EP0823941A1 - Menschliche antikörper aus xenomäusen - Google Patents
Menschliche antikörper aus xenomäusenInfo
- Publication number
- EP0823941A1 EP0823941A1 EP95918935A EP95918935A EP0823941A1 EP 0823941 A1 EP0823941 A1 EP 0823941A1 EP 95918935 A EP95918935 A EP 95918935A EP 95918935 A EP95918935 A EP 95918935A EP 0823941 A1 EP0823941 A1 EP 0823941A1
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- EP
- European Patent Office
- Prior art keywords
- human
- analog
- immunoglobulin
- antigen
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- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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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
- C07K16/2812—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 CD4
-
- 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
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1267—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria
- C07K16/1282—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria from Clostridium (G)
-
- 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
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/241—Tumor Necrosis Factors
-
- 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
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/244—Interleukins [IL]
-
- 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
- C07K16/2851—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 lectin superfamily, e.g. CD23, CD72
- C07K16/2854—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 lectin superfamily, e.g. CD23, CD72 against selectins, e.g. CD62
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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
- C07K16/2875—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 NGF/TNF superfamily, e.g. CD70, CD95L, CD153, CD154
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/42—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins
- C07K16/4283—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins against an allotypic or isotypic determinant on Ig
- C07K16/4291—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins against an allotypic or isotypic determinant on Ig against IgE
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Definitions
- the invention relates to the field of immunology, and in particular to the production of antibodies. More specifically, it concerns producing such antibodies by a process which includes the step of immunizing a transgenic animal with an antigen to which antibodies are desired.
- the transgenic animal has been modified so as to produce human, as opposed to endogenous antibodies.
- Antibodies with various i munospecificities are desirable for therapeutic and diagnostic use.
- Those antibodies intended for human therapeutic and in vivo diagnostic use, in particular, have been problematic because prior art sources for such antibodies resulted in immunoglobulins bearing the characteristic structures of antibodies produced by nonhuman hosts. Such antibodies tend to be immunogenic when used in humans.
- the invention is directed to methods to produce human antibodies by a process wherein at least one step of the process includes immunizing a transgenic nonhuman animal with the desired antigen.
- the modified animal fails to produce endogenous antibodies, but instead produces B-cells which secrete immunoglobulins with fully human variable regions.
- the antibodies produced include fully human antibodies and can be obtained from the animal directly, or from immortalized B-cells derived from the animal. .
- the genes encoding the immunoglobulins with human variable regions can be recovered and expressed to obtain the antibodies directly or modified to obtain analogs of antibodies such as, for example, single chain F v molecules.
- the invention is directed to a method to produce an immunoglobulin with a fully human variable region to a specific antigen or to produce an analog of said immunoglobulin by a process which comprises immunizing a nonhuman animal with the antigen under conditions that stimulate an immune response.
- Fully human immunoglobulins are included in this group and are preferred.
- the nonhuman animal is characterized by being substantially incapable of producing endogenous heavy or light immunoglobulin chain, but capable of producing immunoglobulins either with both human variable regions and constant regions or with fully human variable regions or both.
- the animal produces B cells which secrete immunoglobulins, with at least variable regions that are fully human, specific for the antigen.
- the human immunoglobulin of desired specificity can be directly recovered from the animal, for example, from the serum, or primary B cells can be obtained from the animal and immortalized.
- the immortalized B cells can be used directly as the source of human antibodies or, alternatively, the genes encoding the antibodies can be prepared from the immortalized B cells or from primary B cells of the blood or lymphoid tissue (spleen, tonsils, lymph nodes, bone marrow) of the immunized animal and expressed in recombinant hosts, with or without modification, to produce the immunoglobulin or its analogs.
- the genes encoding the repertoire of immunoglobulins produced by the immunized animal can be used to generate a library of immunoglobulins to permit screening for those variable regions which provide the desired affinity. Clones from the library which have the desired characteristics can then be used as a source of nucleotide sequences encoding the desired variable regions for further manipulation to generate antibodies or analogs with these characteristics using standard recombinant techniques.
- the invention relates to an immortalized nonhuman B cell line derived from the above described animal.
- the invention is directed to a recombinant host cell which is modified to contain the gene encoding either the human immunoglobulin with the desired specificity, or an analog thereof which exhibits the same specificity.
- the invention is directed to antibodies or antibody analogs prepared by the above described methods and to recombinant materials for their production.
- the invention is directed to antibodies with fully human variable regions, including fully human antibodies which are immunospecific with respect to particular antigens set forth herein and to analogs which are similarly immunospecific, as well as to the recombinant materials useful in the production of these antibodies.
- Figure 1 shows the serum titers of anti-IL-6 antibodies from a XenomouseTM 1 immunized with human IL-6 and which antibodies contain human K light chains and/or human ⁇ heavy chains.
- Figure 2 shows the serum titers of anti-IL-8 antibodies from a XenomouseTM immunized with human IL-8 and which antibodies contain human K light chains and/or human ⁇ heavy chains.
- Fi-gure 3 shows the serum titers of anti-TNF ⁇ antibodies from a XenomouseTM immunized with human TNF-o; and which antibodies contain human K light chains and/or human ⁇ heavy chains.
- Figure 4 shows the serum titers of anti-CD4 antibodies from a XenomouseTM immunized with human CD4 and which antibodies contain human K light chains and/or human ⁇ heavy chains.
- Figure 5 shows the serum titers of a XenomouseTM immunized with 300.19 cells expressing L-selectin at their surface. In the ELISA assay used, these antibodies are detectable only if they carry human ⁇ constant region heavy chains.
- Figure 6 shows the serum titers of a XenomouseTM immunized with 300.19 cells expressing L-selectin at their surface. In the ELISA assay used, these antibodies are detectable only if they carry human *c light chains.
