CA2431600A1 - Molecules with extended half-lives, compositions and uses thereof - Google Patents

Molecules with extended half-lives, compositions and uses thereof Download PDF

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Publication number
CA2431600A1
CA2431600A1 CA002431600A CA2431600A CA2431600A1 CA 2431600 A1 CA2431600 A1 CA 2431600A1 CA 002431600 A CA002431600 A CA 002431600A CA 2431600 A CA2431600 A CA 2431600A CA 2431600 A1 CA2431600 A1 CA 2431600A1
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substitution
amino acid
igg
modified
threonine
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CA2431600C (en
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William Dall'acqua
Leslie S. Johnson
Elizabeth Sally Ward
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MedImmune LLC
University of Texas System
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Medimmune, Inc.
William Dall'acqua
Leslie S. Johnson
Elizabeth Sally Ward
Board Of Regents, The University Of Texas System
Medimmune, Llc
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Priority to CA2766160A priority Critical patent/CA2766160A1/en
Publication of CA2431600A1 publication Critical patent/CA2431600A1/en
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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
    • C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
    • C07K16/283—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily against Fc-receptors, e.g. CD16, CD32, CD64
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
    • A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
    • A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
    • A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
    • A61K47/6835—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment the modifying agent being an antibody or an immunoglobulin bearing at least one antigen-binding site
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K49/00—Preparations for testing in vivo
    • A61K49/0002—General or multifunctional contrast agents, e.g. chelated agents
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K49/00—Preparations for testing in vivo
    • A61K49/0004—Screening or testing of compounds for diagnosis of disorders, assessment of conditions, e.g. renal clearance, gastric emptying, testing for diabetes, allergy, rheuma, pancreas functions
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P11/00—Drugs for disorders of the respiratory system
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
    • A61P31/12—Antivirals
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
    • A61P31/12—Antivirals
    • A61P31/14—Antivirals for RNA viruses
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
    • A61P31/12—Antivirals
    • A61P31/14—Antivirals for RNA viruses
    • A61P31/16—Antivirals for RNA viruses for influenza or rhinoviruses
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P37/00—Drugs for immunological or allergic disorders
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P37/00—Drugs for immunological or allergic disorders
    • A61P37/02—Immunomodulators
    • A61P37/04—Immunostimulants
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
    • C07K14/70503—Immunoglobulin superfamily
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2/00—Peptides of undefined number of amino acids; Derivatives thereof
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/10—Immunoglobulins specific features characterized by their source of isolation or production
    • C07K2317/14—Specific host cells or culture conditions, e.g. components, pH or temperature
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
    • C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
    • C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
    • C07K2317/52—Constant or Fc region; Isotype
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
    • C07K2317/52—Constant or Fc region; Isotype
    • C07K2317/53—Hinge
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
    • C07K2317/94—Stability, e.g. half-life, pH, temperature or enzyme-resistance
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
    • Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10S435/00—Chemistry: molecular biology and microbiology
    • Y10S435/81—Packaged device or kit

Abstract

The present invention provides molecules, including IgGs, non-IgG
immunoglobulins, proteins and non-protein agents, that have increased in vivo half-lives due to the presence of an IgG constant domain, or a portion thereof that binds the FcRn, having one or more amino acid modifications that increase the affinity of the constant domain or fragment for FcRn. Such proteins and molecules with increased half-lives have the advantage that smaller amounts and or less frequent dosing is required in the therapeutic, prophylactic or diagnostic use of such molecules.

Claims (86)

1. A modified IgG comprising an IgG constant domain comprising one or more amino acid modifications relative to a wild-type IgG constant domain, wherein the modified IgG has an increased half life compared to the half life of an IgG having the wild-type IgG
constant domain, and wherein the one or more amino acid modifications are at one or more of positions 251, 253, 255, 285-290, 308-314, 385-389, and 428-435.
