Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Bacterium or component thereof or substance produced by said...
Reexamination Certificate
2006-05-30
2006-05-30
Weber, Jon (Department: 1653)
Drug, bio-affecting and body treating compositions
Antigen, epitope, or other immunospecific immunoeffector
Bacterium or component thereof or substance produced by said...
C424S236100, C424S183100, C424S194100, C424S094670, C435S069100, C435S320100, C435S252700, C530S350000, C530S396000, C514S002600, C514S012200
Reexamination Certificate
active
07052702
ABSTRACT:
A class of novel agents that are able to modify nociceptive afferent function is provided. The agents may inhibit the release of neurotransmitters from discrete populations of neurones and thereby reduce or preferably prevent the transmission of afferent pain signals from peripheral to central pain fibers. They comprise a galactose-binding lectin linked to a derivative of a clostridial neurotoxin. The derivative of the clostridial neurotoxin comprises the L-chain, or a fragment thereof, which includes the active proteolytic enzyme domain of the light (L) chain, linked to a molecule or domain with membrane translocating activity. The agents may be used in or as pharmaceuticals for the treatment of pain, particularly chronic pain.
REFERENCES:
patent: 4792447 (1988-12-01), Uhr et al.
patent: 4873346 (1989-10-01), Anderson
patent: 5433946 (1995-07-01), Allen, Jr. et al.
patent: 5668255 (1997-09-01), Murphy
patent: 5721207 (1998-02-01), Nobel et al.
patent: 5989545 (1999-11-01), Foster et al.
patent: 6235313 (2001-05-01), Mathiowitz et al.
patent: 6395513 (2002-05-01), Foster et al.
patent: 6461617 (2002-10-01), Shone et al.
patent: 6632440 (2003-10-01), Quinn et al.
patent: 2003/0049264 (2003-03-01), Foster et al.
patent: 2003/0147895 (2003-08-01), Shone et al.
patent: 2003/0166238 (2003-09-01), Shone et al.
patent: 2004/0071736 (2004-04-01), Quinn et al.
patent: 197 35 105 (1999-03-01), None
patent: 0 602 686 (1994-06-01), None
patent: 0 673 938 (1995-09-01), None
patent: WO 91/09871 (1991-07-01), None
patent: WO 92/15327 (1992-09-01), None
patent: WO 93/04191 (1993-03-01), None
patent: WO 93/15766 (1993-08-01), None
patent: WO 94/21300 (1994-09-01), None
patent: WO 94/28923 (1994-12-01), None
patent: WO 95/17904 (1995-07-01), None
patent: WO 95/28171 (1995-10-01), None
patent: WO 95/32738 (1995-12-01), None
patent: WO 95/33850 (1995-12-01), None
patent: WO 96/12802 (1996-05-01), None
patent: WO 96/33273 (1996-10-01), None
patent: WO 97/13410 (1997-04-01), None
patent: WO 97/18790 (1997-05-01), None
patent: WO 98/07684 (1998-02-01), None
patent: WO 98/07864 (1998-02-01), None
patent: WO 98/08540 (1998-03-01), None
patent: WO 99/58571 (1999-11-01), None
patent: WO 00/04926 (2000-02-01), None
patent: WO 00/10598 (2000-03-01), None
patent: WO 00/57897 (2000-10-01), None
Welch et al., Sensitivity of Embryonic Rat Dorsal Root Ganglia Neurons toClostridium botulinumNeurotoxins. Toxicon 38, 245-258 (2000).
Besson. The Complexity of Physiopharmacological Aspects of Pain. Drugs 53 Suppl 2, 1-9 (1997).
Streit, W.J., et al., “Histochemical Localization of Galactose-Containing Glycoconjugates in Sensory Neurons and Their Processes in the Central and Peripheral Nervous System of the Rat,”J Histochem Cytochem 33: 1042-1052 (1985).
Adar, R. et al., “The amino acid sequence ofErythrina corallodendronlectin and its homology with other legume lectins,”FEBS Lett. 257:81-85 (1989), abstract from PubMed, PMID: 2806566.
Arango, R. et al., “Cloning and sequence analysis of theErythrina corallodendronlectin cDNA,”FEBS Lett. 264:109-111 (1990), abstract from PubMed, PMID: 1692539.
Arango, R. et al., “Expression ofErythrina corallodendronlectin inEscherichia coli,” Eur. J. Biochem. 205:575-581 (1992), abstract from PubMed, PMID: 1572358.
Arora, N. et al., “Cytotoxic effects of a chimeric protein consisting of tetanus toxin light chain and anthrax toxin lethal factor in non-neuronal cells,”J. Biol. Chem. 269:26165-26171 (1994), abstract from PubMed, PMID: 7929330.
Brinkmann, U. et al., “A recombinant immunotoxin containing a disulfide-stabiliz Fv fragment,”Proc. Natl. Acad. Sci. USA 90:7538-7542 (1993), abstract from PubMed, PMID: 8356052.
