Claims
- 1. A composition comprising three polypeptides, wherein each polypeptide comprises a triple helix formation sequence, wherein each polypeptide comprises at least two interpolypeptide linkages such that each polypeptide is covalently attached to at least one of the other two polypeptides of said three polypeptides, and wherein at least one of said interpolypeptide linkages comprises an Ahx-Lys bond.
- 2. The composition of claim 1, wherein said triple helix formation sequence of at least one of said three polypeptides comprises (Gly-Pro-Hyp).
- 3. The composition of claim 1, wherein said triple helix formation sequence of at least one of said three polypeptides comprises (Gly-Pro-Flp).
- 4. The composition of claim 1, wherein at least one of said interpolypeptide linkages comprises a Cys-Cys bond.
- 5. The composition of claim 1, wherein at least one of said three polypeptides comprises a (Gly-Xaa-Yaa)n sequence, said n being an integer from 1 to 100.
- 6. The composition of claim 1, wherein at least one of said three polypeptides comprises a (Gly-Pro-Hyp)x(Gly-Xaa-Yaa)y(Gly-Pro-Hyp)z sequence, wherein said x, y, and z are independently integers from 1 to 100.
- 7. The composition of claim 1, wherein at least one of said interpolypeptide linkages for each polypeptide is located in an N-terminal region.
- 8. The composition of claim 1, wherein at least one of said interpolypeptide linkages for each polypeptide is located in a C-terminal region.
- 9. The composition of claim 1, wherein at least one of said interpolypeptide linkages for each polypeptide is located in an N-terminal region, and wherein at least one of said interpolypeptide linkages for each polypeptide is located in a C-terminal region.
- 10. The composition of claim 1, wherein at least one of said three polypeptides is covalently attached to the other two polypeptides of said three polypeptides.
- 11. The composition of claim 1, wherein each polypeptide is covalently attached to the other two polypeptides of said three polypeptides.
- 12. The composition of claim 1, wherein at least one of said three polypeptides comprises a modified amino acid residue.
- 13. The composition of claim 12, wherein said modified amino acid residue is a glycosylated amino acid residue.
- 14. The composition of claim 1, wherein each polypeptide comprises a modified amino acid residue.
- 15. The composition of claim 1, wherein at least one of said three polypeptides comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
- 16. The composition of claim 1, wherein each polypeptide comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
- 17. A composition comprising three polypeptides, wherein each polypeptide comprises a triple helix formation sequence, wherein each polypeptide comprises at least one interpolypeptide linkage such that each polypeptide is attached to at least one of the other two polypeptides of said three polypeptides, and wherein at least one of said three polypeptides comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
- 18. The composition of claim 17, wherein said triple helix formation sequence of at least one of said three polypeptides comprises (Gly-Pro-Hyp).
- 19. The composition of claim 17, wherein said triple helix formation sequence of at least one of said three polypeptides comprises (Gly-Pro-Flp).
- 20. The composition of claim 17, wherein at least one of said interpolypeptide linkages comprises an Ahx-Lys bond.
- 21. The composition of claim 17, wherein at least one of said interpolypeptide linkages comprises a Cys-Cys bond.
- 22. The composition of claim 17, wherein at least one of said three polypeptides comprises a (Gly-Xaa-Yaa)n sequence, said n being an integer from 1 to 100.
- 23. The composition of claim 17, wherein at least one of said three polypeptides comprises a (Gly-Pro-Hyp)x(Gly-Xaa-Yaa)y(Gly-Pro-Hyp)z sequence, wherein said x, y, and z are independently integers from 1 to 100.
- 24. The composition of claim 17, wherein at least one of said interpolypeptide linkages for each polypeptide is located in an N-terminal region.
- 25. The composition of claim 17, wherein at least one of said interpolypeptide linkages for each polypeptide is located in a C-terminal region.