2. A modified non-human IgG comprising a non-human IgG constant domain comprising one or more amino acid modifications relative to a wild-type non-human IgG
constant domain, wherein the modified IgG has an increased half life compared to the half life of an IgG having the wild-type non-human IgG constant domain, and wherein the one or more amino acid modifications are at one or more of positions 251-256, 285-290, 308-314, 385-389, and 428-436, with the proviso that the one or more amino acid modifications do not include substitution with leucine at position 252, serine at position 254, and phenylalanine at position 256.
3. A modified human or humanized IgG comprising a human IgG constant domain comprising one or more amino acid modifications relative to a wild-type human IgG
constant domain, wherein the modified human or humanized IgG has an increased half life compared to the half life of a human or humanized IgG having the wild-type human IgG
constant domain, and wherein the one or more amino acid modifications are at one or more of positions 251-256, 285-290, 308-314, 385-389, and 428-436.
4. The modified IgG according to claim 1, 2, or 3, wherein at least one of the amino acid modifications is an amino acid substitution.
5. The modified IgG according to claim 1, 2, or 3, wherein at least one of the amino acid modifications is an amino acid deletion.
6. The modified IgG according to claim 1, 2, or 3, wherein at least one of the amino acid modifications is an amino acid insertion.
7. The modified IgG according to claim 1, 2 or 3 which has a higher affinity for FcRn than the IgG having the wild-type IgG constant domain.
8. The modified IgG according to claim 7 which has a higher affinity for the FcRn at pH 6.0 than at pH 7.4.
9. The modified IgG according to claim 1, wherein said one or more amino acid modifications are amino acid substitutions at one or more of positions 251, 255, 308, 309, 311, 312, 314, 385, 386, 387, 389, 428, 433, 434, or 436.
10. The modified IgG according to claim 2 or 3, wherein said one or more amino acid modifications are amino acid substitutions at one or more of positions 251, 252, 254, 255, 256, 308, 309, 311, 312, 314, 385, 386, 387, 389, 428, 433, 434 or 336.
11. The modified IgG according to claim 1 or 3 wherein said one or more amino acid modifications are substitution with leucine at position 251, substitution with tyrosine, tryptophan or phenylalanine at position 252, substitution with threonine or serine at position 254, substitution with arginine at position 255, substitution with glutamine, arginine, serine, threonine, or glutamate at position 256, substitution with threonine at position 308, substitution with proline at position 309, substitution with serine at position 311, substitution with aspartate at position 312, substitution with leucine at position 314, substitution with arginine, aspartate or serine at position 385, substitution with threonine or proline at position 386, substitution with arginine or proline at position 387, substitution with proline, asparagine or serine at position 389, substitution with methionine or threonine at position 428, substitution with tyrosine or phenylalanine at position 434, substitution with histidine, arginine, lysine or serine at position 433, or substitution with histidine, tyrosine, arginine or threonine at position 436.
12. The modified IgG according to claim 11, wherein said one or more amino acid substitutions are substitutions with tyrosine at position 252, threonine at position 254 and glutamate at 256.
13. The modified IgG according to claim 11, wherein said one or more amino acid substitutions are substitutions with lysine at position 433, phenylalanine at position 434 and histidine at position 436.
14. The modified IgG according to claim 11, wherein said amino acid substitution is a substitution with tyrosine or tryptophan at position 252.
15. The modified IgG according to claim 2 wherein said one or more amino acid modifications are substitution with leucine at position 251, substitution with tyrosine, tryptophan or phenylaline at position 252, substitution with threonine at position 254, substitution with arginine at position 255, substitution with glutamine, arginine, serine, threonine, or glutamate at position 256, substitution with threonine at position 308, substitution with proline at position 309, substitution with serine at position 311, substitution with aspartate at position 312, substitution with leucine at position 314, substitution with arginine, aspartate or serine at position 385, substitution with threonine or proline at position 386, substitution with arginine or proline at position 387, substitution with proline, asparagine or serine at position 389, substitution with methionine or threonine at position 428, substitution with tyrosine or phenylalanine at position 434, substitution with histidine, arginine, lysine or serine at position 433, or substitution with histidine, tyrosine, arginine or threonine at position 436.