- Figure 7 shows the serum titers of a XenomouseTM immunized with 300.19 cells expressing L-selectin. In this ELISA, these antibodies are detectable if they carry human K light chain and/or murine y constant regions.
- Figure 8 shows a FACS analysis of human neutrophils coupled to sera from a XenomouseTM (A195-2) immunized with human L-selectin and labeled with an antibody immunoreactive with murine heavy chain y constant region.
- Figure 9 shows a FACS analysis of human neutrophils incubated with serum from a XenomouseTM (A195-2) immunized with human L-selectin and labeled with an antibody immunoreactive with human light chain K region.
- Figure 10 is a diagram of a plasmid used to transfect mammalian cells to effect the production of the human protein gp39.
- Figure 11 represents the serum titration curve of mice immunized with CHO cells expressing human gp39.
- the antibodies detected in this ELISA must be immunoreactive with gp39 and contain human heavy chain ⁇ constant regions or human *c light chains.
- Figure 12 shows the results of a FACS analysis of antibodies from a XenomouseTM (labeled A247-4) immunized with human gp39 reacted with activated human T cells.
- Figure 12A shows the separation of human activated T cells into CD4 + and CD4" populations.
- Panel B shows the results of a FACS analysis of the activated CD4 + T cells with antibodies from the XenomouseTM immunized with gp39 which contain murine heavy chain y constant regions;
- panel C shows the corresponding results with respect to CD4 " populations.
- Figure 13 is a titration curve with respect to monoclonal antibodies secreted by the hybridoma clone D5.1.
- This clone is obtained from a XenomouseTM immunized with tetanus toxin C (TTC) and contains human K light chain and human ⁇ constant region in the heavy chain.
- TTC tetanus toxin C
- Figure 14 is a titration curve with respect to the hybridoma supernatant from clone K4.1.
- This hybridoma clone is obtained from a XenomouseTM immunized with TTC and contains human K light chain and heavy chain having the murine y constant region.
- Figure 15 shows binding curves for various concentrations of the K4.1 monoclonal antibody in a determination of the affinity of the monoclonal with its antigen in a BIAcore instrument.
- Figure 16 shows the complete nucleotide sequence of the heavy chain from the antibody secreted by K4.1.
- Figure 17 shows the complete nucleotide sequence of the light chain from the antibody secreted by K4.1.
- Figure 18 shows the complete nucleotide sequence of the heavy chain from the antibody secreted by D5.1.
- Figure 19 shows the complete nucleotide sequence of the light chain from the antibody secreted by D5.1.
- the methods of the invention include administering an antigen for which human forms of immunospecific reagents are desired to a transgenic nonhuman animal which has been modified genetically so as to be capable of producing human, but not endogenous, antibodies.
- the animal has been modified to disable the endogenous heavy and/or light chain loci in its genome, so that these endogenous loci are incapable of the rearrangement required to generate genes encoding immunoglobulins in response to an antigen.
- the animal will have been provided, stably, in its genome, at least one human heavy chain locus and at least one human light chain locus so that in response to an administered antigen, the human loci can rearrange to provide genes encoding human variable regions immunospecific for the antigen.
- the first step is administration of the antigen.
- Techniques for such administration are conventional and involve suitable immunization protocols and formulations which will depend on the nature of the antigen per se. It may be necessary to provide the antigen with a carrier to enhance its immunogenicity and/or to include formulations which contain adjuvants and/or to administer multiple injections, and the like. Such techniques are standard and optimization of them will depend on the characteristics of the particular antigen for which immunospecific reagents are desired.
- immunospecific reagents includes immunoglobulins and their analogs.
- analogs has a specific meaning in this context. It refers to moieties that contain the fully human portions of the immunoglobulin which account for its immunospecificity.
- variable regions including the complementarity determining regions (CDRs) are required, along with sufficient portions of the framework regions (FRs) to result in the appropriate three dimensional conformation.
- Typical immunospecific analogs of antibodies include F ( a b ' ) _t» F a b ' » and F a b regions. Modified forms of the variable regions to obtain, for example, single chain F v analogs with the appropriate immunospecificity are known.
- variable regions derived from antibodies with varying specificities can also be coupled to a variety of additional substances which can provide toxicity, biological functionality, alternative binding specificities and the like.
- the moieties including the fully human variable regions produced by the methods of the invention include single-chain fusion proteins, molecules coupled by covalent methods other than those involving peptide linkages, and aggregated molecules. Examples of analogs which include variable regions coupled to additional molecules covalently or noncovalently include those in the following nonlimiting illustrative list. Traunecker, A. et al . Int J
- Cancer Supp (1992) Supp 7:51-52 describe the bispecific reagent janusin in which the F v region directed to CD3 is coupled to soluble CD4 or to other ligands such as OVCA and IL-7.
- the fully human variable regions produced by the method of the invention can be constructed into F v molecules and coupled to alternative ligands such as those illustrated in the cited article.
- Higgins, P.J. et al . J Infect Disease (1992) 166:198-202 describe a heteroconjugate antibody composed of 0KT3 cross-linked to an antibody directed to a specific sequence in the V3 region or GP120.
- heteroconjugate antibodies can also be constructed using at least the human variable regions contained in the immunoglobulins produced by the invention methods. Additional examples of bispecific antibodies include those described by Fanger, M.W. et al . Cancer Treat Res (1993) £&:181-194 and by Fanger, M.W. et al . Crit Rev Immunol (1992) 12.:101-124.
- Conjugates that are immunotoxins including conventional antibodies have been widely described in the art.
- the toxins may be coupled to the antibodies by conventional coupling techniques or immunotoxins containing protein toxin portions can be produced as fusion proteins.