- 26. The composition of claim 17, wherein at least one of said interpolypeptide linkages for each polypeptide is located in an N-terminal region, and wherein at least one of said interpolypeptide linkages for each polypeptide is located in a C-terminal region.
- 27. The composition of claim 17, wherein at least one of said three polypeptides is covalently attached to the other two polypeptides of said three polypeptides.
- 28. The composition of claim 17, wherein each polypeptide is covalently attached to the other two polypeptides of said three polypeptides.
- 29. The composition of claim 17, wherein at least one of said three polypeptides comprises a modified amino acid residue.
- 30. The composition of claim 29, wherein said modified amino acid residue is a glycosylated amino acid residue.
- 31. The composition of claim 17, wherein each polypeptide comprises a modified amino acid residue.
- 32. The composition of claim 17, wherein each polypeptide comprises at least two interpolypeptide linkages.
- 33. A composition comprising three polypeptides, wherein each polypeptide comprises a triple helix formation sequence, wherein each polypeptide comprises at least one interpolypeptide linkage such that each polypeptide is covalently attached to at least one of the other two polypeptides of said three polypeptides, and wherein at least one of said three polypeptides comprises a glycosylated amino acid residue.
- 34. The composition of claim 33, wherein at least one of said three polypeptides comprises a modified lysine residue.
- 35. The composition of claim 33, wherein at least one of said three polypeptides comprises a lysine-dinitrophenyl.
- 36. The composition of claim 33, wherein at least one of said three polypeptides comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
- 37. The composition of claim 33, wherein each polypeptide comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
- 38. A composition comprising three polypeptides, wherein each polypeptide comprises at least one interpolypeptide linkage such that each polypeptide is attached to at least one of the other two polypeptides of said three polypeptides, and wherein at least one polypeptide of said three polypeptides comprises (Gly-Pro-Flp).
- 39. The composition of claim 38, wherein each polypeptide of said three polypeptides comprises (Gly-Pro-Flp).
- 40. The composition of claim 38, wherein at least one of said three polypeptides comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
- 41. The composition of claim 38, wherein each polypeptide comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
- 42. A method for detecting an antibody in a sample from a mammal, wherein said antibody has specificity for a triple polypeptide complex, wherein said triple polypeptide complex comprises three polypeptides, wherein each of said three polypeptides comprises a triple helix formation sequence, wherein each of said three polypeptides comprises at least one interpolypeptide linkage such that each polypeptide is attached to at least one of the other two polypeptides of said three polypeptides, and wherein:
(i) each polypeptide comprises at least two interpolypeptide linkages; (ii) at least one polypeptide of said three polypeptides comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56; (iii) at least one polypeptide of said three polypeptides comprises a modified amino acid residue; or (iv) at least one polypeptide of said three polypeptides comprises (Gly-Pro-Flp), said method comprising: (a) contacting said sample with said triple polypeptide complex, and (b) determining the presence or absence of said antibody bound to said triple polypeptide complex, wherein the presence of bound antibody indicates that said sample contains said antibody.
- 43. The method of claim 42, wherein said mammal is a human.
- 44. The method of claim 42, wherein said sample is serum.
- 45. The method of claim 42, wherein said antibody is an anti-collagen antibody.
- 46. The method of claim 42, wherein said antibody is bound to a B-cell.
- 47. The method of claim 42, wherein said antibody is a circulating antibody.
- 48. A method for detecting a T-cell in a sample from a mammal, wherein said T-cell is reactive to a triple polypeptide complex, wherein said triple polypeptide complex comprises three polypeptides, wherein each of said three polypeptides comprises a triple helix formation sequence, wherein each of said three polypeptides comprises at least one interpolypeptide linkage such that each polypeptide is attached to at least one of the other two polypeptides of said three polypeptides, and wherein:
(i) each polypeptide comprises at least two interpolypeptide linkages; (ii) at least one polypeptide of said three polypeptides comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56; (iii) at least one polypeptide of said three polypeptides comprises a modified amino acid residue; or (iv) at least one polypeptide of said three polypeptides comprises (Gly-Pro-Flp), said method comprising: (a) contacting said sample with said triple polypeptide complex, and (b) determining the presence or absence of T-cell activation, wherein the presence of said T-cell activation indicates that said sample contains said T-cell.
