From genome to antivirals: SARS as a test tube

Drug Discovery Today

Volumn 10, Issue 5, 2005, Pages 345-352

  Kliger, Yossef ^a   Levanon, Erez Y ^a   Gerber, Doron ^a  

^a Compugen ^*  (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

1 BENZOYL 4 [(4,7 DIMETHOXY 1H PYRROLO[2,3 C]PYRIDIN 3 YL)OXOACETYL]PIPERAZINE; ANTIVIRUS AGENT; CD4 IMMUNOGLOBULIN G2; CHEMOKINE RECEPTOR CCR5; CYTIDINE DERIVATIVE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; DNA VACCINE; ENFUVIRTIDE; ENZYME INHIBITOR; NUCLEOSIDE ANALOG; PROTEIN INHIBITOR; PROTEINASE INHIBITOR; RECEPTOR BLOCKING AGENT; RECOMBINANT PROTEIN; RIBAVIRIN; RNA DIRECTED DNA POLYMERASE INHIBITOR; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; VIRUS ENZYME; VIRUS VACCINE; ZIDOVUDINE;

ANTIVIRAL ACTIVITY; CLINICAL TRIAL; DRUG DESIGN; DRUG TARGETING; GENE SILENCING; GENOME; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS; LIFE CYCLE; MEMBRANE FUSION; NONHUMAN; PLASMID; PROTEIN PROCESSING; RECEPTOR BINDING; RECEPTOR BLOCKING; REVIEW; RNA PROCESSING; SEVERE ACUTE RESPIRATORY SYNDROME; VIRUS GENE; VIRUS INFECTION;

ANIMALS; ANTIVIRAL AGENTS; GENOME, VIRAL; HUMANS; SARS VIRUS; SEVERE ACUTE RESPIRATORY SYNDROME;

EID: 14644406266     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(04)03320-3     Document Type: Review

References (78)

