Mutant interleukin-2 (IL-2) polypeptides

Drug – bio-affecting and body treating compositions – Lymphokine – Interleukin

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C530S351000, C530S402000

Reexamination Certificate

active

07951360

ABSTRACT:
The present invention relates to IL-2 mutants with increased affinity for the IL-2 alpha-receptor subunit (IL-2Rα). The invention thus includes IL-2 mutants with improved biological potency. The invention also includes methods for directed evolution of IL-2α using yeast surface display to generate mutants with increased affinity for IL-2Rα.

REFERENCES:
patent: 4853332 (1989-08-01), Mark et al.
patent: 5116964 (1992-05-01), Capon et al.
patent: 6451308 (2002-09-01), Strom et al.
patent: 6617135 (2003-09-01), Gillies et al.
patent: WO 99/60128 (1999-11-01), None
Mikayama et al., Proct. Natl. Acad. Sci. USA vol. 90, pp. 10056-10060.
Voet et al., Biochemistry John Wiley & Sons, Inc., pp. 126-128 and 228-234.
Arima et al., “Pseudo-High Affinity Interleukin 2 (IL-2) Receptor Lacks the Third Component That Is Essential for Functional IL-2 Binding and Signaling”J. Exp. Med. 176:1265-1272 (1992).
Atkins et al., “High-Dose Recombinant Interleukin 2 Therapy for Patients with Metastic Melanoma: Analysis of 270 Patients Treated Between 1985 and 1993”J. Clin. Oncol. 17(7):2105-2116 (1999).
Bamborough et al., “The interleukin-2 and interleukin-4 receptors studied by molecular modelling”Structure2:839-851 (1994).
Berndt et al., “Mutagenic Analysis of a Receptor Contact Site on Interleukin-2: Preparation of an IL-2 Analog with Increased Potency”Biochemistry33:6571-6577 (1994).
Blanar et al., “Interaction Cloning: Identification of a Helix-Loop—Helix Zipper Protein That Interacts With c-Fos”Science256:1014-1018 (1992).
Boder et al., “Yeast Surface Display for Directed Evolution of Protein Expression, Affinity, and Stability”Methods Enzymol. 328:430-444 (2000).
Boder et al., “Yeast surface display for screening combinatorial polypeptide libraries”Nat. Biotechnol. 15:553-557 (1997).
Brekke et al., “Structure-Function Relationships of Human IgG”The Immunologist2:125-130 (1994).
Buchli et al., “The Functional Display of Interleukin-2 on Filamentous Phage”Arch. Biochem. Biophys. 339:79-84 (1997).
Dubois et al., “IL-15Rα Recycles and Presents IL-15 intransto Neighboring Cells”Immunity17:537-547 (2002).
Dudley et al., “Cancer Regression and Autoimmunity in Patients After Clonal Repopulation with Antitumor Lymphocytes”Science298:850-854 (2002).
Eicher et al., “IL-2Rα on One Cell Can Present IL-2 to IL-2Rβ/γcon Another Cell to Augment IL-2 Signaling”J. of Immunol. 161(10):5430-5437 (1998).
Fallon et al., “Increased Endosomal Sorting of Ligand to Recycling Enhances Potency of an Interleukin-2 Analog”J. Biol Chem. 275(10):6790-6797 (2000).
Fehniger et al., “Interleukin 15: biology and relevance to human disease”Blood97(1):14-32 (2001).
Fyfe et al., “Results of Treatment of 255 Patients With Metastatic Renal Cell Carcinoma Who Received High-Dose Recombinant Interleukin-2 Therapy”J. Clin. Oncol. 13:688-696 (1995).
Guthridge et al., “Mechanism of Activation of the GM-CSF, IL-3, and IL-5 Family of Receptors”Stem Cells16:310-313 (1998).
Hémar et al., “Endocytosis of Interleukin 2 Receptors in Human T Lymphocytes: Distinct Intracellular Localization and Fate of the Receptor α, β, and γ Chains”J. Cell Biol. 129(1):55-64 (1995).
Hori et al., “Establishment of an Interleukin 2-Dependent Human T Cell Line From a Patient With T Cell Chronic Lymphocytic Leukemia Who Is Not Infected With Human T Cell Leukemia / Lymphoma Virus”Blood70:1069-1072 (1987).
