US2005260215A1PendingUtilityA1

Conjugate between a modified superantigen and a target-seeking compound and the use of the conjugate

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Assignee: ABRAHMSEN LARSPriority: Jul 11, 1994Filed: Jul 29, 2005Published: Nov 24, 2005
Est. expiryJul 11, 2014(expired)· nominal 20-yr term from priority
Inventors:Lars AbrahmsenPer BjorkMikael DohlstenTerje Kalland
C07K 16/30C07K 2319/30A61K 38/00A61P 31/12A61K 2039/505C07K 2319/00A61P 35/00C07K 16/3046A61P 37/02A61K 47/6863C07K 14/31C07K 19/00C07K 2317/55
52
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Claims

Abstract

Methods of lysing cells associated with a disease condition, and method of treating a disease condition by lysing cells associated with the condition, by administering to a mammal a therapeutically effective amount of a conjugate comprising a biospecific affinity counterpart and a peptide that is derived from Staphylococcal enterotoxin A, that has the ability to bind to a Vβ of a T cell receptor and has been modified at amino acid position 47, 128, 187, 225 or 227, in order to have reduced ability to bind to MHC class II antigens.

Claims

exact text as granted — not AI-modified
1 - 13 . (canceled)  
   
   
       14 . A method for the lysis of cells associated with a disease condition in a mammal, which condition is associated with the presence of cells expressing a specific cell surface structure, comprising the step of: 
 administering to the mammal a therapeutically effective amount of a comprising a bacterial superantigen and a biospecific affinity counterpart, wherein    (1) the biospecific affinity counterpart is capable of binding to a specific cell surface structure, and    (2) the superantigen comprises a peptide that:    i. contains an amino acid sequence that is derived from Staphylococcal enterotoxin A, wherein said peptide has the ability to bind to a Vβ chain of a T cell receptor, and    ii. has been modified at an amino acid position 47, 128, 187, 225 or 227, in order to have reduced ability to bind to MHC class II antigens.    
   
   
       15 . The method of  claim 14 , wherein said amino acid modification is a substitution to alanine.  
   
   
       16 . The method of  claim 14 , wherein said amino acid modification is a substitution that is not a conserved substitution of the amino acid at that position in Staphylococcal enterotoxin A.  
   
   
       17 . The method of  claim 14 , wherein the specific cell surface structure is a cancer specific epitope.  
   
   
       18 . The method of  claim 17 , wherein the specific cell surface structure is the C242 epitope.  
   
   
       19 . The method of  claim 14 , wherein the biospecific affinity counterpart is an antibody or an antigen-binding fragment of an antibody.  
   
   
       20 . The method of  claim 19 , wherein the biospecific affinity counterpart is an antigen-binding fragment of an antibody.  
   
   
       21 . The method of  claim 20 , wherein the fragment of an antibody is selected from the group consisting of Fab, F(ab) 2 , Fv, and single chain antibody.  
   
   
       22 . The method of  claim 19 , wherein the biospecific affinity counterpart is monoclonal antibody C242.  
   
   
       23 . The method of  claim 19 , wherein the biospecific affinity counterpart is monoclonal antibody C215.  
   
   
       24 . The method of  claim 14 , wherein the modification is at amino acid position 47.  
   
   
       25 . The method of  claim 14 , wherein the modification is at amino acid position 128.  
   
   
       26 . The method of  claim 14 , wherein the modification is at amino acid position 187.  
   
   
       27 . The method of  claim 14 , wherein the modification is at amino acid position 225.  
   
   
       28 . The method of  claim 14 , wherein the modification is at amino acid position 227.  
   
   
       29 . The method of  claim 14 , wherein the modification is a substitution to serine at amino acid position 227.  
   
   
       30 . The method of  claim 14 , wherein the modification is at amino acid positions 47, 128, 187, 225 and 227.  
   
   
       31 . The method of  claim 15 , wherein the modification is at amino acid positions 47.  
   
   
       32 . The method of  claim 15 , wherein the modification is at amino acid position 128.  
   
   
       33 . The method of  claim 15 , wherein the modification is at amino acid position 187.  
   
   
       34 . The method of  claim 15 , wherein the modification is at amino acid position 225.  
   
   
       35 . The method of  claim 15 , wherein the modification is at amino acid position 227.  
   
   
       36 . The method of  claim 15 , wherein the modification is at amino acid positions 47, 128, 187, 225 and 227.  
   