- 49. The method of claim 48, wherein said mammal is a human.
- 50. The method of claim 48, wherein said sample is a blood sample.
- 51. The method of claim 48, wherein said T-cell is a CD4+T-cell.
- 52. A method of enhancing, in a mammal, tolerance to an endogenous polypeptide, said method comprising administering a composition to said mammal under conditions effective to enhance said tolerance, said composition comprising three polypeptides, wherein each of said three polypeptides comprises a triple helix formation sequence and at least one interpolypeptide linkage such that each of said three polypeptides is covalently attached to at least one of the other two polypeptides of said three polypeptides.
- 53. The method of claim 52, wherein said endogenous polypeptide is a triple helical polypeptide.
- 54. The method of claim 53, wherein said triple helical polypeptide is type II collagen.
- 55. The method of claim 52, wherein each of said three polypeptides comprises at least two interpolypeptide linkages.
- 56. The method of claim 52, wherein at least one of said three polypeptides comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
- 57. The method of claim 52, wherein at least one of said three polypeptides comprises a modified amino acid residue.
- 58. The method of claim 52, wherein at least one polypeptide of said three polypeptides comprises (Gly-Pro-Flp).
- 59. A method of forming, in a mammal, a triple helical polypeptide-antibody complex, said method comprising administering an antibody to said mammal under conditions effective to form said triple helical polypeptide-antibody complex with a triple helical polypeptide, said antibody having specificity for a triple polypeptide complex, wherein said triple polypeptide complex comprises three polypeptides, wherein each polypeptide comprises a triple helix formation sequence and at least one interpolypeptide linkage such that each polypeptide is attached to at least one of the other two polypeptides of said three polypeptides, and wherein at least one polypeptide of said three polypeptides comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
- 60. The method of claim 59, wherein said triple helical polypeptide is type II collagen.
- 61. A method of enhancing, in a mammal, tolerance to an endogenous polypeptide, said method comprising administering an isolated nucleic acid molecule to a somatic cell of said mammal under conditions effective to enhance said tolerance, wherein said nucleic acid molecule comprises a nucleic acid sequence that encodes a polypeptide comprising a triple helix formation sequence.
- 62. The method of claim 61, wherein said mammal has arthritis.
- 63. The method of claim 61, wherein said endogenous polypeptide is a triple helical polypeptide.
- 64. The method of claim 61, wherein said triple helical polypeptide is type II collagen.
- 65. The method of claim 61, wherein said somatic cell is selected from the group consisting of fibroblasts and fibrocytes.
- 66. The method of claim 61, wherein said polypeptide comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
- 67. A method of enhancing, in a mammal, tolerance to an endogenous polypeptide, said method comprising administering cells to said mammal under conditions effective to enhance said tolerance, wherein said cells comprise an isolated nucleic acid molecule encoding a polypeptide comprising a triple helix formation sequence.
- 68. The method of claim 67, wherein said mammal has arthritis.
- 69. The method of claim 67, wherein said endogenous polypeptide is a triple helical polypeptide.
- 70. The method of claim 67, wherein said triple helical polypeptide is type II collagen.
- 71. The method of claim 67, wherein said polypeptide comprises an amino acid sequence at least about 80 percent identical to the sequence set forth in SEQ ID NO:3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 49, 50, 51, 52, 53, 54, 55, or 56.
CROSS-REFERENCE TO RELATED APPLICATIONS
[0001] This application claims priority to U.S. Application Serial No. 60/305,048, which was filed on Jul. 12, 2001.
Provisional Applications (1)
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Number |
Date |
Country |
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60305048 |
Jul 2001 |
US |