ニパウイルスのN、P、Mタンパク質間の協調的な相互作用が distinct な封入体の形成を駆動する
Mitsuki Yasukochi1, Mika Hosogi1, Yuki Kitai1
1Department of Microbiology, Graduate School of Medicine and Faculty of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.
Abstract:
Nipah virus (NiV), a highly pathogenic zoonotic paramyxovirus, forms two distinct types of membrane-less organelles called inclusion bodies (IBs): cytosolic IBs, which serve as sites of viral RNA synthesis, and those beneath the plasma membrane (IB-PMs), which function in viral particle assembly and budding. We identified the essential domains of the NiV nucleocapsid (N) and phospho (P) proteins required for the formation of cytosolic IB-like structures with liquid-like properties. Dual-site interactions between the N- and C-terminal regions of the N and P proteins were necessary for generating these liquid organelles. In contrast, the matrix protein, along with the N and P proteins, was indispensable for the formation of IB-PM-like structures with low internal fluidity. These findings demonstrate that NiV employs specific protein-protein interactions to generate spatially and functionally distinct IBs, providing new insight into the molecular mechanisms governing viral RNA synthesis and particle formation.
関連する概念動画
Intralumenal Vesicles and Multivesicular Bodies
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Intracellular Movement of Viruses and Bacteria
Viral Structure
Phosphoinositides and PIPs
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
SNAREs and Membrane Fusion
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...


