Recent advances in the development of human rhinovirus 3C protease inhibitors

Bibliography

• COUCH RB: Rhinoviruses. In: Fields Virology, 3rd Ed. (Volume 1). Fields BN, Knipe DM, Howley PM et al. (Eds.), Lippincott-Raven Publishers, Philadelphia, USA (1996):713–734.
   Google Scholar
• RUECKERT RR: Picornaviridae: the viruses and their replication. In: Fields Virology, 3rd Ed. (Volume 1). Fields BN, Knipe DM, Howley PM et al. (Eds.), Lippincott-Raven Publishers, Philadelphia, USA (1996):609–654.
   Google Scholar
• HAMPARIAN VV, COLONNO RJ, COONEY MK et al.: A collaborative report: rhinoviruses-extension of the numbering system from 89 to 100. Virology (1987) 159:191–192.
   PubMed Web of Science ®Google Scholar
• BERGMANN EM, JAMES MNG: Proteolytic enzymes ofthe viruses of the family picornaviridae. In: Proteases of Infectious Agents. Academic Press (1999):139–163.
   Google Scholar
• BERGMANN EM, JAMES MNG: The 3C proteinases ofpicornaviruses and other positive-sense, single-stranded RNA viruses. Handb. Exp. Pharmacol. (2000) 140:117–143.
   Google Scholar
• CLARKE ME, HAMMERLE T, WIMMER E, DASGUPTA A:Poliovirus proteinase 3C converts an active form of transcription Factor MC to an inactive form: a mechanism for inhibition of host cell polymerase III transcription by poliovirus. EMBO J. (1991) 10:2941–2947.
   PubMed Web of Science ®Google Scholar
• KNOTT JA, ORR DC, MONTGOMERY DS, SULLIVAN CA,WESTON A: The expression and purification of human rhinovirus protease 3C. Eur. J. Biochem. (1989) 182:547–555.
   PubMedGoogle Scholar
• CORDINGLEY MG, REGISTER RB, CALLAHAN PL, GARSKY VM, COLONNO RJ: Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli. J. Virol. (1989) 63:5037–5045.
   PubMed Web of Science ®Google Scholar
• •Substrate specificity studies of the HRV 3C protease which also influenced subsequent 3C protease inhibitor design.
   Google Scholar
• LEONG LE-C, WALKER PA, PORTER AG: Efficient expres-sion and purification of a protease from the common cold virus, human rhinovirus Type 14.1 Cryst. Growth (1992) 122:246–252.
   Google Scholar
• BIRCH GM, BLACK T, MALCOLM SK, LAI MT, ZIMMERMAN RE, JASKUNAS SJ: Purification of recombinant human rhinovirus 14 3C protease expressed in Escherichia colt. Protein Expr. Purif (1995) 6:609–618.
   PubMed Web of Science ®Google Scholar
• ASCHAUER B, WERNER G, MCCRAY J, ROSENWIRTH B, BACHMAYER H: Biologically active protease 3C of human rhinovirus 1A is expressed from a cloned cDNA segment in Escherichia coli. Virology (1991) 184:587–594.
   PubMed Web of Science ®Google Scholar
• KATI WM, SHAM, HL, MCCALL JO et al.: Inhibition of 3C protease from human rhinovirus strain 1 B by pep tidyl bromomethylketonehydrazides. Arch. Biochem. Biophys. (1999) 362:363–375.
   PubMed Web of Science ®Google Scholar
• WEBBER SE, TIKHE J, WORLAND ST et al.: Design, synthesis and evaluation of nonpeptidic inhibitors of human rhinovirus 3C protease. J Med. Chem. (1996) 39:5072–5082.
   PubMed Web of Science ®Google Scholar
• ORR DC, LONG AC, KAY J, DUNN BM, CAMERON JM: Hydrolysis of a series of synthetic peptide substrates by the human rhinovirus 14 3Cproteinase, cloned and expressed in Escherichia coil J. Gen. Virol. (1989) 70:2931–2942.
   PubMed Web of Science ®Google Scholar
• •Substrate specificity studies of the HRV 3C protease which also influenced subsequent 3C protease inhibitor design.
   Google Scholar
• LONG AC, ORR DC, CAMERON JM, DUNN BM, KAY J: A consensus sequence for substrate hydrolysis by rhinovirus 3C proteinase. FEBS Lett. (1989) 258:75–78.
   PubMed Web of Science ®Google Scholar
• •Substrate specificity studies of the HRV 3C protease which also influenced subsequent 3C protease inhibitor design.
   Google Scholar
• CORDINGLEY MG, CALLAHAN PL, SARDANA VV, GARSKY VM, COLONNO RJ: Substrate requirements of human rhinovirus 3C protease for peptide cleavage in vitro. J. Biol. Chem. (1990) 265:9062–9065.
