Native human monoclonal antibodies (N-huMAbs)

The Immunome platform exclusively captures Native Human Antibodies (N-huMABs). N-huMAbs are human antibodies that exist in exactly the conformations created by the natural protective activity of the human immune system. N-huMAbs may differ from antibodies made in artificial systems that are called “humanized” or even “fully human”. Most of these antibodies are derived in non-human systems, such as test tubes, bacteria, yeast, or transgenic mice. They have not undergone the optimization that naturally occurs within the intact human immune system, in which selective and evolutionary processes increase antigen binding affinity and refine binding specificity. In addition, many antibody cloning methods do not maintain the authentic heavy chain:light chain combinations that define the N-huMAb antigen binding sites. For many illnesses, the most potent therapeutics will be N-huMAbs, which are crafted by the human immune system during its healthy, protective functioning. N-huMAbs preserve the original heavy chain:light chain protein pairings, correctly preserving the structure of the native antibody antigen binding site, and they contain the original constant domain (Fc). N-huMAbs may be also be the safest therapeutics, because these processes also eliminate antibodies that have self-reactive, off-target binding.
Immunome has a proprietary hybridoma method, which can capture the full diversity and power of the N-huMAb repertoire. It involves two core technologies. The first is a novel immortal fusion partner cell line that expresses two genes: the human telomerase catalytic subunit and interleukin-6. These genes ensure stable, high-level antibody expression by the hybridomas. The second technology is a human B-cell selection/expansion method that requires only small blood samples from volunteer donors. It exclusively isolates antibodies that have undergone affinity-maturation in vivo. Immunome has licensed an issued patent and has exclusive rights to additional pending applications.
The Immunome method for cloning natural human monoclonal antibodies has several advantages. First, it produces full-length antibodies that can be functionally characterized without cumbersome recombinant DNA expression steps, obtaining purified monoclonal human antibodies within 12-16 weeks. Second, it is not biased against specific antibody structures, which allows the discovery of natural antibodies not accessible to other methods. This capability is essential as a foundation to select a single best antibody for clinical development. Finally, as the Immunome antibody repertoire comprises the entire human antibody immunome response, we are ideally positioned to develop a broad variety of human antibodies for treatment of un-met medical needs in infectious disease, cancer, bioterror attacks, and Alzheimer's disease.