HGH fragment 176-191 cancer-targeting antibody, and a truncated Fc1Rn fragment. The human Fc fragment was shown to be less efficient at protecting antibodies against degradation than the rabbit Fc fragment.
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We have also described studies demonstrating the efficacy of antibodies having reduced immunogenicity in human patients (see: Y. H. Lee, T. K. Hahm, et al., Humanized monoclonal antibody recognizing melanoma antigen and its role in radioimmunodetection of melanoma, J. Clin. Oncol. 7(5):891-896 (1989)).
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However, these prior efforts are limited to modifying the Fc region by altering the hinge cysteines of an IgG molecule (human antibody) and do not provide a means to significantly reduce or eliminate the problem of serum half-life of an antibody. Moreover, the Fc region of the antibodies described herein was not altered. Additional studies have been directed at reducing the size of antibodies in order to increase their metabolic stability. For example, the use of “diabodies” (D’Andrea et al. (1992), J. Biol. Chem. 267:25446-25450; Hollinger et al. (1993), Proc. Natl. Acad. Sci. USA 90:6444-6448) and “minibodies” (Leung et al., (1994) Biochemistry 33:6320-6328) has been described. Diabodies are antibody fragments containing the VH domain connected to the VL domain via a short peptide linker (see D’Andrea et al., (1992), J. Biol. Chem. 267:25446-25450). In the case of minibodies, only the VH and VL domains are connected.
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The diabody and minibody fragments comprise the VH domain of the parent antibody and a portion of the CH domain, while the VL domain remains unchanged. Other studies have described antibody fragments comprising the variable domains of the heavy and light chains of an antibody (see, e.g., U.S. Pat. No. 5,133,621, and Pratt et al. (1986) J. Immunol. 136:1011-1017). These “diabodies”, owing to their small size, are readily metabolized in vivo. They have been used, for example, as imaging agents, as therapeutics, and to produce antibodies having novel specificities. However, diabodies contain the hinge region of the parent antibody, and thus, have less amino acid residues available for conjugation to toxins or for attachment to other molecules. The generation of large, stable DNA encoding various fragments of antibodies has been described. For example, EP 0 257 003 and U.S. Pat. No. 4,946,778 describe generation of large antibody-encoding DNA molecules (see FIGS. 1 and 3, respectively) obtained by assembly of smaller DNA segments of antibodies or derivatives of antibodies.
However, because such fragments are generated from the entire parent antibody, they are often immunogenic. Moreover, the fragments are generally heterologous to the antibodies from which they were derived. It is often desirable to combine the features of antibody fragments with the advantages of DNA-based expression of recombinant antibodies. The latter can include, for example, reduced batch-to-batch variation and greater stability of the protein during long-term storage as compared to traditional antibody preparations.
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As a result of their smaller size, DNA-encoded antibodies are readily transported across the mucosal barrier, and large amounts of material can be produced in situ using nucleic acid methods (Kozaki et al. (1998) Nat. Biotechnol. 16:245-252; Yang et al. (1994) Proc. Natl. Acad. Sci. USA 91:9564-9568). Thus, DNA-encoded antibodies provide for reduced cost and increased convenience over traditional antibodies for industrial, clinical, and diagnostic uses. Nevertheless, there remains a need for further improvements in the design of antibody molecules. This need is especially acute in the field of vaccine development. For example, the current vaccine against influenza, inactivated influenza virus, has been plagued with suboptimal protection. For example, the induction of a rapid and robust T cell response is critical for achieving a protective immune response.
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Unfortunately, this response to influenza vaccines has been rather inconsistent and has been limited to the induction of neutralizing antibodies. A vaccine against influenza virus could be improved by increasing the magnitude and quality of the cell mediated immune response. This could be achieved by enhancing antigen delivery to antigen presenting cells. The current methods for delivering antigens to APCs in vivo typically utilize live viruses or carriers that are immunogenic to the subject. However, such methods have several disadvantages.
For example, inactivation of viruses is often necessary in order to render a virus non-pathogenic. This can adversely affect antigenicity and immunogenicity of the virus. Similarly, such viral carriers may be unsuitable for clinical use. Moreover, the virus or the viral carrier may also induce an immune response that neutralizes or otherwise decreases immunization. Thus, there remains a need for the development of improved antigen delivery systems that can effectively induce protective immune responses against diseases, including, for example, diseases caused by infection by microbial pathogens. This invention satisfies this need and provides related advantages as well.
