Researchers at Stanford University and New York University have made significant strides in understanding the properties of the LAG-3 protein, shedding light on its structure and function. This breakthrough could have far-reaching implications for the development of immune checkpoint inhibitor drug candidates targeting LAG-3.
The study, published in Proceedings of the National Academy of Sciences, provides crucial insights into the molecular structure of LAG-3 and how it operates. Jennifer Cochran, the Addie and Al Macovski Professor in the School of Engineering and professor of bioengineering at Stanford University, and co-senior author of the study, expressed astonishment at the limited understanding of LAG-3’s function despite the significant investment in therapeutics targeting this protein.
LAG-3, like other checkpoint proteins, serves to prevent the immune system from attacking non-threatening entities. In the context of cancer, these proteins can shield tumor cells from immune recognition, hindering the body’s natural defense mechanisms. Current immunotherapies leverage lab-manufactured antibodies to deactivate these checkpoint proteins, allowing the immune system to identify and combat cancer cells.
While existing antibody treatments focus on checkpoint proteins CTLA-4 and PD-1, the unique mode of action of LAG-3 presents an opportunity for novel approaches in cancer therapy. Scientists are optimistic about the potential of targeting LAG-3, driven by its distinct mechanisms compared to CTLA-4 and PD-1. The differences in LAG-3’s functionality offer promising prospects for enhancing cancer treatment efficacy.