Jacobson et al., “Rational interleukin 2 therapy for HIV positive individuals: Daily low doses enhance immune function without toxicity”Proc. Natl. Acad. Sci. USA93:10405-10410 (1996).
Konrad et al., “Pharmacokinetics of Recombinant Interleukin 2 in Humans”Cancer Res. 50:2009-2017 (1990).
LeClair et al., “The p50 subunit of NF-κB associates with the NF-IL6 transcription factor”Proc. Natl. Acad. Sci. USA89:8145-8149 (1992).
Liparoto et al., “Analysis of the Role of the Interleukin-2 Receptor γ Chain in Ligand Binding”Biochemistry41:2543-2551 (2002).
Lowman et al., “Selecting High-Affinity Binding Proteins by Monovalent Phage Display”Biochemistry30:10832-10838 (1991).
Morrison et al., “Structural Determinants of Human IgG Function”The Immunologist2:119-124 (1994).
Nelson et al., “Biology of the Interleukin-2 Receptor”Adv. Immunol. 70:1-81 (1998).
Parmley et al., “Antibody-selectable filamentous fd phage vectors: affinity purification of target genes”Gene73:305-318 (1988).
Rao et al., “Interleukin-2 mutants with enhanced α-receptor subunit binding affinity”Protein Engineering16(2):1081-1087 (2003).
Raymond et al., “General Method for Plasmid Construction Using Homologous Recombination”BioTechniques26:134-141 (1999).
Saggio et al., “CNTF variants with increased biological potency and receptor selectivity define a functional site of receptor interaction”EMBO J. 14:3045-3054 (1995).
Shanafelt et al., “A T-cell-selective interleukin 2 mutein exhibits potent antitumor activity and is well tolerated in vivo”Nature Biotechnol. 18:1197-202 (2000).
Smith “Cell Growth Signal Transduction is Quantal”Receptor Activation by Antigens, Cytokines, Hormones and Growth Factors766:263-271 (1995).
Smith, “The Interleukin 2 Receptor”Annu. Rev. Cell Biol. 5:397-425 (1989).
Smith, “Lowest Dose Interleukin-2 Immunotherapy”Blood81(6):1414-1423 (1993).
Teshigawara et al., “Interleukin 2 High-Affinity Receptor Expression Requires Two Distinct Binding Proteins”J. Exp. Med. 165:223-238 (1987).
Theze et al., “Interleukin 2 and its receptors: recent advances and new immunological functions”Immunol. Today17:481-486 (1996).
Toniatti et al., “Engineering human interleukin-6 to obtain variants with strongly enhanced bioactivity”EMBO. J. 15(11):2726-2737 (1996).
Voss et al., “Characterization of the Interleukin 2 Receptors (IL-2R) Expressed on Human Natural Killer Cells Activated In Vivo by IL-2: Association of the p64 Il-2R γ Chain with the IL-2R β Chain in Functional Intermediate-Affinity IL-2R”J. Exp. Med. 176:531-541 (1992).
Waldmann et al., “Contrasting Roles of IL-2 and IL-15 in the Life and Death of Lymphocytes: Implications for Immunotherapy”Immunity14:105-110 (2001).
Wu et al., “Solution assembly of the pseudo-high affinity and intermediate affinity interleukin-2 receptor complexes”Protein Sci. 8:482-489 (1999).
Zaccolo et al., “An Approach to Random Mutagenesis of DNA Using Mixtures of Triphosphate Derivatives of Nucleoside Analogues”J. Mol. Biol. 255:589-603 (1996).
Zaccolo et al., “The Effect of High-frequency Random Mutagenesis on in Vitro Protein Evolution: A Study of TEM-1 β-Lactamase”J. Mol. Biol. 285:775-783 (1999).
Wang et al., “The Importance of Amino Acid Residues 62 and 126 to the Biological Function of Interlukin-2,” Acta Biochimica et Biophysica Sinica, vol. 25(5):558-560 (Sep. 1993).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Mutant interleukin-2 (IL-2) polypeptides does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Mutant interleukin-2 (IL-2) polypeptides, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Mutant interleukin-2 (IL-2) polypeptides will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-2635907

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.