The HIV-1 matrix protein (MA) is synthesised as the N-terminal domain of the structural polyprotein Gag, and upon virus release is cleaved from Gag by the viral protease. We have shown that this causes MA to rear-range between two different hexameric protein lattices within the virus particle suggesting that MA has un-discovered functions in maturation and entry. Here we will use cryo-electron microscopy and other methods to ask: What is the mechanism that triggers structural rearrangement of MA? Does MA maturation cause rearrangement of the viral envelope protein to make the virus infectious? Does mature MA promote infection of the target cell?
DFG Programme
Collaborative Research Centres