16. The modified IgG according to claim 15, wherein said one or more amino acid substitutions are substitution with tyrosine at position 252, threonine at position 254 and glutamate at 256.
17. The modified IgG according to claim 15, wherein said one or more amino acid substitutions are substitution with lysine at position 433, phenylalanine at position 434 and histidine at position 436.
18. The modified IgG according to claim 15, wherein said amino acid substitution is a substitution with tyrosine or tryptophan at position 252.
19. The modified IgG according to claim 3 or 15 which has the heavy chain variable domain and light chain variable domain of SYNAGIS®.
20. The modified IgG according to claim 3 or 15 which has the heavy chain variable domain and light chain variable domain of AFFF, p12f2, p12f4, p11d4, Ale109, A12a6, A13c4, A17d4, A4B4, A8C7, 1X-493L1FR, H3-3F4, M3H9, Y10H6, DG, AFFF(1), 6H8, L1-7E5, L215B10, A13A11, A1H5, A4B4(1), A4B4L1FR-S28R, or A4B4-F528.
21. A fusion protein comprising a non-IgG polypeptide covalently linked to a modified IgG constant domain, or a fragment thereof that binds to FcRn, said modified IgG

constant domain or fragment comprising one or more amino acid modifications relative to a wild-type IgG constant domain, wherein the one or more modifications are at one or more of positions 251, 253, 255, 285-290, 308-314, 385-389, and 428-436, and wherein said fusion protein has a longer half life than the non-IgG polypeptide alone.
22. A fusion protein comprising a non-IgG polypeptide covalently linked to a modified non-human IgG constant domain, or a fragment thereof that binds to FcRn, said modified non-human IgG constant domain or fragment comprising one or more amino acid modifications relative to a wild-type non-human IgG constant domain, wherein the one or more modifications are at one or more of positions 251-256, 285-290, 308-314, 385-389, and 428-436, with the proviso that the modified amino acid sequence does not have leucine at position 252, serine at position 254, and phenylalanine at position 256, and wherein said fusion protein has a longer half life than the non-IgG polypeptide alone.
23. A fusion protein comprising a non-IgG polypeptide covalently linked to a modified human IgG constant domain, or a fragment thereof that binds to FcRn, said modified human IgG constant domain or fragment comprising one or more amino acid modifications relative to a wild-type human IgG constant domain, wherein the one or more modifications are at one or more of positions 251-256, 285-290, 308-314, 385-389, and 428-436, and wherein said fusion protein has a longer half life than the non-IgG
polypeptide alone.
24. The fusion protein according to claim 21, 22, or 23, wherein at least one of the amino acid modifications is an amino acid substitution.
25. The fusion protein according to claim 21, 22, or 23, wherein at least one of the amino acid modifications is an amino acid deletion.
26. The fusion protein according to claim 21, 22, or 23, wherein at least one of the amino acid modifications is an amino acid insertion.
27. The fusion protein according to claim 21, 22, or 23, wherein the modified IgG
constant domain or fragment has an increased affinity for FcRn relative to the wild-type IgG
constant domain.
28. The fusion protein according to claim 27, wherein the modified IgG
constant domain or fragment has a higher affinity for the FcRn at pH 6.0 than at pH
7.4.
29. The fusion protein according to claim 21, 22, or 23, wherein the non-IgG
polypeptide is an immunoglobulin.
30. The fusion protein according to claim 21, wherein the one or more amino acid modifications are amino acid substitutions at one or more of positions 251, 255, 308, 309, 311, 312, 314, 385, 386, 387, 389, 428, 433, 434, or 436.
31. The fusion protein according to claim 22 or 23, wherein the one or more amino acid modifications are amino acid substitutions at one or more of positions 251, 252, 254, 255, 256, 308, 309, 311, 312, 314, 385, 386, 387, 389, 428, 433, 434 or 336.