- the analogs of the present invention can be used in a corresponding way to obtain such immunotoxins. Illustrative of such immunotoxins are those described by Byrs, B.S. et al . Seminars Cell Biol (1991) 2:59-70 and by Fanger, M.W. et al. Immunol Today (1991) 12:51-54.
- immunoglobulins and analogs of the invention will have agonist activity with respect to antigens for which they are immunospecific in the cases wherein the antigens perform signal transducing functions.
- a subset of antibodies or analogs prepared according to the methods of the invention which are immunospecific for, for example, a cell surface receptor will be capable of eliciting a response from cells bearing this receptor corresponding to that elicited by the native ligand.
- antibodies or analogs which are immunospecific for substances mimicking transition states of chemical reactions will have catalytic activity.
- a subset of the antibodies and analogs of the invention will function as catalytic antibodies.
- the genes encoding the immunoglobulins produced by the transgenic animals of the invention can be retrieved and the nucleotide sequences encoding the fully human variable region can be manipulated according to known techniques to provide a variety of analogs such as those described above.
- the immunoglobulins themselves containing the human variable regions can be modified using standard coupling techniques to provide conjugates retaining immunospecificity and fully human characteristics in the immunospecific region.
- immunoglobulin "analogs" refers to moieties which contain those portions of the antibodies of the invention which retain their human characteristics and their immunospecificity. These will retain sufficient human variable region to provide the desired specificity.
- all of the methods of the invention include administering the appropriate antigen to the transgenic animal. The recovery or production of the antibodies themselves can be achieved in various ways.
- the polyclonal antibodies produced by the animal and secreted into the bloodstream can be recovered using known techniques. Purified forms of these antibodies can, of course, be readily prepared by standard purification techni-ques, preferably including affinity chromatography with respect to the particular antigen, or even with respect to the particular epitope of the antigen for which specificity is desired. In any case, in order to monitor the success of immunization, the antibody levels with respect to the antigen in serum will be monitored using standard techniques such as ELISA, RIA and the like.
- a portion of the polyclonal antiserum obtained may include an endogenous heavy chain constant region derived from the host, even though the variable regions are fully human.
- use of the polyclonal antiserum directly would be inappropriate.
- the presence of these chimeras which is believed to result from in vivo isotype switching as described by Gerstein et al . Cell (1990) £1:537, is not problematic, in view of conventional purification and modification methods and in view of the availability of alternative methods to recover fully human antibodies, if desired, described in the following paragraphs.
- the polyclonal antiserum could be subjected to suitable separation techniques to provide compositions containing only fully human immunoglobulins. Portions of the serum which display characteristics of the host species can be removed, for example, using affinity reagents with the appropriate anti species immunoglobulins or immunospecific portions thereof. Furthermore, for applications where only the variable regions of the antibodies are required, treating the polyclonal antiserum with suitable reagents so as to generate F ⁇ , F ⁇ , , or F (ab , ) portions results in compositions containing fully human characteristics. Such fragments are sufficient for use, for example, in immunodiagnostic procedures involving coupling the immunospecific portions of immunoglobulins to detecting reagents such as radioisotopes.
- the polyclonal antiserum can be treated to provide compositions with the desired characteristics including compositions consisting essentially of fully human antibodies and compositions including immunoglobulin analogs wherein the immunospecific portion is fully human.
- immunoglobulins and analogs with desired characteristics can be generated from immortalized B cells derived from the transgenic animals used in the method of the invention or from the rearranged genes provided by these animals in response to immunization.
- hybridomas derived from the B cells of the immunized animal can be screened so as to choose only those secreting fully human antibodies and that the genetic material can be recovered from the hybridomas or from lymphocytes in spleen, blood, or lymph nodes of the immunized animal and manipulated using conventional techniques to replace any endogenous constant region with a human one or to produce a desired analog.
- the B cells can be obtained, typically from the spleen, but also, if desired, from the peripheral blood lymphocytes or lymph nodes and immortalized using any of a variety of techniques, most commonly using the fusion methods described by Kohler and Milstein.
- the resulting hybridomas (or otherwise immortalized B cells) can then be cultured as single colonies and screened for secretion of antibodies of the desired specificity.
- the screen can also include a determination of the fully human character of the antibody. For example, as described in the examples below, a sandwich ELISA wherein the monoclonal in the hybridoma supernatant is bound both to antigen and to an antihu an constant region can be employed.
- hybridomas that secrete antibodies which are immunoreactive with antispecies antibodies directed to the species of the immunized animal can be discarded.
- the desired antibodies can be recovered, again using conventional techniques. They can be prepared in quantity by culturing the immortalized B cells using conventional methods, either in vitro, or in vivo to produce ascites fluid. Purification of the resulting monoclonal antibody preparations is less burdensome than in the case of serum since each immortalized colony will secrete only a single type of antibody. In any event, standard purification techniques to isolate the antibody from other proteins in the culture medium can be employed.
- the immortalized cells can be used as a source of rearranged heavy chain and light chain loci for subsequent expression and/or genetic manipulation. Isolation of genes from such antibody-producing cells is straightforward since high levels of the appropriate mRNAs are available for production of a cDNA library.
- the recovered rearranged loci can be manipulated as desired. For example, the constant region can be exchanged for that of a different isotype or that of a human antibody, as described above, or eliminated altogether.
- the variable regions can be linked to encode single chain F v regions. Multiple F v regions can be linked to confer binding ability to more than one target or chimeric heavy and light chain combinations can be employed.
- the coding sequences including those that encode, at a minimum, the variable regions of the human heavy and light chain can be inserted into expression systems contained on vectors which can be transfected into standard recombinant host cells.
- host cells As described below, a variety of such host cells may be used; for efficient processing, however, mammalian cells are preferred. Typical mammalian cell lines useful for this purpose include CHO cells, 293 cells, or NSO-GS cells.
