Identification and use of antiviral compounds that inhibit...

Details Identification and use of antiviral compounds that inhibit... Identification and use of antiviral compounds that inhibit...

2003-01-06

2009-12-15

Lucas, Zachariah (Department: 1648)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Peptide containing doai

C530S300000, C530S326000, C530S327000

Reexamination Certificate

active

07632801

ABSTRACT:
The present invention relates to the identification of host cell proteins that interact with viral proteins required for virus replication, and high throughput assays to identify compounds that interfere with the specific interaction between the viral and host cell protein. Interfering compounds that inhibit viral replication can be used therapeutically to treat viral infection. The invention is based, in part, on the Applicants' discovery of novel interactions between viral proteins and a human host cell proteins. One of these host cell proteins, referred to herein as NPI-1, interacts with influenza virus protein NP. Also, host cell proteins, referred to herein as NS1I-1 and NS1-BP interact with influenza virus protein NS1. In addition, host cell proteins containing WW domains that interact with viral proteins such as Rhabdoviral M protein are described. Compounds that interfere with the binding of the host cell and viral proteins, and inhibit viral replication can be useful for treating viral infection in vivo.

REFERENCES:
patent: 5110906 (1992-05-01), Maddon et al.
patent: 5738985 (1998-04-01), Miles et al.
patent: 5744343 (1998-04-01), Draetta et al.
patent: 5750394 (1998-05-01), Palese et al.
patent: 5834429 (1998-11-01), Pert et al.
patent: 6503703 (2003-01-01), Palese et al.
patent: 2003/0232325 (2003-12-01), Palese et al.
patent: 2005/0191703 (2005-09-01), Palese et al.
patent: WO 94/02606 (1994-02-01), None
patent: WO 95/32310 (1995-11-01), None
patent: WO 97/12967 (1997-04-01), None
Adessi et al., “Converting a peptide into a drug: Strategies to improve stability and bioavailability,” Current Medicinal chemistry, vol. 9, pp. 963-978 (2002).
Cros et al., “An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein,” Traffic vol. 6 No. 3, pp. 205-213 (Mar. 2005).
Steffansen et al., “Delivery aspects of small peptides and substrates for peptide transporters,” European Journal of Pharmaceutics and Biopharmaceutics, vol. 60, pp. 241-245 (2005).
Stevens et al., “The N-terminal extension of the influenza B virus nucleoprotein is not required for nuclear accumulation or the expression and replication of a model RNA,” Journal of Virology, vol. 72 No. 6, pp. 5307-5312 Jun. 9, 1998).
U.S. Appl. No. 60/148,263, filed Aug. 11, 1999, Palese.
U.S. Appl. No. 08/444,994, filed May 19, 1995, Palese et al.
Albagli et al., 1995, “The BTB/POZ domain: a new protein-protein interaction motif common to DNA- and actin-binding proteins”, Cell Growth Diff. 6:1193-1198.
Baez et al., 1981, “Nucleotide sequence of the influenza A/duck/Alberta/60/76 virus NS RNA: conservation of the NS1/NS2 overlapping gene structure in a divergent influenza virus RNA segment”, Virology 113:397-402.
Bardwell and Treisman, 1994, “The POZ domain: a conserved protein-protein interaction motif”, Genes Dev. 8:1664-1677.
Barik and Banerjee, 1992, “Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P”, Proc. Natl. Acad. Sci. USA 89:6570-6574.
Barik and Banerjee, 1992, “Sequential phosphorylation of the phosphoprotein of vesicular stomatitis virus by cellular and viral protein kinases is essential for transcription activation”, J. Virol. 66:1109-1118.
Baudin et al., 1994, “Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent”, EMBO J. 13:3158-3165.
Bean, 1984, “Correlation of influenza A virus nucleoprotein genes with host species”, Virology 133:438-442.
