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Viruses
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Nucleocapsids of Paramyxoviruses
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Nucleocapsids of Paramyxoviruses

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Animal Viruses".

Deadline for manuscript submissions: closed (30 October 2021) | Viewed by 18404

Special Issue Editors

Prof. Dr. Rob W Ruigrok

E-Mail Website
Guest Editor
Institut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 38058 Grenoble, France
Interests: negative strand RNA viruses; structural biology of viruses; structure of RNA of viruses
Special Issues, Collections and Topics in MDPI journals
Dr. Martin Blackledge

E-Mail Website
Guest Editor
Institut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 38058 Grenoble, France
Interests: protein dynamics; nuclear magnetic resonance spectroscopy; intrinsically disordered proteins; self-assembly
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The viral RNA of the viruses of the Paramyxoviridae is always bound to the nucleoprotein (N), making a helical structure (nucleocapsid), and the phosphoprotein (P) transports the polymerase (L) to this helical structure. The nucleocapsid provides the template for the mRNA and the v- and c-RNA of the virus. Recently, N and P have also been shown to form liquid-like membraneless compartments (via liquid–liquid phase separation, LLPS, of viral proteins) which comprise different components of the viral replication complex, forming so-called viral-factories. LLPS could also provide protection of the viral RNA and associated RNA transcription machinery from the innate immune system.

This call of manuscripts would concentrate on proteins in the nucleocapsid, N, P and L, shorter proteins from the gene of P (V and C), LLPS of these proteins, and all cell proteins that bind to these viral proteins and complexes.

Prof. Rob W Ruigrok
Dr. Martin Blackledge
Guest Editors

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Viruses is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • paramyxoviridae
  • measles virus
  • nucleocapsid
  • nucleoprotein
  • phosphoprotein
  • V and C proteins
  • liquid–liquid phase separation
  • replication paramyxoviruses

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Published Papers (5 papers)

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Review

22 pages, 4557 KiB  
Review
C Proteins: Controllers of Orderly Paramyxovirus Replication and of the Innate Immune Response
by Oliver Siering, Roberto Cattaneo and Christian K. Pfaller
Viruses 2022, 14(1), 137; https://doi.org/10.3390/v14010137 - 12 Jan 2022
Cited by 11 | Viewed by 3938
Abstract
Particles of many paramyxoviruses include small amounts of proteins with a molecular weight of about 20 kDa. These proteins, termed “C”, are basic, have low amino acid homology and some secondary structure conservation. C proteins are encoded in alternative reading frames of the [...] Read more.
Particles of many paramyxoviruses include small amounts of proteins with a molecular weight of about 20 kDa. These proteins, termed “C”, are basic, have low amino acid homology and some secondary structure conservation. C proteins are encoded in alternative reading frames of the phosphoprotein gene. Some viruses express nested sets of C proteins that exert their functions in different locations: In the nucleus, they interfere with cellular transcription factors that elicit innate immune responses; in the cytoplasm, they associate with viral ribonucleocapsids and control polymerase processivity and orderly replication, thereby minimizing the activation of innate immunity. In addition, certain C proteins can directly bind to, and interfere with the function of, several cytoplasmic proteins required for interferon induction, interferon signaling and inflammation. Some C proteins are also required for efficient virus particle assembly and budding. C-deficient viruses can be grown in certain transformed cell lines but are not pathogenic in natural hosts. C proteins affect the same host functions as other phosphoprotein gene-encoded proteins named V but use different strategies for this purpose. Multiple independent systems to counteract host defenses may ensure efficient immune evasion and facilitate virus adaptation to new hosts and tissue environments. Full article
(This article belongs to the Special Issue Nucleocapsids of Paramyxoviruses)
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11 pages, 2215 KiB  
Review
Insights into Paramyxovirus Nucleocapsids from Diverse Assemblies
by Tianhao Li and Qing-Tao Shen
Viruses 2021, 13(12), 2479; https://doi.org/10.3390/v13122479 - 10 Dec 2021
Cited by 8 | Viewed by 3371
Abstract
All paramyxoviruses, which include the mumps virus, measles virus, Nipah virus, Newcastle disease virus, and Sendai virus, have non-segmented single-stranded negative-sense RNA genomes. These RNA genomes are enwrapped throughout the viral life cycle by nucleoproteins, forming helical nucleocapsids. In addition to these helical [...] Read more.
All paramyxoviruses, which include the mumps virus, measles virus, Nipah virus, Newcastle disease virus, and Sendai virus, have non-segmented single-stranded negative-sense RNA genomes. These RNA genomes are enwrapped throughout the viral life cycle by nucleoproteins, forming helical nucleocapsids. In addition to these helical structures, recombinant paramyxovirus nucleocapsids may occur in other assembly forms such as rings, clam-shaped structures, and double-headed nucleocapsids; the latter two are composed of two single-stranded helices packed in a back-to-back pattern. In all of these assemblies, the neighboring nucleoprotein protomers adopt the same domain-swapping mode via the N-terminal arm, C-terminal arm, and recently disclosed N-hole. An intrinsically disordered region in the C-terminal domain of the nucleoproteins, called the N-tail, plays an unexpected role in regulating the transition among the different assembly forms that occurs with other viral proteins, especially phosphoprotein. These structures, together with the helical nucleocapsids, significantly enrich the structural diversity of the paramyxovirus nucleocapsids and help explain the functions of these diverse assemblies, including RNA genome protection, transcription, and replication, as well as encapsulation. Full article
(This article belongs to the Special Issue Nucleocapsids of Paramyxoviruses)
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12 pages, 2075 KiB  
Review
Sendai Virus and a Unified Model of Mononegavirus RNA Synthesis
by Daniel Kolakofsky, Philippe Le Mercier, Machiko Nishio, Martin Blackledge, Thibaut Crépin and Rob W. H. Ruigrok
Viruses 2021, 13(12), 2466; https://doi.org/10.3390/v13122466 - 9 Dec 2021
Cited by 3 | Viewed by 3144
Abstract
Vesicular stomatitis virus (VSV), the founding member of the mononegavirus order (Mononegavirales), was found to be a negative strand RNA virus in the 1960s, and since then the number of such viruses has continually increased with no end in sight. Sendai [...] Read more.
Vesicular stomatitis virus (VSV), the founding member of the mononegavirus order (Mononegavirales), was found to be a negative strand RNA virus in the 1960s, and since then the number of such viruses has continually increased with no end in sight. Sendai virus (SeV) was noted soon afterwards due to an outbreak of newborn pneumonitis in Japan whose putative agent was passed in mice, and nowadays this mouse virus is mainly the bane of animal houses and immunologists. However, SeV was important in the study of this class of viruses because, like flu, it grows to high titers in embryonated chicken eggs, facilitating the biochemical characterization of its infection and that of its nucleocapsid, which is very close to that of measles virus (MeV). This review and opinion piece follow SeV as more is known about how various mononegaviruses express their genetic information and carry out their RNA synthesis, and proposes a unified model based on what all MNV have in common. Full article
(This article belongs to the Special Issue Nucleocapsids of Paramyxoviruses)
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28 pages, 10495 KiB  
Review
The Nucleocapsid of Paramyxoviruses: Structure and Function of an Encapsidated Template
by Louis-Marie Bloyet
Viruses 2021, 13(12), 2465; https://doi.org/10.3390/v13122465 - 9 Dec 2021
Cited by 13 | Viewed by 3606
Abstract
Viruses of the Paramyxoviridae family share a common and complex molecular machinery for transcribing and replicating their genomes. Their non-segmented, negative-strand RNA genome is encased in a tight homopolymer of viral nucleoproteins (N). This ribonucleoprotein complex, termed a nucleocapsid, is the template of [...] Read more.
Viruses of the Paramyxoviridae family share a common and complex molecular machinery for transcribing and replicating their genomes. Their non-segmented, negative-strand RNA genome is encased in a tight homopolymer of viral nucleoproteins (N). This ribonucleoprotein complex, termed a nucleocapsid, is the template of the viral polymerase complex made of the large protein (L) and its co-factor, the phosphoprotein (P). This review summarizes the current knowledge on several aspects of paramyxovirus transcription and replication, including structural and functional data on (1) the architecture of the nucleocapsid (structure of the nucleoprotein, interprotomer contacts, interaction with RNA, and organization of the disordered C-terminal tail of N), (2) the encapsidation of the genomic RNAs (structure of the nucleoprotein in complex with its chaperon P and kinetics of RNA encapsidation in vitro), and (3) the use of the nucleocapsid as a template for the polymerase complex (release of the encased RNA and interaction network allowing the progress of the polymerase complex). Finally, this review presents models of paramyxovirus transcription and replication. Full article
(This article belongs to the Special Issue Nucleocapsids of Paramyxoviruses)
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Graphical abstract