1. Ksiazek T.G., et al. A novel coronavirus associated with severe acute respiratory syndrome. N. Engl. J. Med. 348:2003;1953-1966
2. Drosten C., et al. Identification of a novel coronavirus in patients with severe acute respiratory syndrome. N. Engl. J. Med. 348:2003;1967-1976
3. Peiris J.S., et al. Coronavirus as a possible cause of severe acute respiratory syndrome. Lancet. 361:2003;1319-1325
4. Vabret A., et al. An outbreak of coronavirus OC43 respiratory infection in Normandy, France. Clin. Infect. Dis. 36:2003;985-989
5. Marra M.A., et al. The Genome sequence of the SARS-associated coronavirus. Science. 300:2003;1399-1404
6. Rota P.A., et al. Characterization of a novel coronavirus associated with severe acute respiratory syndrome. Science. 300:2003;1394-1399
7. Sainz B. Jr, et al. Interferon-beta and interferon-gamma synergistically inhibit the replication of severe acute respiratory syndrome-associated coronavirus (SARS-CoV). Virology. 329:2004;11-17
8. Fujii T., et al. Current concepts in SARS treatment. J. Infect. Chemother. 10:2004;1-7
9. Barre-Sinoussi F., et al. Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS). Science. 220:1983;868-871
10. Gallo R.C., et al. Frequent detection and isolation of cytopathic retroviruses (HTLV-III) from patients with AIDS and at risk for AIDS. Science. 224:1984;500-503
11. Muesing M.A., et al. Nucleic acid structure and expression of the human AIDS/lymphadenopathy retrovirus. Nature. 313:1985;450-458
12. Richman D.D. Zidovudine resistance of human immunodeficiency virus. Rev. Infect. Dis. 12:(Suppl. 5):1990;507-S510
13. Matthews T., et al. Enfuvirtide: the first therapy to inhibit the entry of HIV-1 into host CD4 lymphocytes. Nat. Rev. Drug Discov. 3:2004;215-225
14. Berger B., Singh M. An iterative method for improved protein structural motif recognition. J. Comput. Biol. 4:1997;261-273
15. Singh M., et al. LearnCoil-VMF: computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins. J. Mol. Biol. 290:1999;1031-1041
16. Klatzmann D., et al. T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV. Nature. 312:1984;767-768
17. Dalgleish A.G., et al. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature. 312:1984;763-767
18. Feng Y., et al. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science. 272:1996;872-877
19. Alkhatib G., et al. CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1. Science. 272:1996;1955-1958
20. Samson M., et al. Resistance to HIV-1 infection in caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene. Nature. 382:1996;722-725
21. Li W., et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature. 426:2003;450-454
22. Sui J., et al. Potent neutralization of severe acute respiratory syndrome (SARS) coronavirus by a human mAb to S1 protein that blocks receptor association. Proc. Natl. Acad. Sci. U. S. A. 101:2004;2536-2541
23. Huentelman M.J., et al. Structure-based discovery of a novel angiotensin-converting enzyme 2 inhibitor. Hypertension. 44:2004;903-906
24. Wong S.K., et al. A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2. J. Biol. Chem. 279:2004;3197-3201
25. Jeffers S.A., et al. CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus. Proc. Natl. Acad. Sci. U. S. A. 101:2004;15748-15753
26. Gallo S.A., et al. The HIV Env-mediated fusion reaction. Biochim. Biophys. Acta. 1614:2003;36-50
27. Gallo S.A., et al. HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process. Biochemistry. 40:2001;12231-12236
28. Reeves J.D., et al. Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics. Proc. Natl. Acad. Sci. U. S. A. 99:2002;16249-16254
29. Reeves J.D., et al. Impact of mutations in the coreceptor binding site on human immunodeficiency virus type 1 fusion, infection, and entry inhibitor sensitivity. J. Virol. 78:2004;5476-5485
30. Tremblay C.L., et al. Anti-human immunodeficiency virus interactions of SCH-C (SCH 351125), a CCR5 antagonist, with other antiretroviral agents in vitro. Antimicrob. Agents Chemother. 46:2002;1336-1339
31. Tremblay C.L., et al. Strong in vitro synergy between the fusion inhibitor T-20 and the CXCR4 blocker AMD-3100. J. Acquir. Immune Defic. Syndr. 25:2000;99-102
32. Nagashima K.A., et al. Human immunodeficiency virus type 1 entry inhibitors PRO 542 and T-20 are potently synergistic in blocking virus-cell and cell-cell fusion. J. Infect. Dis. 183:2001;1121-1125
33. Blumenthal R., et al. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events. J. Cell Biol. 135:1996;63-71
34. Mittal A., et al. Kinetics of influenza hemagglutinin-mediated membrane fusion as a function of technique. Anal. Biochem. 303:2002;145-152
35. Mittal A., et al. Kinetically differentiating influenza hemagglutinin fusion and hemifusion machines. Biophys. J. 85:2003;1713-1724
36. Markosyan R.M., et al. Evolution of intermediates of influenza virus hemagglutinin-mediated fusion revealed by kinetic measurements of pore formation. Biophys. J. 80:2001;812-821
37. Markosyan R.M., et al. HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation. Mol. Biol. Cell. 14:2003;926-938
38. Ng M.L., et al. Early events of SARS coronavirus infection in vero cells. J. Med. Virol. 71:2003;323-331
39. Kliger Y., Levanon E.Y. Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy. BMC Microbiol. 3:2003;20
40. Liu S., et al. Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors. Lancet. 363:2004;938-947
41. Yuan K., et al. Suppression of SARS-CoV entry by peptides corresponding to heptad regions on spike glycoprotein. Biochem. Biophys. Res. Commun. 319:2004;746-752
