Thiopurine analogue inhibitors of severe acute respiratory syndrome-coronavirus papain-like protease, a deubiquitinating and deISGylating enzyme

Antiviral Chemistry and Chemotherapy

Volumn 19, Issue 4, 2009, Pages 151-156

  Chen, Xin ^a   Chou, Chi Yuan ^b   Chang, Gu Gang ^b  

^a NATIONAL HEALTH RESEARCH INSTITUTES   (Taiwan)

^b NATIONAL YANG MING UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

AZATHIOPRINE; CYSTEINE PROTEINASE; MERCAPTOPURINE; PAPAIN LIKE PROTEASE; TIOGUANINE; UNCLASSIFIED DRUG; VIRUS ENZYME; 3C LIKE PROTEASE, SARS CORONAVIRUS; 3C-LIKE PROTEASE, SARS CORONAVIRUS; PROTEINASE INHIBITOR; VIRUS PROTEIN;

ACUTE LYMPHOBLASTIC LEUKEMIA; ACUTE MYELOBLASTIC LEUKEMIA; CANCER CHEMOTHERAPY; CORONAVIRUS; DRUG EFFECT; DRUG INHIBITION; DRUG MECHANISM; DRUG RECEPTOR BINDING; DRUG STRUCTURE; ENTERITIS; ENZYME ACTIVITY; ENZYME STRUCTURE; HUMAN; MOLECULAR DOCKING; NONHUMAN; PRIORITY JOURNAL; REVIEW; RHEUMATOID ARTHRITIS; SEVERE ACUTE RESPIRATORY SYNDROME; STRUCTURE ACTIVITY RELATION; SYSTEMIC LUPUS ERYTHEMATOSUS; UBIQUITINATION; ARTICLE; CHEMISTRY; DRUG ANTAGONISM; ENZYMOLOGY; SARS CORONAVIRUS; VIROLOGY;

6-MERCAPTOPURINE; CYSTEINE ENDOPEPTIDASES; HUMANS; PROTEASE INHIBITORS; SARS VIRUS; SEVERE ACUTE RESPIRATORY SYNDROME; THIOGUANINE; VIRAL PROTEINS;

EID: 65549141218     PISSN: 09563202     EISSN: None     Source Type: Journal    
DOI: 10.1177/095632020901900402     Document Type: Review

References (41)

