Re: LSE:CAT intellectual property
The purpose of this subthread is to document and discuss the intellectual property (IP) of LSE:CAT and its competitors.
Background:
The CAT 1998 annual report makes specific reference to patents by McCafferty et. al and Winter et.al. They further note that they have purchased IP from the Medical Research Council (MRC) without specific reference. In addition, CAT purchased the US company Aptein for its IP related to polysome display. The report notes that they have both licensed technology from Dyax and oppose them in EPO proceedings.
The report notes that they have action against Morphosys for infringement.
The MRC has generated a huge number of patents so need a way of filtering, although it is listed as coapplicant on many CAT applications.
Aptein , Dyax, Morphosys and CAT competitors are NOT in this post. Only CAT related issues.
Patent Abstracts:
Following are abstracts of patents listed for McCafferty, Winter and Cambridge Antibody (when listed as applicant). (Note also that McCafferty and Winter also listed on many CAT applications.)
From the European Patent Office (EPO) we have the following :
(I'm having trouble getting the EPO .img files (facimile in PDF) read by my Acrobat reader. If you are having great success please let me know the secret!)
for McCafferty:
WO9801757 LABELLING AND SELECTION OF MOLECULES
wo.dips.org
and for Winter Greg:
WO9920749 METHOD TO SCREEN PHAGE DISPLAY LIBRARIES WITH DIFFERENT LIGANDS
wo.dips.org
A search with Cambridge Antibody shows the following (partial listing since I need to work on methods to get the cross listings e.g. US and EP and WO all together - MFM)
US5837242 WO9413804 Multivalent and multispecific binding proteins, their manufacture and use
PCT No. PCT/GB93/02492 Sec. 371 Date May 14, 1996 Sec. 102(e) Date May 14, 1996 PCT Filed Dec. 3, 1993 PCT Pub. No. WO94/13804 PCT Pub. Date Jun. 23, 1994Polypeptides comprising a first domain, which comprises a binding region of an immunoglobulin heavy chain variable region, and a second domain, which comprises a binding region of an immunoglobulin light chain variable region, the domains being linked but incapable of associating with each other to form an antigen binding site, associate to form antigen binding multimers, such as dimers, which may be multivalent or have multispecificity. The domains may be linked by a short peptide linker or may be joined directly together. Bispecific dimers may have longer linkers. Methods of preparation of the polypeptides and multimers and diverse repertoires thereof, and their display on the surface of bacteriophage for easy selection of binders of interest, are disclosed, along with many utilities.
US5969108 Methods for producing members of specific binding pairs
PCT No. PCT/GB91/01134 Sec. 371 Date Jan. 8, 1993 Sec. 102(e) Date Jan. 8, 1993 PCT Filed Jul. 10, 1991 PCT Pub. No. WO92/01047 PCT Pub. Date Jan. 23, 1992A member of a specific binding pair (sbp) is identified by expressing DNA encoding a genetically diverse population of such sbp members in recombinant host cells in which the sbp members are displayed in functional form at the surface of a secreted recombinant genetic display package (rgdp) containing DNA encoding the sbp member or a polypeptide component thereof, by virtue of the sbp member or a polypeptide component thereof being expressed as a fusion with a capsid component of the rgdp. The displayed sbps may be selected by affinity with a complementary sbp member, and the DNA recovered from selected rgdps for expression of the selected sbp members. Antibody sbp members may be thus obtained, with the different chains thereof expressed, one fused to the capsid component and the other in free form for association with the fusion partner polypeptide. A phagemid may be used as an expression vector, with said capsid fusion helping to package the phagemid DNA. Using this method libraries of DNA encoding respective chains of such multimeric sbp members may be combined, thereby obtaining a much greater genetic diversity in the sbp members than could easily be obtained by conventional methods.
US5565332 WO9306213 Production of chimeric antibodies - a combinatorial approach
Methods are disclosed which may be used for the production of antibodies, or antibody fragments, which have the same binding specificity as a parent antibody but which have increased human characteristics. Humanised antibodies may be obtained by chain shuffling, perhaps using phage display technology. In one embodiment, a polypeptide comprising a heavy or light chain variable domain of a non-human antibody specific for an antigen of interest is combined with a repertoire of human complementary (light or heavy) chain variable domains. Hybrid pairings which are specific for the antigen of interest are selected. Human chains from the selected pairings may then be combined with a repertoire of human complementary variable domains (heavy or light) and humanised antibody polypeptide dimers can then be selected for binding specificity for antigen. The methods may be combined with CDR-imprinting. In another embodiment, component part of an antigen-binding site of a non-human antibody known to bind a particular antigen is combined with a repertoire of component parts of an antigen-binding site of human antibody, forming a library of antibody polypeptide dimers with antigen-binding sites. Hybrids selected from this library may be used in a second humanising shuffling step, or may already be of sufficient human character to be of value, perhaps after some modification to increase human character still further.
