| Popis: |
Proteolytic processing of HIV-1 proteins is critical to the lifecycle of the virus. Maturation of virions from their non-infectious to their infectious form depends on a number of cleavage steps carried out by a viral enzyme, HIV-1 protease. Because of its critical role in infection, it has been the target of intense research, making it the most well studied proteolytic enzyme. Despite this, many unanswered questions remain regarding the precise actions of the protease during viral maturation. An improved understanding of cleavage dynamics could better inform drug design efforts and provide an important contribution to HIV-1 research. In this work, we use mass spectrometry to investigate specific HIV-1 protease cleavage events with the hope of developing a method to accurately assess cleavage efficiency, kinetics, and interdependence. Here we report the preliminary developmental steps taken to accomplish this. We establish a reliable workflow to evaluate HIV-1 protease processing efficiency in physiologically relevant conditions and discuss the computational approaches that would be necessary to derive meaningful interpretations. Such an analysis may lead to specific insights that would enable us to more effectively target HIV-1 protease. |
