cancer Ther. 2004 ; 3: 385-391