- the production of the antibody or analog is then undertaken by culturing the modified recombinant host under culture conditions appropriate for the growth of the host cells and the expression of the coding sequences.
- the antibodies are then recovered from the culture.
- the expression systems are preferably designed to include signal peptides so that the resulting antibodies are secreted into the medium; however, intracellular production is also possible.
- the phage library is thus screened for the antibodies with highest affinity for the antigen and the genetic material recovered from the appropriate clone. Further rounds of screening can increase the affinity of the original antibody isolated.
- the manipulations described above for recombinant production of the antibody or modification to form a desired analog can then be employed.
- the modified or unmodified rearranged loci are manipulated using standard recombinant techniques by constructing expression systems operable in a desired host cell, such as, typically, a Chinese hamster ovary cell, and the desired immunoglobulin or analog is produced using standard recombinant expression techniques, and recovered and purified using conventional methods.
- compositions of the invention will have utilities similar to those ascribable to nonhuman antibodies directed against the same antigen. Such utilities include, for example, use as a affinity ligands for purification, as reagents in immunoassays, as components of immunoconjugates, and as therapeutic agents for appropriate indications.
- antibodies or their analogs with fully human characteristics.
- These reagents avoid the undesired immune responses engendered by antibodies or analogs which have characteristics marking them as originating from non-human species.
- Other attempts to "humanize” antibodies do not result in reagents with fully human characteristics.
- chimeric antibodies with murine variable regions and human constant regions are easily prepared, but, of course, retain murine characteristics in the variable regions.
- Even the much more difficult procedure of "humanizing" the variable regions by manipulating the genes encoding the amino acid sequences that form the framework regions does not provide the desired result since the CDRs, typically of nonhuman origin, cannot be manipulated without destroying immunospecificity.
- the methods of the present invention provide, for the first time, immunoglobulins that are fully human or analogs which contain immunospecific regions with fully human characteristics.
- leukocyte markers such as CD2, CD3, CD4, CD5, CD6, CD7, CD8, CDlla,b,C, CD13, CD14, CD18, CD19, CD20, CD22, CD23, CD27 and its ligand, CD28 and its ligands B7.1, B7.2, B7.3, CD29 and its ligand, CD30 and its ligand, CD40 and its ligand gp39, CD44, CD45 and isoforms
- CDw52 (Campath antigen)
- CD56, CD58, CD69, CD72, CTLA-4, LFA-1 and TCR histocompatibility antigens such as MHC class I or
- adhesion molecules including the integrins, such as VLA-1, VLA-2, VLA-3, VLA-4, VLA-5, VLA-6, LFA-1, Mac-1 and pl50,95; and the selectins, such as L-selectin, E-selectin, and
- interleukins such as IL-1, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-12, IL-13, IL-14, and IL-15
- interleukin receptors such as IL-1R, IL-2R, IL-3R, IL-4R, IL-5R, IL-6R, IL-7R, IL-8R, IL-9R, IL-10R, IL-11R, IL-12R, IL-13R, IL-14R, and IL-15R
- chemokines such as PF4, RANTES, MlPl ⁇ , MCP1, NAP-2, Gro ⁇ , Gro/3, and IL-8
- growth factors such as TNFalpha, TGFbeta, TSH, VEGF/VPF, PTHrP, EGF family
- Igs and their receptors such as IgE, FceRI, and FCeRII
- tumor antigens such as her2-neu, mucin, CEA and endosialin
- allergens such as house dust mite antigen, lol pi (grass) antigens, and urushiol
- viral proteins such as CMV glycoproteins B, H, and gCIII, HIV-l envelope glycoproteins, RSV envelope glycoproteins, HSV envelope glycoproteins, EBV envelope glycoproteins, VZV envelope glycoproteins, HPV envelope glycoproteins, Hepatitis family surface antigens
- toxins such as pseudomonas endotoxin and osteopontin/uropontin, snake venom, and bee venom
- blood factors such as complement C3b, complement C5a, complement C5b-9, Rh factor, fibrinogen, fibrin, and myelin associated growth inhibitor
- enzymes such as cholesterol ester transfer protein, membrane bound matrix metalloproteases, and glutamic acid
- immunoglobulins and analogs are those immunospecific with respect to human IL-6, human IL-8, human TNFcu, human CD4, human L-selectin, and human gp39.
- Human antibodies against IL-8 are particularly useful in preventing tumor metastasis and inflammatory states such as asthma and reperfusion injury.
- Antibodies and analogs immunoreactive with human TNF ⁇ and human IL-6 are useful in treating cachexia and septic shock as well as autoimmune disease.
- Antibodies and analogs immunoreactive with gp39 or with L-selectin are also effective in treating or preventing autoimmune disease.
- anti-gp39 is helpful in treating graft versus host disease, in preventing organ transplant rejection, and in treating glomerulonephritis.
- Antibodies and analogs against L-selectin are useful in treating ischemia associated with reperfusion injury.
- Typical autoimmune diseases which can be treated using the above-mentioned antibodies and analogs include systemic lupus erythematosus, rheumatoid arthritis, psoriasis, Sjogren's, scleroderma, mixed connective tissue disease, dermatomyositis, polymyositis, Reiter's syndrome, Behcet's disease, Type 1 diabetes, Hashimoto's thyroiditis, Grave's disease, multiple sclerosis, myasthenia gravis and pemphigus.
- mice designated “xenomice”
- xenomice mice
- Immunization protocols appropriate to each antigen are described in the specific examples below.
- the sera of the immunized xenomice (or the supernatants from immortalized B cells) were titrated for antigen specific human antibodies in each case using a standard ELISA format. In this format, the antigen used for immunization was immobilized onto wells of microtiter plates.
