ArticleThe Journal of general virology2025
Coordinated interactions among Nipah virus N, P and M proteins drive formation of distinct inclusion bodies.
Article in The Journal of general virology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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7 authors.
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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.
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