Researchers Map Viral Protein in Human DNA for Cancer Treatment

Scientists at the La Jolla Institute for Immunology have achieved a major breakthrough by mapping the three-dimensional structure of the envelope glycoprotein (Env) from the human endogenous retrovirus K (HERV-K), a viral protein embedded within human DNA. This accomplishment marks the first time a human HERV protein structure has been solved, making it only the third retroviral envelope structure ever mapped after HIV and SIV.

Unlocking the "Dark Matter" of Human DNA

Approximately 8% of the human genome consists of viral sequences—remnants of ancient infections that have persisted through evolution. Most of these sequences remain silent, considered the "dark matter" of our genome. However, in certain disease states, such as cancer and autoimmune disorders, these viral genes can reactivate, leading to the production of viral proteins like HERV-K Env on the surface of affected cells. Until now, the structure of these proteins has eluded scientists due to their instability and tendency to rapidly change shape.

Implications for Cancer and Autoimmune Disease

The successful mapping of the HERV-K Env protein’s structure opens new avenues for developing diagnostics and targeted therapies. The presence of HERV-K Env on cancer cells and in autoimmune diseases suggests it could serve as a biomarker for disease detection and as a therapeutic target. Researchers believe that understanding this protein’s structure will allow for the design of antibodies and drugs that specifically recognize and neutralize cells expressing HERV-K Env, potentially leading to more precise cancer immunotherapies and improved diagnostics for autoimmune conditions.

According to Erica Ollmann Saphire, Ph.D., President and CEO of LJI, "Understanding the HERV-K Env structure, and the antibodies we now have, opens up diagnostic and treatment opportunities" (statement). The discovery is particularly significant because envelope proteins are highly dynamic and difficult to capture in their pre-fusion state, which is essential for understanding how they interact with host cells.

Other experts in the field note that this breakthrough could revolutionize the detection and treatment of tumor biomarkers. Advances in DNA nanotechnology and viral vector delivery systems are already contributing to rapid and sensitive detection of cancer-related proteins, and the new knowledge of HERV-K Env’s structure provides a critical tool for further innovation.

The research also highlights the broader impact of viral proteins in human biology and disease. While HERV-K can no longer produce infectious viruses, its Env protein remains active in certain pathological conditions, making it a promising focus for future studies on cancer and immune system disorders. The mapping of this protein is expected to catalyze new collaborations between structural biologists, immunologists, and clinical researchers aiming to translate these findings into clinical applications.