- the plates were washed and blocked and the sera (or supernatants) were added as serial dilutions for 1-2 hours of incubation. After washing, bound antibody having human characteristics was detected by adding the appropriate antispecies Ig (typically antihuman K chain antibody or antihuman ⁇ chain antibody) conjugated to horseradish peroxidase (HRP) for one hour. In some cases, the bound antibodies were tested for murine characteristics using antimurine antibodies, typically antimurine y chain antibody. After again washing, the chromogenic reagent o-phenylene diamine (OPD) substrate and hydrogen peroxide were added and the plates were read 30 minutes later at 492 nm using a microplate reader.
- Ig typically antihuman K chain antibody or antihuman ⁇ chain antibody conjugated to horseradish peroxidase
- HRP horseradish peroxidase
- the bound antibodies were tested for murine characteristics using antimurine antibodies, typically antimurine y chain antibody.
- OPD chromogenic reagent o-phenylene
- the antigen was coated using plate coating buffer (0.1 M carbonate buffer, pH 9.6); the assay blocking buffer used was 0.5% BSA, 0.1% Tween 20 and 0.01% Thimerosal in PBS; the substrate buffer used in color development was citric acid 7.14 g/1: dibasic sodium phosphate 17.96 g/1; the developing solution (made immediately before use) was 10 ml substrate buffer, 10 mg OPD, plus 5 ml hydrogen peroxide; the stop solution (used to stop color development) was 2 M sulfuric acid. The wash solution was 0.05% Tween 20 in PBS.
- EXflW le l Human Antibodies Against Human IL-6 Three to 5 xenomice aged 8-20 weeks were age-matched and immunized intraperitoneally with 50 ⁇ g human IL-6 emulsified in complete Freund's adjuvant for primary immunization and in incomplete Freund's adjuvant for subse-quent injections. The mice received 6 injections 2-3 weeks apart. Serum titers were determined after the second dose and following each dose thereafter. Bleeds were performed 6-7 days after injections from the retrobulbar plexus. The blood was allowed to clot at room temperature for about 2 hours and then incubated at 4°C for at least 2 hours before separating and collecting the sera.
- ELISAs were conducted as described above by applying 100 ⁇ l/well of recombinant human IL-6 at 2 mg/ml in coating buffer. Plates were then incubated at 4°C overnight or at 37°C for 2 hours and then washed three times in washing buffer. Addition of 100 ⁇ l/well blocking buffer was followed by incubation at room temperature for 2 hours, and an additional 3 washes.
- Immunization and serum preparation were as described in Example 1 as except that human recombinant IL-8 was used as an immunogen.
- ELISA assays were performed with respect to the recovered serum, also exactly as described in Example 1, except that the ELISA plates were initially coated using 100 ⁇ l/well of recombinant human IL-8 at 0.5 mg/ml in the coating buffer.
- the results obtained for various serum dilutions from XenomouseTM A260-5 after 6 injections are shown in Figure 2.
- Human anti- IL-8 binding was again shown at serum dilutions having concentrations higher than that represented by a 1:1,000 dilution.
- Example 3 Human Antibodies Against Human TNF ⁇ Immunization and serum preparation were conducted as described in Example 1 except that human recombinant TNF ⁇ was substituted for human IL-6. ELISAs were conducted as described in Example 1 except that the initial coating of the ELISA plate employed 100 ⁇ l/well recombinant human TNF ⁇ at 1 mg/ml in coating buffer.
- Human CD4 antigen was prepared as a surface protein using human CD4 f on transfected recombinant cells as follows.
- Human CD4 ⁇ * consists of the extracellular domain of CD4, the transmembrane domain of CD4, and the cytoplasmic domain of residues 31-142 of the mature £ chain.
- RBL- 2H3 cells at 10 6 cells per well were cultured in 750 ml DMEM low + 20% FBS (Gibco) and 16 ⁇ g/ml polybrene with an equal volume of proviral supernatant for 2 hours at 37°C, 5% C0 2 .
- 750 ml of medium was removed and 750 ⁇ l of infection medium and retroviral supernatant were added to each well and the cultures incubated overnight.
- the cells were washed and expanded in DMEM low + 10% FBS until sufficient cells were available for sorting.
- the CD4 " zeta transduced RBL-2H3 cells were sorted using the FACSTAR plus (Becton Dickinson) .
- the cells were stained for human CD4 with a mouse antihuman CD4 " PE antibody and the top 2-3% expressing cells were selected.
- Immunizations were conducted as described in Example 1 using 10 x 10 6 cells per mouse except that the primary injection was subcutaneous at the base of the neck. The mice received 6 injections 2-3 weeks apart. Serum was prepared and analyzed by ELISA as described in Example 1 except that the initial coating of the ELISA plate utilized 100 ⁇ l per well of recombinant soluble CD4 at 2 mg/ml of coating buffer. The titration curve for serum from XenomouseTM A207-1 after 6 injections is shown in Figure 4. Titers of human anti-CD4 reactivity were shown at concentrations representing greater than those at 1:1,000 dilution.
- the antigen was prepared as a surface displayed protein in C51 cells, a high expressing clone derived by transfecting the mouse pre-B cell 300.19 with LAM-1 cDNA (LAM-1 is the gene encoding L-selectin) (Tedder, et al . , J Immunol (1990) ______..- 532 ) or with similarly transfected CHO cells.
- LAM-1 is the gene encoding L-selectin
- the transfected cells were sorted using fluorescent activated cell sorting using anti-Leu-8 antibody as label.
- the C51 and the transfected CHO cells were grown in DME 4.5 g/1 glucose with 10% FCS and 1 mg/ml G418 in 100 mm dishes.
- Negative control cells, 3T3-P317 (transfected with gag/pol/env genes of Moloney virus) were grown in the same medium without G418.