Kurazono, H. et al., “Minimal Essential Domains Specifying Toxicity of the Light Chains of Tetanus Toxin and Botulinum Neurotoxin Type A,”J. Biol. Chem. 267:14721-14729, The American Society for Biochemistry and Molecular Biology, Inc. (1992).
Lamb, F.I. et al., “Nucleotide sequence of cloned cDNA coding for preproricin,”Eur. J. Biochem. 148:265-270 (1985), abstract from PubMed, PMID: 3838723.
Law, I. J., “Cloning and expression of cDNA for galactose-binding lectin from peanut nodules,”Plant Science 115:71-79, Elsevier Science Ireland Ltd. (1996).
Lorberboum-Galski, H. et al., “Cytotoxic activity of an interleukin 2-Pseudomonas exotoxi chimeric protein produced inEscherichia coli,” Proc. Natl. Acad. Sci. USA 85:1922-1926 (1988), abstract from PubMed, PMID: 3126499.
Murphy, J.R., “Diphtheria-related peptide hormone gene fusions: a molecular genetic approach to chimeric toxin development,”Cancer Treat. Res. 37:123-140 (1988), abstract from PubMed, PMID: 2908622.
Nathan, S. and Halina, L., “Legume lectins—a large family of homologous proteins,”The FASEB J. 4:3198-3208, The Federation of American Societies for Experimental Biology (1990).
“NeuroBloc (Botulinum Toxin Type B) For Cervical Dystonia Launched in UK,”Doctor's Guide, P/S/L Consulting Group Inc. (Mar. 2001), visited <Nov. 28, 2001> at <http://www.pslgroup.com/dg/1F4216.htm>.
O'Hare, M. et al., “Cytotoxicity of a recombinant ricin-A-chain fusion protein containing a proteolytically-cleavable spacer sequence,”FEBS Lett. 273:200-204 (1990), abstract from PubMed, PMID: 2121540.
Plank, C. et al., “The influence of endosome-disruptive peptides on gene transfer using synthetic virus-like gene transfer systems,”J. Biol. Chem. 269:12918-12924 (1994), abstract from PubMed, PMID: 8175709.
Van Damme, E.J.M. et al., “Molecular cloning of the bark and seed lectins from the Japanese pagoda tree (Sophora japonica),”Plant Molec. Biol. 33:523-536, Kluwer Academic Publishers (1997).
Williams, D.P. et al., “Diphtheria toxin receptor binding domain substitution with interleukin-2: genetic construction and properties of a diphtheria toxin-related interleukin-2 fusion protein,”Protein Eng. 1:493-498 (1987), abstract from PubMed, PMID: 3334101.
Wood, K.A. et al., “Preproabrin: genomic cloning, characterisation and the expression of the A-chain inEscherichia coli,” Eur. J. Biochem. 198:723-732 (1991), abstract from PubMed, PMID: 2050149.
Yamaguchi, O. et al., “Chemical structures of two subunits, A-subunit and B-subunit, of galactose-specific isolectins fromErythrina variegataseeds,”J. Biochem(Tokyo)114:560-566 (1993), abstract from PubMed, PMID: 8276768.
Black, J.D., and Dolly, J.O., “Interaction of125Labeled Botulinum Neurotoxins with Nerve Terminals. I. Ultrastructural Autoradiographic Localization and Quantitation of Distinct Membrane Acceptors for Types A and B on Motor Nerves,”J. Cell Biol. 103:521-534, The Rockefeller University Press (1986).
Blaustein, R.O., et al., “The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers,”FEBS Letts. 226:115-120, Elsevier Science Publishers B.V. (1987).
Shone, C.C., et al., “Inactivation ofClostridium botulinumtype A neurotoxin by trypsin and purification of two tryptic fragments. Proteolytic action near the COOH-terminus of the heavy subunit destroys toxin-binding activity,”Eur. J. Biochem. 151:75-82, Springer International (1985).
Shone, C.C., et al., “A 50-kDa fragment from the NH2-terminus of the heavy subunit ofClostridium botulinumtype A neurotoxin forms channels in lipid vesicles,”Eur. J. Biochem.167:175-180, Springer International (1987).
Sutton, J.M., et al., “Tyrosine-1290 of tetanus neurotoxin plays a key role in its binding to gangliosides and functional binding to neurones,”FEBS Letts. 493:45-49, Elsevier Science B.V. (Mar. 2001).
Yamazaki, N., et al., “Endogenous lectins as targets for drug delivery,”Advanced Drug Delivery Reviews 43:225-244, Elsevier Science B.V. (Sep. 2000).
Dialog File 351, WPI Accession No. 1999-168079/199915, Derwent WPI English la
Chaddock John Andrew
Duggan Michael John
Health Protection Agency
Ipsen Limited
Kam Chih-Min
Weber Jon
LandOfFree
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