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- Nachgewiesen in: USPTO Patent Grants
- Sprachen: English
- Patent Number: 7,670,802
- Publication Date: March 02, 2010
- Appl. No: 12/067221
- Application Filed: October 30, 2006
- Assignees: Merck Serono SA (Coinsins, Vaud, CH)
- Claim: 1. An isolated polypeptide comprising: a)SEQ ID NO: 5 (Evasin-3); b)SEQ ID NO: 6 (mature Evasin-3); c)SEQ ID NO: 17 (Evasin-3-HIS); d)SEQ ID NO: 18 (mature Evasin-3-HIS); e)SEQ ID NO: 26 (Met-Evasin-3); or f)SEQ ID NO: 5 in which a cysteine residue in the position corresponding to residues 48, 52, 59, 63, 65 or 76 or the asparagine at position 51 or 82 has been substituted.
- Claim: 2. The isolated polypeptide according to claim 1 , wherein said polypeptide comprises SEQ ID NO: 5 (Evasin-3).
- Claim: 3. The isolated polypeptide according to claim 1 , wherein said polypeptide comprises SEQ ID NO: 6 (mature Evasin-3).
- Claim: 4. The isolated polvpeptide according to claim 1 , wherein said polypeptide comprises SEQ ID NO: 17 (Evasin-3-HIS).
- Claim: 5. The isolated polypeptide according to claim 1 , wherein said polypeptide comprises SEQ ID NO: 18 (mature Evasin-3-HIS).
- Claim: 6. The isolated polypeptide according to claim 1 , wherein said polypeptide comprises SEQ ID NO: 26 (Met-Evasin-3).
- Claim: 7. The isolated polypeptide according to claim 1 , wherein said polypeptide comprises SEQ ID NO: 5 (Evasin-3) and in which a cysteine residue in the position corresponding to residues 48, 52, 59, 63, 65 or 76 or the asparagine at position 51 or 82 has been substituted.
- Claim: 8. The isolated polypeptide according to claim 1 wherein said polypeptide further comprises one or more amino acid sequences chosen from the following: an extracellular domain of a membrane-bound protein, an immunoglobulin constant region, a multimerization domain, a heterodimeric protein hormone, a signal peptide, an export signal or a tag sequence operably linked to said polypeptide.
- Claim: 9. A composition comprising a pharmaceutically acceptable carrier and a polypeptide comprising; a) SEQ ID NO: 5 (Evasin-3); b) SEQ ID NO:6 (mature Evasin -3); c) SEQ ID NO: 17 (Evasin-3-HIS); d) SEQ ID NO: 18 (mature Evasin-3-HIS); e) SEQ ID NO: 26 (Met-Evasin-3); or f) SEQ ID NO: 5 in which a cysteine residue in the position corresponding to residues 48, 52, 59, 63, 65 or 76 or the asparagine at position 51 or 82 has been substituted.
- Claim: 10. The composition according to claim 9 , wherein said polypeptide comprises SEQ ID NO: 5 (Evasin-3).
- Claim: 11. The composition according to claim 9 , wherein said polypeptide comprises SEQ ID NO: 6 (mature Evasin-3).
- Claim: 12. The composition according to claim 9 , wherein said polypeptide comprises SEQ ID NO: 17 (Evasin-3-HIS)
- Claim: 13. The composition according to claim 9 , wherein said polypeptide comprises SEQ ID NO): 18 (mature Evasin-3-HIS).
- Claim: 14. The composition according to claim 9 , wherein said polypeptide comprises SEQ ID NO: 26 (Met-Evasin-3).
- Claim: 15. The composition according to claim 9 , wherein said polypeptide comprises SEQ ID NO: 5 (Evasin-3) and in which a evsteine residue in the position corresponding to residues 48, 52, 59, 63, 65 or 76 or the asparagine at position 51 or 82 has been substituted.
- Claim: 16. The composition according to claim 9 , wherein said polypeptide further comprises one or more amino acid sequences chosen from the following: an extracellular domain of a membrane-bound protein, an immunoglobulin constant region, a multimerization domain, a heterodimeric protein hormone, a signal peptide, an export signal or a tag sequence operably linked to said polypeptide.
