Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Transferase other than ribonuclease
Reexamination Certificate
2011-02-15
2011-02-15
Fronda, Christian L (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Transferase other than ribonuclease
C435S183000, C435S320100, C536S023200
Reexamination Certificate
active
07888091
ABSTRACT:
The present invention provides isolated nucleic acid molecules encoding a Herpesviridae thymidine kinase enzyme comprising one or more mutations, at least one of the mutations encoding an amino acid substitution located toward the N-terminus from a DRH nucleoside binding site which increases a biological activity of the thymidine kinase, as compared to unmutated thymidine kinase. Such mutations include amino acid substitutions within a Q substrate binding domain which increases a biological activity of the thymidine kinase, as compared to unmutated thymidine kinase. Within a further aspect, fusion proteins are provided which have both guanylate kinase and thymidine kinase biological properties. Also provided are vectors suitable for expressing such DNA molecules, as well as methods for utilizing such vectors.
REFERENCES:
patent: 4851341 (1989-07-01), Hopp
patent: 5877010 (1999-03-01), Loeb
patent: WO95/14102 (1995-05-01), None
patent: WO95/30007 (1995-11-01), None
patent: WO96/06176 (1996-02-01), None
patent: WO97/29196 (1997-08-01), None
patent: WO97/35024 (1997-09-01), None
Chica et al. Curr Opin Biotechnol. Aug. 2005;16(4):378-84.
Sen et al. Appl Biochem Biotechnol. Dec. 2007;143(3):212-23.
Accession AAT05183, Jun. 14, 1996.
Accession J03366, Feb. 20, 1989.
Graham, et. al., GenBank Accession No. X03764, (1993).
Kit, et. al., Gen Bank Accession Nos. X01712, J02225, (1993).
Balasubramaniam, et. al., “Herpesviral Deoxythymidine Kinases Contain A Site Analogous To The Phosphoryl-Binding Arginine-Rich Region Of Porcine Adenylate Kinase; Comparison Of Secondary Structure Predictions And Conservation,” J. Gen. Virol. 71: 2979-2987, 1990.
Black and Hruby, “Identification Of The ATP-Binding Domain Of Vaccinia Virus Thymidine AR Kinase,” J. Biol. Chem. 265(29):17584-17592, 1990.
Black and Loeb, “Identification Of Important Residues-Within The Putative Nucleoside Binding Site Of HSV-1 Thymidine Kinase By Random Sequence Selection: Analysis Of Selected Mutants In Vitro,” Biochemistry 32:11618-11626, 1993.
Black, et. al., “Creation Of Drug-Specific Herpes Simplex Virus Type 1 Thymidine Kinase Mutants For Gene Therapy,” Proc. Natl. Acad. Sci. USA 93:3525-359, 1996.
Black, et. al., “Effect On Substrate Binding Of An Alteration At The Conserved Aspartic Acid-162 In Herpes Simplex Virus Type 1 Thymidine Kinase,” J. Gen. Virol. 77:1521-1527, 1996.
Brown, et. al., “Crystal Structures Of The Thymidine Kinase From Herpes Simplex Virus Type-1 Incomplex With Deoxythymidine And Ganciclovir,” Nat. Struct. Biol. 2:876-881, 1995.
Chica, et. al., “Semi-Rational Approaches To Engineering Enzyme Activity: Combining The Benefits Of Directed Evolution And Rational Design,” Curr. Opin. Boitechnol. 16(4):378-384, 2005.
Deonarain, et al., “Genetic Delivery Of Enzymes For Cancer Therapy,” Gene Ther. 2:235-44, 1995.
Drake, et. al., “Metabolism And Activities Of 3′-Azido-2′,3′-Dideoxythymidine And 2′,3′-Didehydro-2′ ,3′-Dideoxythymidine In Herpesvirus Thymidine Kinase Transduced T-Lymphocytes,” Antiviral Res. 35: 177-85, 1997.
Esandi, et. al., “Gene Therapy Of Experimental Malignant Mesothelioma Using Adenovirus Vectorsencoding the HSVtk Gene,” Gene Ther. 4:280-7, 1997.
Hardy, et. al., “Atomic Structure Of Thymidylate Synthase: Target For Rational Drug Design,” Science 235:448-455, 1987.
Hopp, et. al., “A Short Polypeptide Marker Sequence Useful For Recombinant Protein Identification And Purification,” Bio/Technology 6:1204-1210, 1988.
Knoll, et. al., “Mapping Of The Active Site Of T7 RNA Polymerase With 8-azidoATP,” Biochimica et Biophysica Acta. 1121:252-260, 1992.
McKnight, “The Nucleotide Sequence And Transcript Map Of The Herpes Simplex Virus Thymidine Kinase Gene,” Nucleic Acids Res. 8(24):5949-5964, 1980.
Montfort, et. al., “Structure, Multiple Site Binding, And Segmental Accommodation In Thymidylate Synthase On Binding dUMP And An Anti-Folate,” Biochem. 29: 6964-6977, 1990.
Munch-Petersen, et. al., “Diverging Substrate Specificity Of Pure Human Thymidine Kinases 1 And 2 Against Antiviral Dideoxynucleosides,” J Biol. Chem. 266:9032-8, 1991.
Munir, et. al., “Permissible Amino Acid Substitutions Within The Putative Nucleoside Binding Site Of Herpes Simplex Virus Type 1 Encoded Thymidine Kinase Established By Random Sequence Mutagenesis,” J. Biol. Chem. 267:6584-9, 1992.
Munir, et. al., “Thymidine Kinase Mutants Obtained By Random Sequence Selection,” Proc. Natl. Acad. Sci. USA 90: 4012-4016, 1993.
Sanderson, et. al., “Purification And Crystallization Of Thymidine Kinase From Herpes Simplex Virus Type 1,” J. Mol. Biol. 202:917-919, 1988.
Sen, et. al., “Developments In Directed Evolution For Improving Enzyme Functions,” Appl. Biochem. Biotechnol. 143(3):212-223, 2007.
Waldman et al., “Purification And Characterization Of Herpes Simplex Virus (Type 1) Thymidine Kinase Produced InEscherichia coliBy A High Efficiency Expression Plasmid Utilizing A Lambda PL Promoter And CI857 Temperature-Sensitive Repressor,” J Biol. Chem. 258(19):11571-5, 1983.
Darwin Molecular Corporation
Fronda Christian L
K&L Gates LLP
Winger C. Rachal
LandOfFree
Fusion proteins having thymidine kinase and guanylate kinase... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Fusion proteins having thymidine kinase and guanylate kinase..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Fusion proteins having thymidine kinase and guanylate kinase... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2619438