19 pages, 3005 KiB  
Review
Interactions between the Nucleoprotein and the Phosphoprotein of Pneumoviruses: Structural Insight for Rational Design of Antivirals
by Hortense Decool, Lorène Gonnin, Irina Gutsche, Christina Sizun, Jean-François Eléouët and Marie Galloux
Viruses 2021, 13(12), 2449; https://doi.org/10.3390/v13122449 - 6 Dec 2021
Cited by 6 | Viewed by 3521
Abstract
Pneumoviruses include pathogenic human and animal viruses, the most known and studied being the human respiratory syncytial virus (hRSV) and the metapneumovirus (hMPV), which are the major cause of severe acute respiratory tract illness in young children worldwide, and main pathogens infecting elderly [...] Read more.
Pneumoviruses include pathogenic human and animal viruses, the most known and studied being the human respiratory syncytial virus (hRSV) and the metapneumovirus (hMPV), which are the major cause of severe acute respiratory tract illness in young children worldwide, and main pathogens infecting elderly and immune-compromised people. The transcription and replication of these viruses take place in specific cytoplasmic inclusions called inclusion bodies (IBs). These activities depend on viral polymerase L, associated with its cofactor phosphoprotein P, for the recognition of the viral RNA genome encapsidated by the nucleoprotein N, forming the nucleocapsid (NC). The polymerase activities rely on diverse transient protein-protein interactions orchestrated by P playing the hub role. Among these interactions, P interacts with the NC to recruit L to the genome. The P protein also plays the role of chaperone to maintain the neosynthesized N monomeric and RNA-free (called N0) before specific encapsidation of the viral genome and antigenome. This review aims at giving an overview of recent structural information obtained for hRSV and hMPV P, N, and more specifically for P-NC and N0-P complexes that pave the way for the rational design of new antivirals against those viruses. Full article
(This article belongs to the Special Issue Nucleocapsids of Paramyxoviruses)
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