- Claim: 17. An isolated nucleic acid encoding a polypeptide comprising: a) SEQ ID NO:5 (Evasin-31); b) SEQ ID NO:6 (mature Evasin-3); c) SEQ ID NO: 17 (Evasin-3-HIS); d) SEQ ID NO: 18 (mature Evasin-3HIS); e) SEQ ID NO: 26 (Met-Evasin-3); or f) SEQ ID NO: 5 in which a cysteine residue in the position corresponding to residues 48, 52, 59, 63, 65 or 76 or the asparagine at position 51 or 82 has been substituted.
- Claim: 18. An isolated cloning or expression vector comprising a nuclcic acid encoding a polypeptide comprising; a) SEQ ID NO: 5 (Evasin-3); b) SEQ ID NO: 6 (mature Evasin-3); c) SEQ ID NO: 17 (Evasin-3-HIS); d) SEQ ID NO: 18 (mature Evasin-3-HIS); e) SEQ ID NO: 26 (Met-Evasin-3); or f) SEQ ID NO: 5 in which a cysteine residue in the position corresponding to residues 48, 52, 59, 63, 65 or 76 or the asparagine at position 51 or 82 has been substituted.
- Claim: 19. An isolated host cell comprising an expression vector comprising a nucleic acid encoding a polypeptide comprising: a) SEQ ID NO: 5 (Evasin-3); b) SEQ ID NO: 6 (mature Evasin-3); c) SEQ ID NO: 17 (Evasin-3-HIS); d) SEQ ID NO: 18 (mature Evasin-3-HIS); e) SEQ ID NO: 26 (Met-Evasin-3); or f) SEQ ID NO: 5 in which a cysteine residue in the position corresponding to residues 48, 52, 59, 63, 65 or 76 or the asparagine at position 51 or 82 has been substituted.
- Claim: 20. A method for producing a polypeptide comprising culturing a host cell under conditions allowing or promoting expression of said polypeptide, wherein said host cell comprising an expression vector comprising: a nucleic acid encoding a polypeptide comprising: a) SEQ ID NO: 5 (Evasin-3); b) SEQ ID NO: 6 (mature Evasin-3); c) SEQ ID NO: 17 (Evasin-3-HIS); d) SEQ ID NO: 18 (mature Evasin-3-HIS); e) SEQ ID NO: 26 (Met-Evasin-3); or f) SEQ ID NO:5 in which a cysteine residue in the position corresponding to residues 48, 52, 59, 63, 65 or 76 or the asparagine at position 51 or 82 has been substituted.
- Claim: 21. The method according to claim 20 , further comprising purifying the polypeptide.
- Claim: 22. The method according to claim 21 , further comprising formulating the polypeptide with a pharmaceutically acceptable carrier.
- Claim: 23. A method for immunizing an animal against a blood-feeding ectoparasite comprising administering to said animal a polypeptide comprising: comprising a nucleic acid encoding a polypeptide comprising: a) SEQ ID NO: 5 (Evasin-3); b) SEQ ID NO: 6 (mature Evasin-3) c) SEQ ID NO: 17 (Evasin-3-HIS); d) SEQ ID NO: 18 (mature Evasin-3-HIS); e) SEQ ID NO: 26 (Met-Evasin-3); or f) SEQ ID NO: 5 in which a cysteine residue in the position corresponding to residues 48, 52, 59, 63, 65 or 76 or the asparagine at position 51 or 82 has been substituted.