   
       37 . The method of  claim 16 , wherein the modification is at amino acid position 47.  
   
   
       38 . The method of  claim 16 , wherein the modification is at amino acid position 128.  
   
   
       39 . The method of  claim 16 , wherein the modification is at amino acid position 187.  
   
   
       40 . The method of  claim 16 , wherein the modification is at amino acid position 225.  
   
   
       41 . The method of  claim 16 , wherein the modification is at amino acid position 227.  
   
   
       42 . The method of  claim 16 , wherein the modification is at amino acid positions 47, 128, 187, 225 and 227.  
   
   
       43 . A method for the lysis of cells associated with a disease condition in a mammal, which condition is associated with the presence of cells expressing a specific cell surface structure, comprising the step of: 
 administering to the mammal a therapeutically effective amount of a pharmaceutical composition comprising:    (A) a conjugate comprising a bacterial superantigen and a biospecific affinity counterpart, wherein    (1) the biospecific affinity counterpart is capable of binding to a specific cell surface structure, and    (2) the superantigen comprises a peptide that:    i. contains an amino acid sequence that is derived from Staphylococcal enterotoxin A, wherein said peptide has the ability to bind to a Vβ chain of a T cell receptor, and    ii. has been modified at an amino acid position 47, 128, 187, 225 or 227, in order to have reduced ability to bind to MHC class II antigens; and    (B) a pharmaceutically acceptable vehicle.    
   
   
       44 . The method of  claim 43 , wherein said amino acid modification is a substitution to alanine.  
   
   
       45 . The method of  claim 43 , wherein said amino acid modification is a substitution that is not a conserved substitution of the amino acid at that position in Staphylococcal enterotoxin A.  
   
   
       46 . The method of  claim 43 , wherein the specific cell surface structure is a cancer specific epitope.  
   
   
       47 . The method of  claim 46 , wherein the specific cell surface structure is the C242 epitope.  
   
   
       48 . The method of  claim 43 , wherein the biospecific affinity counterpart is an antibody or an antigen-binding fragment of an antibody.  
   
   
       49 . The method of  claim 48 , wherein the biospecific affinity counterpart is an antigen-binding fragment of an antibody.  
   
   
       50 . The method of  claim 49 , wherein the fragment of an antibody is selected from the group consisting of Fab, F(ab) 2 , Fv, and single chain antibody.  
   
   
       51 . The method of  claim 48 , wherein the biospecific affinity counterpart is monoclonal antibody C242.  
   
   
       52 . The method of  claim 48 , wherein the biospecific affinity counterpart is monoclonal antibody C215.  
   
   
       53 . The method of  claim 43 , wherein the modification is at amino acid position 47.  
   
   
       54 . The method of  claim 43 , wherein the modification is at amino acid position 128.  
   
   
       55 . The method of  claim 43 , wherein the modification is at amino acid position 187.  
   
   
       56 . The method of  claim 43 , wherein the modification is at amino acid position 225.  
   
   
       57 . The method of  claim 43 , wherein the modification is at amino acid position 227.  
   
   
       58 . The method of  claim 43 , wherein the modification is a substitution to serine at amino acid position 227.  
   
   
       59 . The method of  claim 43 , wherein the modification is at amino acid positions 47, 128, 187, 225 and 227.  
   
   
       60 . The method of  claim 44 , wherein the modification is at amino acid position 47.  
   
   
       61 . The method of  claim 44 , wherein the modification is at amino acid position 128.  
   
   
       62 . The method of  claim 44 , wherein the modification is at amino acid position 187.  
   
   
       63 . The method of  claim 44 , wherein the modification is at amino acid position 225.  
   
   
       64 . The method of  claim 44 , wherein the modification is at amino acid position 227.  
   
   
       65 . The method of  claim 44 , wherein the modification is at amino acid positions 47, 128, 187, 225 and 227.  
   
   
       66 . The method of  claim 45 , wherein the modification is at amino acid position 47.  
   
   
       67 . The method of  claim 45 , wherein the modification is at amino acid position 128.  
   
   
       68 . The method of  claim 45 , wherein the modification is at amino acid position 187.  
   
   
       69 . The method of  claim 45 , wherein the modification is at amino acid position 225.  
   
   
       70 . The method of  claim 45 , wherein the modification is at amino acid position 227.  
   
   
       71 . The conjugate of  claim 45 , wherein the modification is at amino acid positions 47, 128, 187, 225 and 227.

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