32. The fusion protein according to claim 21 or 23, wherein said one or more amino acid modifications are substitution with leucine at position 251, substitution with tyrosine, tryptophan or phenylalanine at position 252, substitution with threonine or serine at position 254, substitution with arginine at position 255, substitution with glutamine, arginine, serine, threonine, or glutamate at position 256, substitution with threonine at position 308, substitution with proline at position 309, substitution with serine at position 311, substitution with aspartate at position 312, substitution with leucine at position 314, substitution with arginine, aspartate or serine at position 385, substitution with threonine or proline at position 386, substitution with arginine or proline at position 387, substitution with proline, asparagine or serine at position 389, substitution with methionine or threonine at position 428, substitution with tyrosine or phenylalanine at position 434, substitution with histidine, arginine, lysine or serine at position 433, or substitution with histidine, tyrosine, arginine or threonine at position 436.
33. The fusion protein according to claim 32, wherein said one or more amino acid substitutions are substitutions with tyrosine at position 252, threonine at position 254 and glutamate at 256.
34. The fusion protein according to claim 32, wherein said one or more amino acid substitutions are substitutions with lysine at position 433, phenylalanine at position 434 and histidine at position 436.
35. The fusion protein according to claim 32, wherein said amino acid substitution is a substitution with tyrosine or tryptophan at position 252.
36. The fusion protein according to claim 32, wherein said one or more amino acid modifications are substitution with leucine at position 251, substitution with tyrosine, tryptophan or phenylalanine at position 252, substitution with threonine at position 254, substitution with arginine at position 255, substitution with glutamine, arginine, serine, threonine, or glutamate at position 256, substitution with threonine at position 308, substitution with proline at position 309, substitution with serine at position 311, substitution with aspartate at position 312, substitution with leucine at position 314, substitution with arginine, aspartate or serine at position 385, substitution with threonine or proline at position 386, substitution with arginine or proline at position 387, substitution with proline, asparagine or serine at position 389, substitution with methionine or threonine at position 428, substitution with tyrosine or phenylalanine at position 434, substitution with histidine, arginine, lysine or serine at position 433, or substitution with histidine, tyrosine, arginine or threonine at position 436.
37. The fusion protein according to claim 36, wherein said one or more amino acid substitutions are substitutions with tyrosine at position 252, threonine at position 254 and glutamate at 256.
38. The fusion protein according to claim 36, wherein said one or more amino acid substitutions are substitutions with lysine at position 433, phenylalanine at position 434 and histidine at position 436.
39. The fusion protein according to claim 36, wherein said amino acid substitution is a substitution with tyrosine or tryptophan at position 252.
40. A molecule comprising a non-protein agent conjugated to a modified IgG
constant domain, or a fragment thereof that binds to FcRn, said modified IgG
constant domain or fragment comprising one or more amino acid modifications relative to a wild-type IgG constant domain, wherein the one or more modifications are at one or more of positions 251, 253, 255, 285-290, 308-314, 385-389, and 428-436, and wherein said molecule has a longer half life than the non-protein agent alone.
41. A molecule comprising a non-protein agent conjugated to a modified non-human IgG constant domain, or a fragment thereof that binds to FcRn, said modified non-human IgG constant domain or fragment comprising one or more amino acid modifications relative to a wild-type non-human IgG constant domain, wherein the one or more modifications are at one or more of positions 251-256, 285-290, 308-314, 385-389, and 428-436, with the proviso that the modified amino acid sequence does not have leucine at position 252, serine at position 254, and phenylalanine at position 256, and wherein said molecule has a longer half life than the non-protein agent alone.
42. A molecule comprising a non-protein agent conjugated to a modified human IgG constant domain, or a fragment thereof that binds to FcRn, said modified human IgG
constant domain or fragment comprising one or more amino acid modifications relative to a wild-type human IgG constant domain, wherein the one or more modifications are at one or more of positions 251-256, 285-290, 308-314, 385-389, and 428-436, and wherein said molecule has a longer half life than the non-protein agent alone.
43. The molecule according to claim 40, 41, or 42 wherein at least one of the amino acid modifications is an amino acid substitution.