1. Chou CY, Chien CH, Han YS, et al. Thiopurine analogues inhibit papain-like protease of severe acute respiratory syndrome coronavirus. Biochem Pharmacol 2008; 75:1601-1609.
2. Elion GB. The purine path to chemotherapy. Science 1989; 244:41-47.
3. Pui CH, Evans WE. Acute lymphoblastic leukemia. N Engl J Med 1998; 339:605-615.
4. O'Connor KA, Roth BL. Finding new tricks for old drugs: an efficient route for public-sector drug discovery. Nat Rev Drug Discov 2005; 4:1005-1014.
5. Harcourt BH, Jukneliene D, Kanjanahaluethai A, et al. Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity. J Virol 2004; 78:13600-13612.
6. Han YS, Chang GG, Juo CG, et al. Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV): expression, purification, characterization, and inhibition. Biochemistry 2005; 44:10349-10359.
7. Karran P, Attard N. Thiopurines in current medical practice: molecular mechanisms and contributions to therapy-related cancer. Nat Rev Cancer 2008; 8:24-36.
8. Barretto N, Jukneliene D, Ratia K, et al. The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity. J Virol 2005; 79:15189-15198. (Pubitemid 43032301)
9. Lindner HA, Fotouhi-Ardakani N, Lytvyn V, et al. The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme. J Virol 2005; 79:15199-15208. (Pubitemid 43032302)
10. Lindner HA, Lytvyn V, Qi H, et al. Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus papain-like protease. Arch Biochem Biophys 2007; 466:8-14. (Pubitemid 47405070)
11. Sadler AJ, Williams BR. Interferon-inducible antiviral effectors. Nat Rev Immunol 2008; 8:559-568.
12. Ritchie KJ, Hahn CS, Kim KI, et al. Role of ISG15 protease UBP43 (USP18) in innate immunity to viral infection. Nat Med 2004; 10:1374-1378.
13. Osiak A, Utermöhlen O, Niendorf S, Horak J, Knobeloch KP. ISG15, an interferon-stimulated ubiquitin-like protein, is not essential for STAT1 signalling and responses against vesicular stomatitis and lymphocytic choriomeningitis virus. Mol Cell Biol 2005; 25:6338-6345. (Pubitemid 41023211)
14. Lenschow DJ, Giannakopoulos NV, Gunn LJ, et al. Identification of interferon-stimulated gene 15 as an antiviral molecule during Sindbis virus infection in vivo. J Virol 2005; 79:13974-13983.
15. Lenschow DJ, Lai C, Frias-Staheli N, et al. IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses. Proc Natl Acad Sci U S A 2007; 104:1371-1376. (Pubitemid 46184011)
16. Ratia K, Saikatendu KS, Santarsiero BD, et al. Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme. Proc Natl Acad Sci U S A 2006; 103:5717-5722.
17. Hochstrasser M. Ubiquitin-dependent protein degradation. Annu Rev Genet 1996; 30:405-439.
18. Chung CH, Baek SH. Deubiquitinating enzymes: their diversity and emerging roles. Biochem Biophys Res Commun 1999; 266:633-640.
19. Wilkinson KD. Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB J 1997; 11:1245-1256.
20. Nijman SM, Luna-Vargas MP, Velds A, et al. A genomic and functional inventory of deubiquitinating enzymes. Cell 2005; 123:773-786. (Pubitemid 41721026)
21. Nicholson B, Marblestone JG, Butt TR, Mattern MR. Deubiquitinating enzymes as novel anticancer targets. Future Oncol 2007; 3:191-199. (Pubitemid 46592727)
22. Guédat P, Colland F. Patented small molecule inhibitors in the ubiquitin proteasome system. BMC Biochem 2007; 8 Suppl 1:S14. (Pubitemid 351813994)
23. Love KR, Catic A, Schlieker C, Ploegh HL. Mechanisms, biology and inhibitors of deubiquitinating enzymes. Nat Chem Biol 2007; 3:697-705. (Pubitemid 47609116)
24. Hershko A, Rose IA. Ubiquitin-aldehyde: a general inhibitor of ubiquitin-recycling processes. Proc Natl Acad Sci U S A 1987; 84:1829-1833. (Pubitemid 17054106)
25. Pickart CM, Cohen RE. Proteasomes and their kin: proteases in the machine age. Nat Rev Mol Cell Biol 2004; 5:177-187.
26. Catic A, Fiebiger E, Korbel GA, Blom D, Galardy PJ, Ploegh HL. Screen for ISG15-crossreactive deubiquitinases. PLoS One 2007; 2:e679.
27. Malakhov MP, Malakhova OA, Kim KI, Ritchie KJ, Zhang DE. UBP43 (USP18) specifically removes ISG15 from conjugated proteins. J Biol Chem 2002; 277:9976-9981.
28. Frias-Staheli N, Giannakopoulos NV, Kikkert M, et al. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe 2007; 2:404-416. (Pubitemid 350225347)
29. Lindner HA. Deubiquitination in virus infection. Virology 2007; 362:245-256.
30. Krissinel E, Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 2004; 60:2256-2268. (Pubitemid 41742778)
31. Hu M, Li P, Li M, et al. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 2002; 111:1041-1054. (Pubitemid 36050118)
32. Hu M, Li P, Song L, et al. Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. EMBO J 2005; 24:3747-3756. (Pubitemid 41581691)
33. Renatus M, Parrado SG, D'Arcy A, et al. Structural basis of ubiquitin recognition by the deubiquitinating protease USP2. Structure 2006; 14:1293-1302. (Pubitemid 44176373)
34. Komander D, Barford D. Structure of the A20 OTU domain and mechanistic insights into deubiquitination. Biochem J 2008; 409:77-85.
35. Komander D, Lord CJ, Scheel H, et al. The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. Mol Cell 2008; 29:451-464. (Pubitemid 351282537)
36. Avvakumov GV, Walker JR, Xue S, et al. Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J Biol Chem 2006; 281:38061-38070. (Pubitemid 46042109)
37. Schlieker C, Weihofen WA, Frijns E, Kattenhorn LM, Gaudet R, Ploegh HL. Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes. Mol Cell 2007; 25:677-687. (Pubitemid 46341922)
38. Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution. EMBO J 1997; 16:3787-3796. (Pubitemid 27280994)
39. Nicholson B, Leach CA, Goldenberg SJ, et al. Characterization of ubiquitin and ubiquitin-like-protein isopeptidase activities. Protein Sci 2008; 17:1035-1043. (Pubitemid 351749209)
40. Roberts A, Lamirande EW, Vogel L, et al. Animal models and vaccines for SARS-CoV infection. Virus Res 2008; 133:20-32. (Pubitemid 351374756)
41. Chernova TA, Allen KD, Wesoloski LM, Shanks JR, Chernoff YO, Wilkinson KD. Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. J Biol Chem 2003; 278:52102-52115.