| Abstract [eng] |
The object of this work is three influenza virus nucleoproteins (NP). The two major surface glycoproteins, hemagglutinin (HA) and neuraminidase (NA), are currently the main vaccine targets. However, both HA and NA have high mutation rates and as a result the antigenic drift and/or shift allows the virus to escape from established humoral immunity in the host. Vaccines must then be reformulated. By contrast, internal viral proteins, such as NP, are considerably more conserved carrying out multiple functions in influenza virus life cycle, and consequently are ideal targets for T-cell-mediated immunity and antiviral drugs. In the search for new anti-influenza agents, the viral polymerase has often been targeted due to the involvement of multiple conserved proteins and their distinct activities. However, NP has recently emerged as a new potential target for anti-influenza drug development. In this context, an atomic resolution structure of NP is of crucial importance. This work focused on the development of influenza virus NP purification strategy using S. cerevisiae expression system. The three NP proteins (IBV-NP-L, IBV-NP-S, IAV-NP) were successfully purified handling newly developed effective and efficient strategy which included various purification steps. |