- Sera were collected as described in Example l and analyzed by ELISA in a protocol similar to that set forth in Example 1.
- the transfected cells were plated into 96 well plates and cell monolayers grown for 1-2 days depending on cell number and used for ELISA when confluent.
- the cells were fixed by first washing with cold 1 x PBS and then fixing solution (5% glacial acetic acid, 95% ethanol) was added.
- the plates were incubated at -25°C for 5 minutes and can be stored at this temperature if sealed with plate sealers.
- the ELISA is begun by bringing the plates to room temperature, flicking to remove fixing solution and washing 5 times with DMEM medium containing 10% FCS at 200 ⁇ l per well.
- the wells were treated with various serum dilutions or with positive or negative controls.
- Positive control wells contained murine IgGl monoclonal antibody to human L-selectin.
- the wells were incubated for 45 minutes and monolayer integrity was checked under a microscope.
- the wells were then incubated with either antimouse IgG (1/1000) or with antihuman K chain antibody or antihuman ⁇ chain antibody conjugates with HRP described in Example 1.
- the plates were then washed with 1% BSA/PBS and again with PBS and monolayer integrity was checked. The plates were developed, stopped, and read as described above.
- the results for serum from XenomouseTM A303-3 are shown in Figs.
- ELISAs were also performed using as the immobilized antigen a fusion protein consisting of the extracellular domain of human L-selectin fused to the constant domain of human IgG x (Guo, et al . , Cell Immunol (1994) 154:202) .
- the L-selectin fusion protein was made by transient transfection of human 293 cells using calcium phosphate transfection (Wigler, M. , Cell (1979) 16_:777) .
- Serum preparation was performed as described in Example 1.
- ELISAs were conducted essentially as in Example 1, except that the initial coating of the ELISA plate employed 100 ⁇ l transfected 293 cell culture supernatant containing the L-selectin-Ig fusion protein. Detection employed HRP-mouse antihuman K and HRP-goat antimouse IgG.
- Figure 7 shows the results from XenomouseTM A195-2; antibodies specific for L-selectin having human * light chains and/or human variable regions with murine heavy chain y regions are present in the serum.
- the antisera obtained from the immunized xenomice were also tested for staining of human neutrophils which express L-selectin.
- Human neutrophils were prepared as follows: peripheral blood was collected from normal volunteers with 100 units/ml heparin. About 3.5 ml blood was layered over an equal volume of One-step Polymorph Gradient (Accurate Chemical, Westbury, NY) and spun for 30 minutes at 450 x g at 20°C. The neutrophil fraction was removed and washed twice in DPBS/2% FBS. The neutrophils were then stained with either:
- mouse monoclonal antibody LAM1-3 as a positive control, mouse monoclonal antibody LAM1-3 (against L-selectin) ; and (3) as negative control, antiserum from a XenomouseTM immunized with cells expressing human gp39.
- Example 6 Human Antibodies Against Human gp39 gp39 (the ligand for CD40) is expressed on activated human CD4 + T cells.
- the sera of xenomice immunized with recombinant gp39 according to this example contained antibodies immunospecific for gp39 with fully human variable regions; the sera contained fully human IgM antibodies and chimeric IgG antibodies containing human variable regions and murine constant heavy chain y region.
- the antigen consisted of stable transfectants of
- CHO cells were split 1:10 prior to transfection in DMEM 4.5 g/1 glucose, 10% FBS, 2 mM glutamine, MEM, NEAA supplemented with additional glycine, hypoxanthine and thymidine.
- the cells were cotransfected with the gp39 vector at 9 ⁇ g/10 cm plate (6 X 10 5 cells) and the DHFR expressing vector pSV2DHFRs (Subranani et al . Mol Cell Biol (1981) 2:854) at 1 ⁇ g/10 cm plate using calcium phosphate transfection. 24 hours later the cells were split 1:10 into the original medium containing G418 at 0.6 mg/ml.
- Cells producing gp39 were sorted by FACS using an anti-gp39 antibody.
- mice grouped as described in Example 1 were immunized with 300.19 cells expressing gp39 using a primary immunization subcutaneously at the base of the neck and with secondary intraperitoneal injections every 2-3 weeks.
- Sera were harvested as described in Example 1 for the ELISA assay.
- the ELISA procedure was conducted substantially as set forth in Example 1; the microtiter plates were coated with CHO cells expressing gp39 grown in a 100 mm dish in DMEM, 4.5 g/1 glucose, 10% FCS, 4 mM glutamine, and nonessential amino acid (NEAA) solution for MEM (100X) .
- the cells were trypsinized and plated into 96-well filtration plates at 10 5 cells/200 ⁇ l well and incubated at 37°C overnight.
- the positive controls were mouse antihuman gp39; negative controls were antisera from mice immunized with an antigen other than gp39. 50 ⁇ l of sample were used for each assay. The remainder of the assay is as described in Example 1.
- the dilution curves for the sera obtained after 4 injections from mice immunized with gp39 expressed on CHO cells are shown in Figure 11. As shown, the sera contained antihuman gp39 immunospecificity which is detectable with human K and human ⁇ chain antibodies coupled to HRP.
- PBMC peripheral blood was collected from normal volunteers with the addition of 100 unit/ml heparin.
- PBMC peripheral blood was collected from normal volunteers with the addition of 100 unit/ml heparin.
- PBMC peripheral blood was collected from normal volunteers with the addition of 100 unit/ml heparin.
- PBMC peripheral blood was collected from normal volunteers with the addition of 100 unit/ml heparin.
- PBMC peripheral blood was collected from normal volunteers with the addition of 100 unit/ml heparin.
- PBMC were isolated over Ficoll gradient and activated with 3 ⁇ g/ml PHA, 1 ⁇ g/ml PMA in IMDM plus 10% FBS plus 25 ⁇ M 2-mercaptoethanol for 4 hours.