US5962255 Methods for producing recombinant vectors
Methods, recombinant host cells and kits are disclosed for the production of members of specific binding pairs (sbp), e.g. antibodies, using display on the surface of secreted replicable genetic display packages (rgdps), e.g. filamentous phage. To produce a library of great diversity recombination occurs between first and second vectors comprising nucleic acid encoding first and second polypeptide chains of sbp members respectively, thereby producing recombinant vectors each encoding both a first and a second polypeptide chain component of a sbp member. The recombination may take place in vitro or intracellularly and may be site-specific, e.g. involving use of the loxP sequence and mutants thereof. Recombination may take place after prior screening or selecting for rgdps displaying sbp members which bind complementary sbp member of interest.
EP0945464 Specific binding members for human transforming growth factor beta; materials and methods
Specific binding members comprising human antibody antigen binding domains specific for human transforming growth factor beta (TGF beta ) bind specifically isoforms TGF beta 2 and TGF beta 1 or both, preferentially compared with TGF beta 3. Specific binding members may be isolated and utilised in the treatment of disease, particularly fibrotic disease and also immune/inflammatory diseases. Therapeutic utility is demonstrated using in vitro and in vivo models. Full sequence and binding information is provided, including epitope sequence information for a particularly advantageous specific binding member which binds the active form of TGF beta 2, neutralising its activity, but does not bind the latent form.
WO9923222 GB2332433 CYSTEINE NOOSE ANTIBODY LIBRARIES, MEANS FOR THEIR PRODUCTION AND USES THEREOF
The invention provides libraries comprising a repertoire of specific binding members, which binding members comprise an antibody variable domain, wherein said repertoire comprises at least 10<3> members which each carry a cysteine noose in at least one of their complementary determining regions (CDR) present in said variable domains. These binding members may be used to provide agonists or antagonists of targets such as cytokines or other proteins, and as a basis for obtaining mimetic cysteine noose peptides
US5885793 WO9311236 Production of anti-self antibodies from antibody segment repertoires and displayed on phage
PCT No. PCT/GB92/02240 Sec. 371 Date Oct. 26, 1994 Sec. 102(e) Date Oct. 26, 1994 PCT Filed Dec. 2, 1992 PCT Pub. No. WO93/11236 PCT Pub. Date Jun. 10, 1993Methods are disclosed for the production of anti-self antibodies and antibody fragments, being antibodies or fragments of a particular species of mammal which bind self-antigens of that species. Methods comprise providing a library of replicable genetic display packages (rgdps), such as filamentous phage, each rgdp displaying at its surface a member of a specific binding pair which is an antibody or antibody fragment, and each rgdp containing nucleic acid sequence derived from a species of mammal. The nucleic acid sequence in each rgdp encodes a polypeptide chain which is a component part of the sbp member displayed at the surface of that rgdp. Anti-self antibody fragments are selected by binding with a self antigen from the said species of mammal. The displayed antibody fragments may be scFv, Fd, Fab or any other fragment which has the capability of binding antigen. Nucleic acid libraries used may be derived from a rearranged V-gene sequences of unimmunised mammal. Synthetic or artificial libraries are described and shown to be useful.
US5872215 Specific binding members, materials and methods
Specific binding members for human carcinoembryonic antigen (CEA) comprise a human antibody antigen binding domain. The specific binding members may have a dissociation constant less than 1.0x10-8M and may be substantially non-crossreactive with human liver and/or other normal tissues. They may be specific for the A3-B3 extracellular domain of CEA. They may be specific for a carbohydrate epitope of CEA. They may be produced by recombinant expression from encoding nucleic acid and modified and manipulated in various manners in accordance with known techniques. CEA is a tumour antigen and the specific binding members have proven ability to bind and target CEA both in vitro and in vivo.
US5733743 WO9319172 Methods for producing members of specific binding pairs ÿ
PCT No. PCT/GB93/00605 Sec. 371 Date Nov. 18, 1994 Sec. 102(e) Date Nov. 18, 1994 PCT Filed Mar. 24, 1993 PCT Pub. No. WO93/19172 PCT Pub. Date Sep. 30, 1993Methods, recombinant host cells and kits are disclosed for the production of members of specific binding pairs (sbp), e.g. antibodies, using display on the surface of secreted replicable genetic display packages (rgdps), e.g. filamentous phage. To produce a library of great diversity, recombination occurs between first and second vectors comprising nucleic acid encoding first and second polypeptide chains of sbp members respectively, thereby producing recombinant vectors each encoding both a first and a second polypeptide chain component of an sbp member. The recombination may take place in vitro or intracellularly and may be site-specific, e.g. involving use of the loxP sequence and mutants thereof. Recombination may take place after prior screening or selecting for rgdps displaying sbp members which bind complementary sbp member of interest.
