Assembly and transport of filovirus nucleocapsids

Filovirus-infected cells are characterized by typical cytoplasmic inclusion bodies (IBs) located in the perinuclear region. The formation of these IBs is induced mainly by the accumulation of the filoviral nucleoprotein NP, which recruits the other nucleocapsid proteins, the polymerase co-factor VP3...

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Bibliographic Details
Published in:PLoS pathogens Vol. 18; no. 7; p. e1010616
Main Authors: Dolnik, Olga, Becker, Stephan
Format: Journal Article
Language:English
Published: San Francisco Public Library of Science 28.07.2022
Public Library of Science (PLoS)
Subjects:
Actin
Amino acids
Assembly
Binding sites
Biological transport
Biology and Life Sciences
Budding
C-Terminus
Filoviridae
Genetic aspects
Genomes
Genomics
Handedness
Helices
Inclusion bodies
Medicine and Health Sciences
N-Terminus
Nucleocapsids
Nucleoproteins
Physiological aspects
Plasma
Polymerization
Protein interaction
Protein-protein interactions
Proteins
Review
Ribonucleic acid
RNA
RNA viruses
Structure
Synthesis
Tomography
Transcription factors
Transmission electron microscopy
Viral proteins
Virus research
VP24 protein
Germany
ISSN:1553-7374, 1553-7366, 1553-7374
Online Access:Get full text
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Summary:Filovirus-infected cells are characterized by typical cytoplasmic inclusion bodies (IBs) located in the perinuclear region. The formation of these IBs is induced mainly by the accumulation of the filoviral nucleoprotein NP, which recruits the other nucleocapsid proteins, the polymerase co-factor VP35, the polymerase L, the transcription factor VP30 and VP24 via direct or indirect protein–protein interactions. Replication of the negative-strand RNA genomes by the viral polymerase L and VP35 occurs in the IBs, resulting in the synthesis of positive-strand genomes, which are encapsidated by NP, thus forming ribonucleoprotein complexes (antigenomic RNPs). These newly formed antigenomic RNPs in turn serve as templates for the synthesis of negative-strand RNA genomes that are also encapsidated by NP (genomic RNPs). Still in the IBs, genomic RNPs mature into tightly packed transport-competent nucleocapsids (NCs) by the recruitment of the viral protein VP24. NCs are tightly coiled left-handed helices whose structure is mainly determined by the multimerization of NP at its N-terminus, and these helices form the inner layer of the NCs. The RNA genome is fixed by 2 lobes of the NP N-terminus and is thus guided by individual NP molecules along the turns of the helix. Direct interaction of the NP C-terminus with the VP35 and VP24 molecules forms the outer layer of the NCs. Once formed, NCs that are located at the border of the IBs recruit actin polymerization machinery to one of their ends to drive their transport to budding sites for their envelopment and final release. Here, we review the current knowledge on the structure, assembly, and transport of filovirus NCs.
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The authors have declared that no competing interests exist.
ISSN:1553-7374
1553-7366
1553-7374
DOI:10.1371/journal.ppat.1010616