Recognizing molecules as "self," versus foreign invaders to be destroyed, is a central responsibility of the immune system. Tumors closely resemble self or "host" tissues and can confuse the system. Viruses and bacteria are immediately recognizable as foreign, but have learned to change shape so often that the system loses track of them. Pathogens use the same tricks to escape the immunity provided by vaccines.
In an effort to deny diseases the ability to hide, researchers have for years been asking a key question: Why do our bodies select certain, small pieces (epitopes) of each disease-causing molecule to trigger an immune response, while ignoring the rest? Those few, triggering protein fragments are termed "immunodominant." Unfortunately, the immune system sometimes makes poor choices about which epitopes to pay attention to, and which to ignore. Understanding of how immunodominance is conferred would enable vaccine designers to shift the immune system spotlight to parts of pathogens that they cannot change in efforts to escape detection. For example, a vaccine could be designed to target a protein fragment central to a virus's ability to reproduce, or to invade its prey.
"Our study identified for the first time the chemical mechanism that determines immunodominance, and proved that it can be fine-tuned," said Andrea Sant, Ph.D., a professor within the David H. Smith Center for Vaccine Biology and Immunology at the University of Rochester Medical Center, and the stud
Contact: Greg Williams
University of Rochester Medical Center