- Current U.S. Class: 435/691
- Patent References Cited: 7393660 July 2008 Power et al. ; 2006/0228327 October 2006 Proudfoot et al. ; 2007/0224125 September 2007 Power et al. ; WO 00/27873 May 2000 ; WO 01/58941 August 2001 ; WO 2005/063812 July 2005
- Other References: Alarcon-Chaidez, F. J. et al. “Characterization of a recombinant immunomodulatory protein from the salivary glands of Dermacentor andersoni” Parasite Immunology, 2003, pp. 69-77, vol. 25. cited by other ; Aljamali, M.N. et al. “RNA interference in ticks: a study using histamine binding protein dsRNA in the female tick Amblyomma americanum” Insect Molecular Biology, 2003, pp. 299-305, vol. 12, No. 3. cited by other ; Baggiolini, M. “Chemokines in pathology and medicine” Journal of internal Medicine, 2001, pp. 91-104, vol. 250. cited by other ; Baggilolini, M. et al. “Human Chemokines: An Update” Annu. Rev. Immunol, 1997, pp. 675-705, vol. 15. cited by other ; Beck, C. G. et al. “The Viral CC Chemokine-binding Protein vCCI Inhibits Monocyte Chemoattractant Protein-1 Activity by Masking Its CCR2B-binding Site” The Journal of Biological Chemistry, Nov. 16, 2001, pp. 43270-43276, vol. 276, No. 46. cited by other ; Ben-Bassat, A. “Methods for Removing N-Terminal Methionine from Recombinant Proteins” Bioprocess Technol.1991, pp. 147-159, vol. 12. cited by other ; Brown, A. et al. “The Total Chemical Synthesis of Monocyte Chemotactic Protein-1 (MCP-1)” Journal of Peptide Science, 1996, pp. 40-46, vol. 2. cited by other ; Burns, J. et al. “Comprehensive Mapping of Poxvirus vCCI Chemokine-binding Protein” The Journal of Biological Chemistry, Jan. 25, 2002, pp. 2785-2789, vol. 277, No. 4. cited by other ; Bursill, C.A. et al. “Broad-Spectrum CC-Chemokine Blockade by Gene Transfer Inhibits Macrophage Recruitment and Atherosclerotic Plaque Formation in Apolipoprotein E-Knockout Mice” Circulation, 2004, pp. 2460-2466, vol. 110. cited by other ; Chuang, V. T. et al. “Pharmaceutical Strategies Utilizing Recombinant Human Serum Albumin” Pharmaceutical Research, May 2002, pp. 569-577, vol. 19, No. 5. cited by other ; Clackson, T. et al. “Making antibody fragments using phage display libraries” Nature, Aug. 15, 1991, pp. 624-628, vol. 352. cited by other ; Cleland, J. et al. “Emerging protein delivery methods” Current Opinion in Biotechnology, 2001, pp. 212-219, vol. 12. cited by other ; Coleman, R. A. et al. “Use of human tissue in ADME and safety profiling of development candidates” Drug Discovery Today, Nov. 21, 2001, pp. 1116-1126, vol. 6, No. 21. cited by other ; Doughtery, D. A. “Unnatural amino acids as probes of protein structure and function” Current Opinion in Chemical Biology, 2000, pp. 645-652, vol. 4. cited by other ; Ferreira, B. R. et al. “Saliva of Rhipicephalus sanguineus tick impairs T cell proliferation and IFN-y-induced macrophage microbicidal activity” Veterinary Immunology and Immunopatholgy, Mar. 26, 1998, pp. 279-293, vol. 64. cited by other ; Gendel, S. M. “Sequence Analysis for Assessing Potential Allergenicity” Ann. N.Y. Acad. Sci., 2002, pp. 87-98, vol. 964. cited by other ; Gillespie, R. D. et al. “Identification of an IL-2 Binding Protein in the Saliva of the Lyme Disease Vector Tick, Ixodes scapularis” The Journal of Immunology, 2001, pp. 4319-4326, vol. 166. cited by other ; Goding, J.W. “3. Production of Monoclonal Antibodies” In: Monoclonal Antibodies: Principals and Practice, 1986, pp. 59-103, Academic Press, Harcourt Javanovich, publisher. cited by other ; Golebiowski, A. et al. “High-throughput organic synthesis of peptide mimetics” Current Opinion in Drug Discovery & Development, 2001, pp. 428-434, vol. 4. cited by other ; Graslund, T. et