US5871907 Methods for producing members of specific binding pairs
PCT No. PCT/GB92/00883 Sec. 371 Date Mar. 31, 1994 Sec. 102(e) Date Mar. 31, 1994 PCT Filed May 15, 1992 PCT Pub. No. WO92/20791 PCT Pub. Date Nov. 26, 1992The invention provides methods and kits for producing specific binding pairs (sbp) members. Populations of polypeptide chain components of sbp members are combined to form libraries of sbps displayed by secreted replicable genetic display packages (rgdp). At least one of the polypeptide chains is expressed as a fusion with a component of an rgdp which thereby displays that polypeptide chain at the surface of rgdp. At least one population of polypeptide chains is expressed from nucleic acid which is capable of being packaged using a component of an rgdp, whereby the genetic material of rgdps produced encodes a polypeptide chain. The methods enable production of libraries of multimeric sbp members from a very large number of possible combinations. In one embodiment of the invention a method employs "chain shuffling" in the production of sbp members of desired specificity for a counterpart sbp member. Selection procedures are also described.
US5858657 Methods for producing members of specific binding pairs
The invention provides methods and kits for producing specific binding pairs (sbp) members. Populations of polypeptide chain components of sbp members are combined to form libraries of sbps displayed by secreted replicable genetic display packages (rgdp). At least one of the polypeptide chains is expressed as a fusion with a component of an rgdp which thereby displays that polypeptide chain at the surface of rgdp. At least one population of polypeptide chains is expressed from nucleic acid which is capable of being packaged using a component of an rgdp, whereby the genetic material of rgdps produced encodes a polypeptide chain. The methods enable production of libraries of multimeric sbp members from a very large number of possible combinations. In one embodiment of the invention a method employs "chain shuffling" in the production of sbp members of desired specificity for a counterpart sbp member. Selection procedures are also described.
US5837242 WO9413804 Multivalent and multispecific binding proteins, their manufacture and use ÿ
PCT No. PCT/GB93/02492 Sec. 371 Date May 14, 1996 Sec. 102(e) Date May 14, 1996 PCT Filed Dec. 3, 1993 PCT Pub. No. WO94/13804 PCT Pub. Date Jun. 23, 1994Polypeptides comprising a first domain, which comprises a binding region of an immunoglobulin heavy chain variable region, and a second domain, which comprises a binding region of an immunoglobulin light chain variable region, the domains being linked but incapable of associating with each other to form an antigen binding site, associate to form antigen binding multimers, such as dimers, which may be multivalent or have multispecificity. The domains may be linked by a short peptide linker or may be joined directly together. Bispecific dimers may have longer linkers. Methods of preparation of the polypeptides and multimers and diverse repertoires thereof, and their display on the surface of bacteriophage for easy selection of binders of interest, are disclosed, along with many utilities.
WO9720932 SPECIFIC BINDING MEMBERS FOR HUMAN CARCINOEMBRYONIC ANTIGEN, MATERIALS AND METHODS
Sequence and binding information is provided for particularly advantageous specific binding members which bind human carcinoembryonic antigen (CEA) with a dissociation constant which is less than 1,0 x 10<-8>M, are substantially non-cross-reactive with human liver cells, bind to the A3-B3 extracellular domain of human carcinoembryonic antigen and/or bind to cell-associated human carcinoembryonic antigen preferentially over soluble human carcinoembryonic antigen. These are useful particularly in determination of CEA expression by cells such as tumour cells.
WO9713844 SPECIFIC BINDING MEMBERS FOR HUMAN TRANSFORMING GROWTH FACTOR BETA; MATERIALS AND METHODS
Specific binding members comprising human antibody antigen binding domains specific for human transforming growth factor beta (TGF beta ) bind specifically isoforms TGF beta 2 and TGF beta 1 or both, preferentially compared with TGF beta 3. Specific binding members may be isolated and utilised in the treatment of disease, particularly fibrotic disease and also immune/inflammatory diseases. Therapeutic utility is demonstrated using in vitro and in vivo models. Full sequence and binding information is provided, including epitope sequence information for a particularly advantageous specific binding member which binds the active form of TGF beta 2, neutralising its activity, but does not bind the latent form.
WO9211031 TARGETTING IgE EFFECTOR CELLS TO TUMOR CELLS ÿ
The invention relates to binding molecules capable of recruiting IgE effector functions. The invention provides molecules having a first binding domain capable of binding to a tumour antigen and a second binding domain capable of binding to a Fc epsilon receptor on cells of the immune system, whereby the molecule is able to mediate IgE effector mechanisms against a tumour cell expressing the antigen
WO9201787 BINDING DOMAINS ÿ
This invention concerns binding domains e.g. single chain variable domains which are synthetic analogues of other single chain variable domains of members of an immunoglobulin family or superfamily. In the analogue, one or more amino acid residues is altered as compared to the other domain, so that the analogue is more hydrophilic than the natural domain. The altered amino acid is substituted with a residue which occurs in an analogous position in a member of an immunoglobulin family or superfamily. This increased hydrophilicity means that the synthetic analogue will show less non-specific binding than the natural domain. The analogue may retain the binding specificity of the natural domain. Alternatively, the complementarity determining regions may be altered to change the binding specificity. The invention also concerns methods for making these binding domains. |