   PubMed Web of Science ®Google Scholar
• •Substrate specificity studies of the HRV 3C protease which also influenced subsequent 3C protease inhibitor design.
   Google Scholar
• CHEAH K-C, LEONG LE-C, PORTER AG: Site-directedmutagenesis suggests close functional relationship between human rhinovirus 3C protease and cellular trypsin-like serine proteases. J Biol. Chem. (1990) 265:7180–7187.
   PubMed Web of Science ®Google Scholar
• LEONG LE-C, WALKER PA, PORTER AG: Human rhinovirus-1 4 protease 3C (3Cpro) binds specifically to the 5'-noncoding region of the viral RNA. J Chem. (1993) 268:25735–25739.
   Web of Science ®Google Scholar
• COX GA, JOHNSON RB, COOK JA et al: Identificationand characterization of human rhinovirus-1 4 3C protease deamidation isoform. J Biol. Chem. (1999) 274:13211–13216.
   PubMed Web of Science ®Google Scholar
• DAVIS GJ, WANG QM, COX GA et al.: Expression andpurification of recombinant rhinovirus 14 3CD proteinase and its comparison to the 3C proteinase. Arch. Biochem. Biophys. (1997) 346:125–130.
   PubMed Web of Science ®Google Scholar
• HOPKINS JL, BETAGERI R, COHEN KA et al.: Rhinovirus3C protease catalyzes efficient cleavage of a fluorescein-labeled peptide affording a rapid and robust assay. J. Biochem. Biophys. Methods (1991) 23:107–113.
   PubMedGoogle Scholar
• HEINZ BA, TANG J, LABUS JM, CHADWELL, FW, KALDORSW, HAMMOND M: Simple in vitro translation assay to analyze inhibitors of rhinovirus proteases. Antimicrob. Agents Chemother. (1996) 40:267–270.
   PubMed Web of Science ®Google Scholar
• WANG QM, JOHNSON RB, COX GA, VILLARREAL EC, LONCHARICH RJ: A continuous colorimetric assay for rhinovirus-14 3C protease using peptide p-nitroanilides as substrates. Anal. Biochem. (1997) 252:238–245.
   PubMed Web of Science ®Google Scholar
• MATTHEWS DA, SMITH WW, FERRE RA et al.: Structure ofhuman rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA binding site and means for cleavingprecursor polyprotein. Cell (1994)77:761–771.
   PubMed Web of Science ®Google Scholar
• •Crystal structure of the HRV 3C protease.
   Google Scholar
• LEE W-M, WANG W, RUECKERT RR: Complete sequenceof the RNA genome of human rhinovirus 16, a clinically useful common cold virus belonging to the ICA1VI-1 receptor group. Virus Genes (1994) 9:177-181 and references therein.
   Google Scholar
• GORBALENYA AE, BLINOV VM, DONCHENKO AP: Poliovirus-en coded pro teinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families. FEBS Lett. (1986) 194:253–259.
   PubMed Web of Science ®Google Scholar
• MATTHEWS DA, DRAGOVICH PS, WEBBER SE et al: Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes. Proc. Nati Acad. Sci. USA (1999) 96:11000–11007.
   PubMed Web of Science ®Google Scholar
• WANG QM: Human rhinovirus 3C protease inhibitors:recent developments. Exp. Opin. Ther. Patents (1998) 8:1151–1156.
   Web of Science ®Google Scholar
• WANG QM: Protease inhibitors as potential antiviral agents for the treatment of picornaviral infections. Prog. Drug. Res. (1999) 52:197–219.
   PubMedGoogle Scholar
• WANG QM: Design of rhinovirus protease inhibitors for the treatment of the common cold. Drugs Future (2000) 25:279–286.
   Google Scholar
• HANZLIK RP, THOMPSON SA: Vinylogous amino acid esters: anew class of inactivators for thiol proteases. Med. Chem. (1984) 27:711–712.
   Web of Science ®Google Scholar
• PALMER JT, RASNICK D, KLAUS JL, BROMME D: Vinyl sulfones as mechanism-based cysteine protease inhibitors. J. Med. Chem. (1995) 38:3193–3196.
   PubMed Web of Science ®Google Scholar
• KONG J-S, VENKATRAMAN S, FURNESS K et al.: Synthesis and evaluation of peptidyl Michael acceptors that inactivate human rhinovirus 3C protease and inhibit virus replication. J Med. Chem. (1998) 41:2579–2587.
   PubMed Web of Science ®Google Scholar
• ••First literature report of peptidyl Michael acceptors as HRV3C protease inhibitors.
   Google Scholar
• DRAGOVICH PS, WEBBER SE, BABINE RE et al.: Structure-based design, synthesis and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 1. Michael-acceptor structure-activity studies. J. Med. Chem. (1998) 41:2806–2818.
   Google Scholar
• ••Second literature report of peptidyl Michael acceptors asHRV 3C protease inhibitors.