al. “Production of a Thermostable DNA Polymerase by Site-Specific Cleavage of a Heat-Eluded Affinity Fusion Protein” Protein Expression and Purification, 1997, pp. 125-132, vol. 9. cited by other ; Greenwald, R.B. et al. “Effective drug delivery by PEGylated drug conjugates” Advanced Drug Delivery Reviews, 2003, pp. 217-250, vol. 55. cited by other ; Hajnicka, V. et al. “Anti-interleukin-8 activity of tick salivary gland extracts” Parasite Immunology, 2001, pp. 483-489, vol. 23. cited by other ; Hajnicka, V. et al. “Manipulation of host cytokine network by ticks: a potential gateway for pathogen transmission” Parasitology, 2005, pp. 333-342, vol. 130. cited by other ; Harris, J. M. et al. “Effect of Pegylation on Pharmaceuticals” Nature Review Drug Discovery, Mar. 2003, pp. 214-221, vol. 2. cited by other ; Hill, C. A. et al. “A method for extraction and analysis of high quality genomic DNA from ixodid ticks” Medical and Veterinary Entomology, 2003, pp. 224-227, vol. 17. cited by other ; Holt, L. J. et al. “Domain antibodies: proteins for therapy” TRENDS in Biotechnology, Nov. 2003, pp. 484-490, vol. 21, No. 11. cited by other ; Hoogenboom, H. R. et al. “By-passing Immunization Human Antibodies from Synthetic Repertoires of Germline V Gene Segments Rearranged in Vitro” J. Mol. Biol, 1992, pp. 381-388, vol. 227. cited by other ; Hruby, V. J. et al. “Conformational and Topographical Considerations in Designing Agonist Peptidomimetics from Peptide Leads” Current Medicinal Chemistry, 2000, pp. 945-970, vol. 7. cited by other ; Jensen, K. K. et al. “Disruption of CCL21-Induced Chemotaxis In Vitro and In Vivo by M3, a Chemokine-Binding Protein Encoded by Murine Gammaherpesvirus 68” Journal of Virology, Jan. 2003, pp. 624-630, vol. 77. cited by other ; Jones, P. T. et al. “Replacing the complementarity- determining regions in a human antibody with those from a mouse” Nature, May 29, 1986, pp. 522-525, vol. 321. cited by other ; Kipriyanov, S. M. et al. “Generation and Production of Engineered Antibodies” Molecular Biotechnology, 2004, pp. 39-60, vol. 26. cited by other ; Kocakova, P. et al. “Effect of fast protein liquid chromatography fractionated salivary gland extracts from different ixodid tick species on interleukin-8 binding to its cell receptors” Folia Parasitologica, 2003, pp. 79-84, vol. 50. cited by other ; Kohler, et al. “Continuous cultures of fused cells secreting antibody of predefined specificity” Nature, Aug. 7, 1975, p. 495, vol. 256. cited by other ; Li, A.P. “Screening for human ADME/Tox drug properties in drug discovery” Drug Discovery Today, Apr. 2001, pp. 357-366, vol. 6, No. 7. cited by other ; Luo, Y., et al. “Novel biomaterials for drug delivery” Expert Opinion Ther. Patents, 2001, pp. 1395-1410, vol. 11. No. 9. cited by other ; Madden, R. D. et al. “A proteomics approach to characterizing tick salivary secretions” Experimental and Applied Acarology, 2003, pp. 77-87, vol. 28. cited by other ; Marks, J. D. et al. “By-passing Immunization Human Antibodies from V-gene Libraries Displayed on Phage” J. Mol. Biol., 1991, pp. 581-597, vol. 222. cited by other ; Marshall, S. A. et al. “Rational design and engineering of therapeutic proteins” Drug Discovery Today, Mar. 2003, pp. 212-221, vol. 8, No. 5. cited by other ; Mulenga, A. et al. “Issues in tick vaccine development: identification and characterization of potential candidate vaccine antigens” Microbes and Infection, 2000, pp. 1353-1361, vol. 2. cited by other ; Murrell, A. et al. “A Total-Evidence Phylogeny of Ticks Provides Insights into the Evolution of Life Cycles and Biogeography” Molecular Phylogenetics and Evolution, Nov. 2001, pp. 244-258, vol. 21, No. 2. cited by