42. Zhu J., et al. Following the rule: formation of the 6-helix bundle of the fusion core from severe acute respiratory syndrome coronavirus spike protein and identification of potent peptide inhibitors. Biochem. Biophys. Res. Commun. 319:2004;283-288
43. Simmons G., et al. Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry. Proc. Natl. Acad. Sci. U. S. A. 101:2004;4240-4245
44. Ingallinella P., et al. Structural characterization of the fusion-active complex of severe acute respiratory syndrome (SARS) coronavirus. Proc. Natl. Acad. Sci. U. S. A. 101:2004;8709-8714
45. Xu Y., et al. Crystal structure of SARS-CoV spike protein fusion core. J. Biol. Chem. 279:2004;49414-49419
46. Tripet B., et al. Structural characterization of the SARS-coronavirus spike S fusion protein core. J. Biol. Chem. 279:2004;20836-20849
47. Bosch B.J., et al. Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides. Proc. Natl. Acad. Sci. U. S. A. 101:2004;8455-8460
48. Pastey M.K., et al. A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3. Nat. Med. 6:2000;35-40
49. Snijder E.J., et al. Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage. J. Mol. Biol. 331:2003;991-1004
50. Thiel V., et al. Mechanisms and enzymes involved in SARS coronavirus genome expression. J. Gen. Virol. 84:2003;2305-2315
51. Tanner J.A., et al. The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5′ to 3′ viral helicases. J. Biol. Chem. 278:2003;39578-39582
52. Wu C.Y., et al. Small molecules targeting severe acute respiratory syndrome human coronavirus. Proc. Natl. Acad. Sci. U. S. A. 101:2004;10012-10017
53. Koolen M.J., et al. Immunogenic peptide comprising a mouse hepatitis virus A59 B-cell epitope and an influenza virus T-cell epitope protects against lethal infection. J. Virol. 64:1990;6270-6273
54. Takamura K., et al. Field study of bovine coronavirus vaccine enriched with hemagglutinating antigen for winter dysentery in dairy cows. Can. J. Vet. Res. 66:2002;278-281
55. Bisht H., et al. Severe acute respiratory syndrome coronavirus spike protein expressed by attenuated vaccinia virus protectively immunizes mice. Proc. Natl. Acad. Sci. U. S. A. 101:2004;6641-6646
56. Yang Z.Y., et al. A DNA vaccine induces SARS coronavirus neutralization and protective immunity in mice. Nature. 428:2004;561-564
57. McCaffrey A.P., et al. Inhibition of hepatitis B virus in mice by RNA interference. Nat. Biotechnol. 21:2003;639-644
58. Zhang R., et al. Inhibiting severe acute respiratory syndrome-associated coronavirus by small interfering RNA. Chin Med J (Engl). 116:2003;1262-1264
59. Zhang X.W., Yap Y.L. Old drugs as lead compounds for a new disease? Binding analysis of SARS coronavirus main proteinase with HIV, psychotic and parasite drugs. Bioorg. Med. Chem. 12:2004;2517-2521
60. Wang Z., et al. Inhibition of severe acute respiratory syndrome virus replication by small interfering RNAs in mammalian cells. J. Virol. 78:2004;7523-7527
61. Sledz C.A., et al. Activation of the interferon system by short-interfering RNAs. Nat. Cell Biol. 5:2003;834-839
62. Opalinska J.B., Gewirtz A.M. Nucleic-acid therapeutics: basic principles and recent applications. Nat. Rev. Drug Discov. 1:2002;503-514
63. Yeh S.H., et al. Characterization of severe acute respiratory syndrome coronavirus genomes in Taiwan: Molecular epidemiology and genome evolution. Proc. Natl. Acad. Sci. U. S. A. 101:2004;2542-2547
64. Chinese S.M.E.C. Molecular evolution of the SARS coronavirus during the course of the SARS epidemic in China. Science. 303:2004;1666-1669
65. von Grotthuss M., et al. mRNA cap-1 methyltransferase in the SARS genome. Cell. 113:2003;701-702
66. Ivanov K.A., et al. Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase. J. Virol. 78:2004;5619-5632
67. Kao R.Y., et al. Identification of novel small-molecule inhibitors of severe acute respiratory syndrome-associated coronavirus by chemical genetics. Chem. Biol. 11:2004;1293-1299
68. Xu X., et al. Molecular model of SARS coronavirus polymerase: implications for biochemical functions and drug design. Nucleic Acids Res. 31:2003;7117-7130
69. Barnard D.L., et al. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARSCoV) by calpain inhibitors and beta-D-N4-hydroxycytidine. Antivir. Chem. Chemother. 15:2004;15-22
70. Chen F., et al. In vitro susceptibility of 10 clinical isolates of SARS coronavirus to selected antiviral compounds. J. Clin. Virol. 31:2004;69-75
71. Leong H.N., et al. Investigational use of ribavirin in the treatment of severe acute respiratory syndrome, Singapore, 2003. Trop. Med. Int. Health. 9:2004;923-927
72. Wang W.K., et al. Temporal relationship of viral load, ribavirin, interleukin (IL)-6, IL-8, and clinical progression in patients with severe acute respiratory syndrome. Clin. Infect. Dis. 39:2004;1071-1075
73. Anand K., et al. Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science. 300:2003;1763-1767
74. Yang H., et al. The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor. Proc. Natl. Acad. Sci. U. S. A. 100:2003;13190-13195
75. Hillisch A., et al. Utility of homology models in the drug discovery process. Drug Discov. Today. 9:2004;659-669
76. Kao R.Y., et al. Characterization of SARS-CoV main protease and identification of biologically active small molecule inhibitors using a continuous fluorescence-based assay. FEBS Lett. 576:2004;325-330
77. Blanchard J.E., et al. High-Throughput Screening Identifies Inhibitors of the SARS Coronavirus Main Proteinase. Chem. Biol. 11:2004;1445-1453
78. Yamamoto N., et al. HIV protease inhibitor nelfinavir inhibits replication of SARS-associated coronavirus. Biochem. Biophys. Res. Commun. 318:2004;719-725