44. The molecule according to claim 40, 41, or 42 wherein at least one of the amino acid modifications is an amino acid deletion.
45. The molecule according to claim 40, 41 or 42, wherein at least one of the amino acid modifications is an amino acid insertion.
46. The molecule according to claim 40, 41 or 42, wherein the modified IgG
constant domain or fragment has an increased affinity fox FcRn relative to the wild-type constant domain.
47. The molecule according to claim 46, wherein the modified IgG constant domain or fragment has a higher affinity for the FcRn at pH 6.0 than at pH
7.4.
48. The molecule according to claim 40, wherein the one or more amino acid modifications are amino acid substitutions at one or more of positions 251, 255, 308, 309, 311, 312, 314, 385, 386, 387, 389, 428, 433, 434, or 436.
49. The molecule according to claim 41 or 42, wherein the one or more amino acid modifications are substitution at one or more of positions 251, 252, 254, 255, 256, 308, 309, 311, 312, 314, 385, 386, 387, 389, 428, 433, 434 or 336.
50. The molecule according to claim 40 or 42, wherein said one or more amino acid modifications are substitution with leucine at position 251, substitution with tyrosine, tryptophan or phenylalanine at position 252, substitution with threonine or serine at position 254, substitution with arginine at position 255, substitution with glutamine, arginine, serine, threonine, or glutamate at position 256, substitution with threonine at position 308, substitution with proline at position 309, substitution with serine at position 311, substitution with aspartate at position 312, substitution with leucine at position 314, substitution with arginine, aspartate or serine at position 385, substitution with threonine or proline at position 386, substitution with arginine or proline at position 387, substitution with proline, asparagine or serine at position 389, substitution with methionine or threonine at position 428, substitution with tyrosine or phenylalanine at position 434, substitution with histidine, arginine, lysine or serine at position 433, or substitution with histidine, tyrosine, arginine or threonine at position 436.
51. The molecule according to claim 50, wherein said one or more amino acid substitutions are substitutions with tyrosine at position 252, threonine at position 254 and glutamate at 256.
52. The molecule according to claim 50, wherein said one or more amino acid substitutions are substitutions with lysine at position 433, phenylalanine at position 434 and histidine at position 436.
53. The molecule according to claim 50, wherein said amino acid substitution is a substitution with tyrosine or tryptophan at position 252.
54. The molecule according to claim 41, wherein said one or more amino acid modifications are substitution with leucine at position 251, substitution with tyrosine, tryptophan or phenylalanine at position 252, substitution with threonine at position 254, substitution with arginine at position 255, substitution with glutamine, arginine, serine, threonine, or glutamate at position 256, substitution with threonine at position 308, substitution with proline at position 309, substitution with serine at position 311, substitution with aspartate at position 312, substitution with leucine at position 314, substitution with arginine, aspartate or serine at position 385, substitution with threonine or proline at position 386, substitution with arginine or proline at position 387, substitution with proline, asparagine or serine at position 389, substitution with methionine or threonine at position 428, substitution with tyrosine or phenylalanine at position 434, substitution with histidine, arginine, lysine or serine at position 433, or substitution with histidine, tyrosine, arginine or threonine at position 436.
55. The molecule according to claim 54, wherein said one or more amino acid substitutions are substitutions with tyrosine at position 252, threonine at position 254 and glutamate at 256.
56. The molecule according to claim 54, wherein said one or more amino acid substitutions are substitutions with lysine at position 433, phenylalanine at position 434 and histidine at position 436.
57. The molecule according to claim 54, wherein said amino acid substitution is a substitution with tyrosine or tryptophan at position 252.
58. A pharmaceutical composition comprising the modified human or humanized IgG according to claim 3 and a pharmaceutically acceptable carrier.
59. A pharmaceutical composition comprising the fusion protein according to claim 23 and a pharmaceutically acceptable carrier.
60. A pharmaceutical composition comprising the molecule according to claim 42 and a pharmaceutically acceptable carrier.