other ; Murphy, L. R. et al. “Simplified amino acid alphabets for protein fold recognition and implications for folding” Protein Engineering, 2000, pp. 149-152, vol. 13, No. 3. cited by other ; Nilsson, J. et al. “Affinity Fusion Strategies for Detection, Purification and Immobilization of Recombinant Proteins” Protein Expression and Purification, 1997, pp. 1-16, vol. 11. cited by other ; Pearson, W. R. “Flexible Sequence Similarity Searching with the FASTA3 Program Package” Methods in Molecular Biology, 2000, pp. 185-219, vol. 132. cited by other ; Pillai, O. et al. “Polymers in drug delivery” Current Opinion in Chemical Biology, 2001, pp. 447-451, vol. 5. cited by other ; Presta, L. “Antibody engineering for therapeutics” Current Opinion in Structural Biology, 2003, pp. 519-525, vol. 13. cited by other ; Pyo, R. et al. “Inhibition of Intimal Hyperplasia in Transgenic Mice Conditionally Expressing the Chemokine-Binding Protein M3” American Journal of Pathology, Jun. 2004, pp. 2289-2297, vol. 164, No. 6. cited by other ; Rapoport, T.A., et al. “Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes” Annual Review Biochemistry, 1996, pp. 271-303, vol. 65. cited by other ; Rogov, S. L. et al. “A numerical measure of amino acid residues similarity based on the analysis of their surroundings in natural protein sequences” Protein Engineering, 2001, pp. 459-463, vol. 14, No. 7. cited by other ; Scatchard, G. “The Attractions of Proteins for Small Molecules and Ions” Ann NY Acad. Sci., 1949, pp. 660-672, vol. 51. cited by other ; Schellekens, H. “Bioequivalence and the Immunogenicity of Biopharmaceuticals” Nature Review Drug Discovery, Jun. 2002, pp. 457-462, vol. 1. cited by other ; Seet, B.T. et al. “Molecular determinants for CC-chemokine recognition by a poxvirus CC-chemokine inhibitor” Proc. Natl. Acad. Science USA, Jul. 31, 2001, pp. 9008-9013, vol. 98, No. 16. cited by other ; Ullmann, A. J. et al. “A preliminary linkage map of the tick, Ixodes scapularis” Experimental and Applied Acarology, 2002, pp. 107-126, vol. 28. cited by other ; Vaitukaitis, J. et al. “A method for producing specific antisera with small doses of Immunogen” J. Clin. Endocr, 1971, p. 988, vol. 33. cited by other ; Valenzuela, J.G. et al. “Editorial: Exploring the messages of the salivary glands of Ixodes Ricinus” Am. J. Trop. Med. Hyg., 2002, pp. 223-224, vol. 66, No. 3. cited by other ; Van Valkenburgh, H. A. et al. “Coexpression of Proteins with Methionine Aminopeptidase and/or N-Myristoyltransferase in Escherichia coli to Increase Acylation and Homogeneity of Protein Preparations” Methods in Enzymology, 2002, pp. 186-193, vol. 344. cited by other ; Vasserot, A.P. et al. “Optimization of protein therapeutics by directed evolution” Drug Discovery Today, Feb. 2003, pp. 118-126, vol. 8, No. 3. cited by other ; Villain, M. et al. “Covalent capture: a new tool for the purification of synthetic and recombinant polypeptides” Chemistry & Biology, 2001, pp. 673-679, vol. 8. cited by other ; Wang, H. et al. “Molecular individuality: polymorphism of salivary gland proteins in three species of ixodid tick” Experimental and Applied Acarolgy, 1999, pp. 969-975, vol. 23. cited by other ; Ward, E.S., et al. “Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli” Nature, Oct. 12, 1989, p. 544, vol. 341. cited by other ; Webb, L. M. et al. “The gammaherpesvirus chemokine binding protein can inhibit the interaction of chemokines with glycosaminoglycans” The FASEB Journal, Jan. 20, 2004, pp. 571-573, vol. 18. cited by other
- Primary Examiner: Saoud, Christine J
- Attorney, Agent or Firm: Saliwanchik, Lloyd & Saliwanchik
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