- the PBMC were stained with mouse Mab against human CD4 labeled with FITC to permit separation of CD4 + and CD4" human T cells.
- the activated CD4 + and CD4 " T cells were then analyzed by FACS using staining with either:
- the detecting antibody in the FACS analysis was goat antimouse IgG (PE) .
- the results are shown in Figure 12.
- CD4 + (R2) and CD4" (R3) cells were separated prior to FACS analysis.
- Panel B shows the results for CD4 + cells and shows that sera from mice immunized with gp39 (labeled A247-4 in the figure) reacted with these activated CD4 + T cells;
- panel C shows that these sera did not react with CD4" cells.
- These antibodies carried murine heavy chain y constant regions.
- the results of panels B and C also confirm that the TNF-injected XenomouseTM did not make antibodies against gp39.
- Example 7 Preparation of High-Affinity Human Mabs Agajngt Tetmug Tpyjn
- the antibodies prepared in this example were secreted by hybridomas obtained by immortalizing B cells from xenomice immunized with tetanus toxin.
- the immunization protocol was similar to that set forth in Example 1 using 50 ⁇ g tetanus toxin emulsified in complete Freund's adjuvant for intraperitoneal primary immunization followed by subsequent intraperitoneal injections with antigen incorporated into incomplete Freund's adjuvant.
- the mice received a total of 4 injections 2-3 weeks apart.
- anti-TTC antitetanus toxinC
- the spleen cells were fused with myeloma cells P3X63- Ag8.653 as described by Galfre, G. and Milstein, C. Methods in Enzymology (1981) 21:3-46.
- the cells were resuspended in DMEM, 15% FCS, containing HAT supplemented with glutamine, pen/strep for culture at 37°C and 10% C0 2 .
- the cells were plated in microtiter trays and maintained in HAT-supplemented medium for two weeks before transfer to HAT-supplemented medium.
- the ELISA was conducted as described in Example 1 wherein the antigen coating consisted of 100 ⁇ l/well of tetanus toxin C (TTC) protein at 2 mg/ml in coating buffer, followed by incubation at 4°C overnight or at 37°C for two hours.
- TTC tetanus toxin C
- HRP-conjugated goat antimouse IgG at 1/2000 was used in addition to HRP mouse antihuman IgM as described in Example 1.
- Two hybridomas that secreted anti-TTC according to the ELISA assay, clone D5.1 and clone K4.1 were used for further analysis.
- clone D5.1 secretes fully human anti-TTC which is detectable using HRP-conjugated antihuman ⁇ chain antibody and HRP-conjugated antihuman K chain antibody. This is confirmed in Figures 18 and 19.
- Figure 14 shows that clone K4.1 secretes anti-TTC which is immunoreactive with antimurine y and antihuman K HRP-conjugated antibodies.
- clone K4.1 provides anti-TTC fully with human variable region as confirmed in Figures 16 and 17 and a murine constant heavy chain ⁇ region.
- the antibodies secreted by D5.l and K4.1 did not immunoreact in ELISAs using TNF ⁇ , IL-6, or IL-8 as immobilized antigen under conditions where positive controls (sera from xenomice immunized with TNF ⁇ , IL-6 and IL-8 respectively) showed positive ELISA results.
- TTC TTC antigen
- the surface was activated with 35 ⁇ l of equal volumes 0.1 M NHS and 0.1 M EDC injected across the surface followed by 30 ⁇ l of TTC fragment at 100 ⁇ g/ml in 10 mM sodium acetate buffer pH 5.0. The surface was blocked by injecting 35 ⁇ l 1 M ethanolamine and washed to remove noncovalently bound TCC using 5 ⁇ l 0.1 M HC1. The entire immobilization procedure was conducted with a continuous flow of buffer at 5 ⁇ l/min. This results in about 7500-8500 response units (RU) of TTC per chip. (1000 RU corresponds to about 1 ng of protein per mm 2 .) For chips with low antigen density, the procedure utilizes 15 ⁇ l rather than 30 ⁇ l of TTC, resulting in chips containing 550-950 RU.
- Chips could be regenerated after use in single determinations by injecting 10 ⁇ l formal or MgCl 2 .
- the chips are used to determine binding affinities by determining k a and k b (the association and dissociation rate constants) for the antibody with respect to the immobilized TTC.
- the association rate constant is measured over six minutes at a flow rate of 5 ⁇ l/min. at different concentrations of K4.1 Mab in the range of 2.16 nm-69.33 n .
- the dissociation rate constant is measured at a constant buffer flow rate of 5 ⁇ l/min after completion of the antibody injection.
- the raw data are graphed in Figure 15 and the calculated results are shown in Table 1.
- Immobilized K4.1 cone. rate rate constant constant tetanus toxinC range nM ka(10 5 M ⁇ s -1 ) kd(10 5 s _:l ) KAW ⁇ -ka/kd KD(M) kd/ka
- the K4.1 antibody has a binding constant (K a ) for TTC somewhat larger than 10 10 M *1 .
- the complete nucleotide sequence of the cDNAs encoding the heavy and light chains of the K4.1 and D5.1 monoclonals were determined as shown in Fi-gures 16-19.
- PolyA mRNA was isolated from about 10 6 hybridoma cells and used to generate cDNA using random hexamers as primers. Portions of the product were amplified by PCR using the appropriate primers.
- Both cell lines were known to provide human light chains; for PCR amplification of light chain encoding cDNA, the primers used were HKP1 (5' -CTCTGTGACACTCTCCTGGGAGTT-3' ) for priming from the constant region terminus and two oligos, used in equal amounts to prime from the variable segments: B3 (5' -CCACCATCAACTGCAAGTCCAGCCA-3' ) and B2/Bl (5' -GAAACGACACTCACGCAGTCTCCAGC-3' ) .
