CryoEM structure of the Nipah virus nucleocapsid assembly

Ker, De-Sheng; Jenkins, Huw T.; Greive, Sandra J.; Antson, A.A.

doi:10.1101/2020.01.20.912261

Cited by 3 publications

(1 citation statement)

References 43 publications

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“…1B), could confer a considerable reach to the elements of the replication machinery enabling them to act as scaffolds for partner tethering. It could also enable the L-P complex to simultaneously bind to successive turns of the helical nucleocapsid (one turn being ~6 nm high [1,155] (Fig. 1B).…”

Section: Disorder As a Determinant Of Scaffolding And Tetheringmentioning

confidence: 99%

Functional benefit of structural disorder for the replication of measles, Nipah and Hendra viruses

Gondelaud

Pesce

Nilsson

et al. 2022

Essays in Biochemistry

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Measles, Nipah and Hendra viruses are severe human pathogens within the Paramyxoviridae family. Their non-segmented, single-stranded, negative-sense RNA genome is encapsidated by the nucleoprotein (N) within a helical nucleocapsid that is the substrate used by the viral RNA-dependent-RNA-polymerase (RpRd) for transcription and replication. The RpRd is a complex made of the large protein (L) and of the phosphoprotein (P), the latter serving as an obligate polymerase cofactor and as a chaperon for N. Both the N and P proteins are enriched in intrinsically disordered regions (IDRs), i.e. regions devoid of stable secondary and tertiary structure. N possesses a C-terminal IDR (NTAIL), while P consists of a large, intrinsically disordered N-terminal domain (NTD) and a C-terminal domain (CTD) encompassing alternating disordered and ordered regions. The V and W proteins, two non-structural proteins that are encoded by the P gene via a mechanism of co-transcriptional edition of the P mRNA, are prevalently disordered too, sharing with P the disordered NTD. They are key players in the evasion of the host antiviral response and were shown to phase separate and to form amyloid-like fibrils in vitro. In this review, we summarize the available information on IDRs within the N, P, V and W proteins from these three model paramyxoviruses and describe their molecular partnership. We discuss the functional benefit of disorder to virus replication in light of the critical role of IDRs in affording promiscuity, multifunctionality, fine regulation of interaction strength, scaffolding functions and in promoting liquid–liquid phase separation and fibrillation.

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Section: Disorder As a Determinant Of Scaffolding And Tetheringmentioning

confidence: 99%

Functional benefit of structural disorder for the replication of measles, Nipah and Hendra viruses

Gondelaud

Pesce

Nilsson

et al. 2022

Essays in Biochemistry

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Structural Dynamics of the C-terminal X Domain of Nipah and Hendra Viruses Controls the Attachment to the C-terminal Tail of the Nucleocapsid Protein

Bourhis

Yabukarski

Communie

et al. 2022

Journal of Molecular Biology

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Structure and assembly of double-headed Sendai virus nucleocapsids

et al. 2021

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Paramyxoviruses, including the mumps virus, measles virus, Nipah virus and Sendai virus (SeV), have non-segmented single-stranded negative-sense RNA genomes which are encapsidated by nucleoproteins into helical nucleocapsids. Here, we reported a double-headed SeV nucleocapsid assembled in a tail-to-tail manner, and resolved its helical stems and clam-shaped joint at the respective resolutions of 2.9 and 3.9 Å, via cryo-electron microscopy. Our structures offer important insights into the mechanism of the helical polymerization, in particular via an unnoticed exchange of a N-terminal hole formed by three loops of nucleoproteins, and unveil the clam-shaped joint in a hyper-closed state for nucleocapsid dimerization. Direct visualization of the loop from the disordered C-terminal tail provides structural evidence that C-terminal tail is correlated to the curvature of nucleocapsid and links nucleocapsid condensation and genome replication and transcription with different assembly forms.

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CryoEM structure of the Nipah virus nucleocapsid assembly

Cited by 3 publications

References 43 publications

Functional benefit of structural disorder for the replication of measles, Nipah and Hendra viruses

Functional benefit of structural disorder for the replication of measles, Nipah and Hendra viruses

Structural Dynamics of the C-terminal X Domain of Nipah and Hendra Viruses Controls the Attachment to the C-terminal Tail of the Nucleocapsid Protein

Structure and assembly of double-headed Sendai virus nucleocapsids

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