Beaton and Krug, 1986, “Transcription antitermination during influenza viral template RNA synthesis requires the nucleocapsid protein and the absence of a 5′ capped end”, Proc. Natl. Acad. Sci. USA 83:6282-6286.
Belanger et al., 1994, “Genetic and physical interactions between Srp1p and nuclear pore complex proteins Nup1p and Nup2p”, J. Cell Biol. 126:619-630.
Benmansour et al., 1994, “The polymerase-associated protein (M1) and the matrix protein (M2) from a virulent and an avirulent strain of viral hemorrhagic septicemia virus (VHSV), a fish rhabdovirus”, Virology 198:602-612.
Bennett et al., 1993, “Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus gag proteins”, J. Virol. 67:6487-6498.
Bennett et al., 1991, “Amino acids encoded downstream ofgagare not required by Rous sarcoma virus protease during gag-mediated assembly”, J. Virol. 65:272-280.
Bond, 1988, “Heat shock but not other stress inducers leads to the disruption of a sub-set of snRNPs and inhibition of in vitro splicing in HeLa cells”, EMBO J. 7:3509-3518.
Bork and Doolittle, 1994, “Drosophila kelchmotif is derived from a common enzyme fold”, J. Mol. Biol. 236:1277-128.
Bork and Sudol, 1994, “The WW domain: a signalling site in dystrophin?”, Trends Biochem. Sci. 19:531-533.
Brown et al., 1995, “Herpes simplex virustrans-regulatory protein ICP27 stabilizes and binds to 3′ ends of labile mRNA”, J. Virol. 69:7187-7195.
Buckler-White and Murphy, 1986, “Nucleotide sequence analysis of the nucleoprotein gene of an avian and a human influenza virus strain indentifies two classes of nucleoproteins”, Virology 55:345-355.
Bukreyev et al., 1995, “The complete nucleotide sequence of the Popp (1967) strain of Marburg virus: a comparison with the Musoke (1980) strain”, Arch. Virol. 140:1589-1600.
Buonagurio et al., 1985, “Evolution of human influenza A viruses over 50 years: rapid, uniform rate of change in NS gene”, Science 232:980-982.
Chang-Yeh et al., 1991, “Identification of a novel murine IAP-promoted placenta-expressed gene”, Nucl. Acids Res. 19:3667-3672.
Chelsky et al., 1989, “Sequence requirements for synthetic peptide-mediated translocation to the nucleus”, Mol. Cell. Biol. 9:2487-2492.
Chen et al., 1997, “Characterization of the WW domain of human Yes-associated protein and its polyproline-containing ligands”, J. Biol. Chem. 272:17070-17077.
Chen and Sudol, 1996, “Identification and characterization of protein ligands to the WW domain by Western ligand blotting”, Techniques in Protein Chemistry VII, 7:3-12.
Chen and Sudol, 1995, “The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules”, Proc. Natl. Acad. Sci. USA 92:7819-7823.
Chen et al., 1995, “The BTB domain ofbric a bracmediates dimerization in vitro”, Mol. Cell. Biol. 15:3424-3429 [retracted by Mol. Cell Biol. 17:6772 (1997)].
Chen et al., 1993, “Site-specific mutagenesis ofDrosophilaalcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis”, Biochem. 32:3342-3346.
Chien et al., 1991, “The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest”, Proc. Natl. Acad. Sci. USA 88:9578-9582.
Chong and Rose, 1994, “Interactions of normal and mutant vesicular stomatitis virus matrix proteins with the plasma membrane and nucleocapsids”, J. Virol. 68:441-447.
Chong and Rose, 1993, “Membrane association of functional vesicular stomatitis virus matrix protein in vivo”, J. Virol. 67:407-414.
Cortes et al., 1994, “RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1” Proc. Natl. Acad. Sci. USA 91:7633-7637.
Craven et al., 1999, “Late domain function indentified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras”, J. Virol. 73:3359-3365.
Craven et al., 1993, “Necessity of the spacer peptide between CA and NC in the Rous sarcoma virus gag protein”, J. V

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