   Google Scholar
• DRAGOVICH PS, WEBBER SE, BABINE RE et al.: Structure-based design, synthesis and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 2. Peptide structure-activity studies. J. Med. Chem. (1998) 41:2819–2834.
   Google Scholar
• ••Synthesis and evaluation of additional peptidyl Michaelacceptors as HRV 3C protease inhibitors.
   Google Scholar
• DRAGOVICH PS, ZHOU R, SKALITZKY DJ et al.: Solid-phase synthesis of irreversible human rhinovirus 3C protease inhibitors. Part 1: Optimization of tripep tides incorporating N-terminal amides. Bioorg. Med. Chem. (1999) 7:589–598.
   Google Scholar
• DRAGOVICH PS, PRINS TJ, ZHOU R et al.: Structure-baseddesign, synthesis and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 3. Structure-activity studies of ketomethylene-containing peptidomimetics. J. Med. Chem. (1999) 42:1203–1212.
   Google Scholar
• •Synthesis and evaluation of peptidomimetic, ketomethylene-containing Michael acceptors as HRV 3C protease inhibitors.
   Google Scholar
• DRAGOVICH PS, WEBBER SE, PRINS TJ et al.: Structure-based design of irreversible, tripeptidyl human rhinovirus 3C protease inhibitors containing N-methyl amino acids. Bioorg. Med. Chem. Lett. (1999) 9:2189–2194.
   PubMed Web of Science ®Google Scholar
• DRAGOVICH PS, PRINS TJ, ZHOU R et al.: Structure-baseddesign, synthesis and biological evaluation of irreversible human rhinovirus 3C protease inhibitors.4. Incorporation of Pi lactam moieties as L-glutamine replacements. J. Med. Chem. (1999) 42:1213–1224.
   Google Scholar
• ••Further improvement of peptidomimetic Michael acceptorsas HRV 3C protease inhibitors. Disclosure of AG7088.
   Google Scholar
• PATICK AK, BINFORD SL, BROTHERS MA et al: In vitro antiviral activity of AG7088, a potent inhibitor of human rhinovirus 3C protease. Antimicrob. Agents Chemother. (1999) 43:2444–2450.
   PubMed Web of Science ®Google Scholar
• •In vitro antirhinoviral activity of AG7088 against 48 HRV serotypes.
   Google Scholar
• ZALMAN LS, BROTHERS MA, DRAGOVICH PS et al: Inhibition of human rhinovirus-induced cytokine production by AG7088, a human rhinovirus 3C protease inhibitor. Antimicrob. Agents Chemother. (2000) 44:1236–1241.
   PubMed Web of Science ®Google Scholar
• GRAUL A, CASTASIER J.: AG-7088, anti-rhinovirus drug HRV3Cprotease inhibitor. Drugs Future (2000) 25:9–15.
   Google Scholar
• REICH SH, JOHNSON T, WALLACE MB et al: Substituted benzamide inhibitors of human rhinovirus 3C protease: structure-based design, synthesis and biological evaluation. J. Med. Chem. (2000) 43: 1670–1683.
   PubMed Web of Science ®Google Scholar
• •Synthesis and evaluation of non-peptide Michael acceptors as HRV 3C protease inhibitors.
   Google Scholar
• HILL RD, VEDERAS JC: Azodicarbox amides: a new class of cysteine protease inhibitor for hepatitis A virus and human rhinovirus 3C enzymes. J. Org. Chem. (1999) 64:9538–9546.
   Web of Science ®Google Scholar
• •Synthesis and evaluation of non-peptide azodicarbox-amides as HRV 3C protease inhibitors.
   Google Scholar
• VENKATRAMAN S, KONG J-s, NIMKAR S, WANG QM, AUBÉ J, HANZLIK RP: Design, synthesis and evaluation of azapeptides as substrates and inhibitors for human rhinovirus 3C protease. Bioorg. Med. Chem. Lett. (1999) 9:577–580.
   PubMed Web of Science ®Google Scholar
• DRAGOVICH PS, ZHOU R, WEBBER SE et al: Structure- based design of ketone-containing, tripeptidyl human rhinovirus 3C protease inhibitors. Bioorg. Med. Chem. Lett. (2000) 10: 45–48.
   PubMed Web of Science ®Google Scholar
• •Synthesis and evaluation of peptidyl heterocyclic ketones as HRV 3C protease inhibitors.
   Google Scholar
• ROGERS JM, DIANA GD, MCKINLAY MA: Pleconaril, a broad spectrum antipicornavir al agent. Antiviral Chemother. (1999) 5:69–76.
   Google Scholar
• XIAN M, WANG QM, CHEN X, WANG K, WANG PG: S-Nitrosothiols as novel, reversible inhibitors of human rhinovirus 3C protease. Bioorg. Med. Chem. Lett. (2000) 10:2097–2100.
   PubMed Web of Science ®Google Scholar