61. A method of treating a disease or disorder comprising administering to a patient in need thereof a therapeutically effective amount of the modified human or humanized IgG according to claim 3.
62. The method according to claim 61 which comprises passive immunotherapy.
63. A method of treating a disease or disorder comprising administering to a patient in need thereof a therapeutically effective amount of the fusion protein according to claim 23.
64. A method of treating a disease or disorder comprising administering to a patient in need thereof a therapeutically effective amount of the molecule according to claim 42.
65. A nucleic acid comprising a nucleotide sequence encoding the modified IgG
constant domain according to claim 1, 2 or 3, or an FcRn binding fragment thereof.
66. A nucleic acid comprising a nucleotide sequence encoding the fusion protein according to claim 21, 22, or 23.
67. A host cell comprising the nucleic acid according to claim 65.
68. A host cell comprising the nucleic acid according to claim 66.
69. A kit comprising the modified human or humanized IgG according to claim 3.
70. A kit comprising the fusion protein according to claim 23.
71. A kit comprising the molecule according to claim 42.
72. A method of preventing a disease or disorder comprising administering to a subject a prophylactically effective amount of the modified human or humanized IgG
according to claim 3.
73. The method according to claim 72 which is passive immunotherapy.
74. The method according to claim 72 wherein the disease is RSV infection.
75. The method according to claim 74, wherein said modified human or humanized IgG is a modified SYNAGIS® antibody.
76. The method according to claim 74, wherein said modified human or humanized IgG is a modified AFFF, p 12f2, p 12f4, p11d4, Ale109, A12a6, A13c4, A17d4, A4B4, A8C7, 1X-493L1FR, H3-3F4, M3H9, Y10H6, DG, AFFF(1), 6H8, L1-7E5, L215B10, A13A11, A1H5, A4B4(1), A4B4L1FR-S28R or A4B4-F52S antibody.
77. A method of vaccinating a subject comprising administering to said subject an amount of the modified human or humanized IgG according to claim 3 effective to elicit an immune response.
78. A method of vaccinating a subject comprising administering to said subject an amount of the fusion protein according to claim 23 effective to elicit an immune response.
79. The method according to 61 which comprises administrating a dose of said modified human or humanized IgG that is lower than the lowest therapeutically effective dose of a second IgG identical to said modified human or humanized IgG except that said second IgG lacks said one or more amino acid modifications.
80. The method according to claim 79 which results in fewer or less severe side effects than administration of the therapeutically effective dose of the second IgG.
81. The method according to claim 61 which comprises administering a therapeutically effective dosing schedule having less frequent doses of said modified human or humanized IgG than the therapeutically effective dosing schedule having the least frequent dosing of a second IgG identical to said modified human or humanized IgG
except that said second IgG lacks said one or more amino acid modifications.
82. The method according to claim 72 which comprises administrating a prophylactically effective dose of said modified human or humanized IgG that is lower than the lowest prophylactically effective dose of a second IgG identical to said modified human or humanized IgG except that said second IgG lacks said one or more amino acid modifications.
83. The method according to claim 82 which results in fewer or less severe side effects than administration of the prophylactically effective dose of the second IgG.
84. The method according to claim 72 which comprises administering a prophylactically effective dosing schedule having less frequent doses of said modified human or humanized IgG than the prophylactically effective dosing schedule with the least frequent dosing of a second IgG identical to said humani or humanized IgG except that said second IgG lacks said one or more amino acid modifications.
85. A method of in vivo diagnosis in a subject comprising:
(a) administering to a subject an effective amount of the modified human or humanized IgG according to claim 3 labeled with a detectable marker, said modified human or humanized IgG specifically binding to an antigen associated with a disease or disorder;
(b) allowing the modified human or humanized IgG to concentrate at sites in said subject where said antigen is found; and (c) detecting said detectable marker, whereby detection of said detectable marker above a background or standard level indicates that the subject has said disease or disorder.
86. The modified human or humanized IgG according to claim 3 which immunospecifically binds to an RSV antigen.
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