Abstract
Formation of cytoplasmic inclusion bodies (IBs) is a hallmark of infections with non-segmented negative-strand RNA viruses (order Mononegavirales). We show here that Nipah virus (NiV), a bat-derived highly pathogenic member of the Paramyxoviridae family, differs from mononegaviruses of the Rhabdo-, Filo- and Pneumoviridae families by forming two types of IBs with distinct localizations, formation kinetics, and protein compositions. IBs in the perinuclear region form rapidly upon expression of the nucleocapsid proteins. These IBperi are highly mobile and associate with the aggresome marker y-tubulin. IBperi can recruit unrelated overexpressed cytosolic proteins but do not contain the viral matrix (M) protein. Additionally, NiV forms an as yet undescribed IB population at the plasma membrane (IBPM) that is y-tubulin-negative but contains the M protein. Infection studies with recombinant NiV revealed that IBPM require the M protein for their formation, and most likely represent sites of NiV assembly and budding. The identification of this novel type of plasma membrane-associated IBs not only provides new insights into NiV biology and may open new avenues to develop novel antiviral approaches to treat these highly pathogenic viruses, it also provides a basis for a more detailed characterization of IBs and their role in virus assembly and replication in infections with other Mononegavirales.
Highlights
Nipah virus (NiV) and the closely related Hendra virus (HeV) are members of the Henipavirus genus in the family Paramyxoviridae [1]
inclusion bodies (IBs) induced by members of the Paramyxoviridae family are much less well characterized, and this study provides evidence that paramyxoviral IBs may have different compositions and functions
At 24 h post infection (p.i.), multiple IBs were formed within NiV-induced syncytia (Fig 1A), and these IBs were found in the syncytium periphery, and partially located close to nuclei
Summary
Nipah virus (NiV) and the closely related Hendra virus (HeV) are members of the Henipavirus genus in the family Paramyxoviridae (order Mononegavirales) [1]. The genomic RNA together with the nucleoprotein (N), the phosphoprotein (P) and viral polymerase (L) form the nucleocapsid (NC) which is surrounded by a lipid envelope that is derived from the plasma membrane during the budding process Both NiV surface glycoproteins, the receptor-binding (G) and the fusion (F) protein, are incorporated into the viral envelope. While budding of correctly assembled, infectious virus particles was greatly reduced, viral RNA synthesis and viral protein synthesis in infected cells was not markedly different compared to wildtype infection [16]. This indicated that the NiV M protein is essential for assembly and budding but does not play a central role in virus replication and transcription processes
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