- the primers were MG-24Vi for the human variable regions: 5' -CAGGTGCAGCTGGAGCAGTCiGG-3' which, with inosine as shown recognizes the human variable regions V H1 _ 2 , V H1 _ 3 , V H4 and V H6 , and from the constant region MG-25 i.e.,
- MG-24VI was used to prime from the variable and ⁇ Pl (5' -TTTTCTTTGTTGCCGTTGGGGTGC-3' ) was used to prime from the constant region terminus.
- Figure 16 representing the heavy chain of the Mab secreted by K4.1
- the sequence shows the presence of the human variable segment VH6, the human diversity region DN1, and the human joining segment JH4 linked to the murine ⁇ l constant region.
- VH6 the human variable segment
- DN1 the human diversity region
- JH4 the human joining segment JH4 linked to the murine ⁇ l constant region.
- Figure 17 which shows the light chain of the K4.1 antibody
- analysis shows the presence of the human K variable region B3 and joining region JK4. Eight nucleotides are missing from B3 at the V ⁇ -J ⁇ junction and four mutations were found in the variable region.
- Five nongermline nucleotide additions were present at the V ⁇ -J ⁇ junction.
- FIG 18 which sets forth the sequence for the heavy chain of the antibody secreted by clone D5.1, this shows the heavy chain is comprised of the human variable fragment VH6, the human diversity region DNl and the human joining segment JH4 linked to the human ⁇ constant region.
- VH6 the human variable fragment
- DNl the human diversity region
- JH4 the human joining segment
- Germline chimeric mice containing integrated human DNA from the immunoglobulin loci were immunized by injection of 15- 20 ⁇ g of human IgE/ ⁇ in adjuvant. The mice were boosted with 15-20 ⁇ g of human IgE/ ⁇ every 14 days after the primary immunization. A bleed was done on the immunized animals to test the titer of serum antibodies against human IgE/ ⁇ . The mice with the highest titers were sacrificed and the spleen removed.
- Myeloma cells line P3X63-Ag8.653, used as the fusion partner for the spleen cells, were thawed 6 days prior to the fusion and grown in tissue culture.
- cells were split into fresh medium containing 10% fetal calf serum (FCS) at a ratio of 1:3.
- FCS fetal calf serum
- FCS fetal calf serum
- the splenocytes were further washed twice by centrifugation in serum-free medium. Myeloma cells were also washed in serum-free medium at this time. Each cell type was counted and combined at a ratio of 1:3 (myeloma to splenocyte) , mixed gently and centrifuged once together.
- a solution of 40% polyethylene glycol (PEG) was slowly added to the cell pellet while the cells were gently resuspended over a period of one minute. Cells were incubated at room temperature for one minute in the PEG solution and then slowly diluted into 5 ml serum-free medium over 5 minutes. Five ml more were added over the next 90 seconds. Cells were incubated at room temperature for 5 minutes. The cells were centrifuged at low speed and the supernatant removed. The cells were resuspended slowly and very gently in 5 ml of hybridoma medium containing 10% FCS, IX OPI, IX NE amino acids and 10 mM HEPES.
- PEG polyethylene glycol
- Cells were further diluted to 100 ml final volume in hybridoma medium with IX HAT solution (hypoxanthine, aminopterin and thymidine) .
- the fused cells were aliquoted 100 ⁇ l/well of 96- 2311 plates and cultured at 37°C and 10% C0 2 .
- Cells were fed at 10 days post-fusion with 100 ⁇ l/well of hybridoma medium with IX HT (hypoxanthine and thymidine) and allowed to grow close to confluence before screening.
- IX HAT solution hypoxanthine, aminopterin and thymidine
- Positive wells were further tested for human IgE/ ⁇ specificity.
- the cells were transferred from the 96-well plate to 0.5 ml of hybridoma medium with IX HT in a 48-well plate. At this stage the cells were subcloned by limiting dilution into 96-well plates so that a single antibody producing cell was in culture. As the culture became confluent, the cells were expanded to l ml, 3 ml, 5 ml, etc. and frozen aliquots were stored in liquid nitrogen to preserve the cell stocks.
- a chimeric nonhuman host particularly a murine host
- a transgenic host can be immunized with immunogens which could not be used with a human host.
- the resulting B cells may then be used for immortalization for the continuous production of the desired antibody.
- the immortalized cells may be used for isolation of the genes encoding the immunoglobulin or analog and be subjected to further molecular modification by methods such as in vitro mutagenesis or other techniques to modify the properties of the antibodies. These modified genes may then be returned to the immortalized cells by transfection to provide for a continuous mammalian cellular source of the desired antibodies.
- the subject invention provides for a convenient source of human antibodies, where the human antibodies are produced in analogous manner to the production of antibodies in a human host.
- the animal host cells conveniently provide for the activation and rearrangement of human DNA in the host cells for production of human antibodies.
- human antibodies can be produced to human immunogens, e.g., proteins, by immunization of the subject host mammal with human immunogens.
- the resulting antisera will be specific for the human immunogen and may be harvested from the serum of the host.
- the immunized host B cells may be used for immortalization, e.g., myeloma cell fusion, transfection, etc. to provide immortal cells, e.g., hybridomas, to produce monoclonal antibodies.
- the antibodies, antiserum and monoclonal antibodies will be glycosylated in accordance with the species of the cell producing the antibodies.
- Rare variable regions of the Ig locus may be recruited in producing the antibodies, so that antibodies having rare variable regions may be obtained.
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Also Published As
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WO1996034096A1 (en) | 1996-10-31 |
EP0823941A4 (de) | 2001-09-19 |
AU2466895A (en) | 1996-11-18 |
CA2219486A1 (en) | 1996-10-31 |
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