Assembly of Ebola Virus Matrix Protein is Regulated by Latch-Like Properties of N - and C-Terminal Tails

摘要

1. The assembly processes of full -length VP40 Ebola virus matrix protein has been monitored for the first time. 2. Treatment with 4M urea, as a mimic of plasma membrane interaction, causes instability in the hinge region, but the latch like association of the N - and C -tails prevents assembly. 3. Only upon binding of the RNA trimer are both tails strongly denatured, and assembly of octamers induced. 4. As RNA on its own is insufficient to induce assembly, we suggest that the initial in vivo destabilization may arise through interactions with the inner membrane.