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Viruses
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RNA Viruses and Membranes
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RNA Viruses and Membranes

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

Deadline for manuscript submissions: closed (28 February 2021) | Viewed by 16302

Special Issue Editor

Dr. Delphine M. Muriaux

E-Mail Website
Guest Editor
IRIM CNRS, University of Montpellier, Montpellier, France
Interests: RNA envelopped viruses assembly; super resolution microscopy; HIV-1 assembly; CD4 T cell plasma membrane; viral proteins; host-cell lipids; sub-plasma membrane; pandemic Influenza H1N1; respiratory viruses; fluorescent replicative viruses; antiviral compounds; emerging SARS-CoV2; arboviruses
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enveloped viruses are obligatory host cell parasites that require host cell membranes as platforms for replicating and assembling into newly formed infectious particles. Thus, cell membranes, lipids, and host cell factors associated with membranes remain in close interplay with virus factories. Enveloped viruses can bud from the host cell plasma membrane, where the main viral components are targeted and assemble into particles, as in the case for retroviruses. Some respiratory viruses, such as influenza, also assemble at the host cell plasma membrane, where their viral ribonucleoprotein complexes are targeted for their transport via intracellular vesicles. Other RNA enveloped viruses, such as the recent emerging SARS-CoV2 coronavirus or the re-emerging Dengue virus, prefer to usurp the endoplasmic reticulum and trans-Golgi to developed virus factories, ending up in completely deforming the ER membrane by creating an army of accumulating viruses until the cell burns out. Viruses will use either the plasma membrane, secretory pathway, or exosomal pathway to exit the infected cell. All of these processes heavily exploit the host cell lipids and membranes as well as vesicle trafficking, resulting in the complete diversion of host cell lipid metabolism and membrane function towards virus manufacture.

This Special Issue is designed to provide an up-to-date view of enveloped RNA virus particle assembly mechanisms, including virus–membrane interactions, in the light of virology, biology, biochemistry, biophysics, or superresolution microscopy.

Prof. Dr. Delphine M. Muriaux
Guest Editor

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

  • RNA envelopped viruses
  • virus assembly
  • budding
  • membrane curvature
  • lipids
  • membrane nanodomains
  • virus factories
  • virus containing compartment
  • virus trafficking
  • virus exocytosis

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Related Special Issues

Published Papers (4 papers)

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Research

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13 pages, 3462 KiB  
Article
Hepatitis D Virus Entry Inhibitors Based on Repurposing Intestinal Bile Acid Reabsorption Inhibitors
by Michael Kirstgen, Kira Alessandra Alicia Theresa Lowjaga, Simon Franz Müller, Nora Goldmann, Felix Lehmann, Dieter Glebe, Karl-Heinz Baringhaus and Joachim Geyer
Viruses 2021, 13(4), 666; https://doi.org/10.3390/v13040666 - 12 Apr 2021
Cited by 7 | Viewed by 3044
Abstract
Identification of Na+/taurocholate co-transporting polypeptide (NTCP) as high-affinity hepatic entry receptor for the Hepatitis B and D viruses (HBV/HDV) opened the field for target-based development of cell-entry inhibitors. However, most of the HBV/HDV entry inhibitors identified so far also interfere with [...] Read more.
Identification of Na+/taurocholate co-transporting polypeptide (NTCP) as high-affinity hepatic entry receptor for the Hepatitis B and D viruses (HBV/HDV) opened the field for target-based development of cell-entry inhibitors. However, most of the HBV/HDV entry inhibitors identified so far also interfere with the physiological bile acid transporter function of NTCP. The present study aimed to identify more virus-selective inhibitors of NTCP by screening of 87 propanolamine derivatives from the former development of intestinal bile acid reabsorption inhibitors (BARIs), which interact with the NTCP-homologous intestinal apical sodium-dependent bile acid transporter (ASBT). In NTCP-HEK293 cells, the ability of these compounds to block the HBV/HDV-derived preS1-peptide binding to NTCP (virus receptor function) as well as the taurocholic acid transport via NTCP (bile acid transporter function) were analyzed in parallel. Hits were subsequently validated by performing in vitro HDV infection experiments in NTCP-HepG2 cells. The most potent compounds S985852, A000295231, and S973509 showed in vitro anti-HDV activities with IC50 values of 15, 40, and 70 µM, respectively, while the taurocholic acid uptake inhibition occurred at much higher IC50 values of 24, 780, and 490 µM, respectively. In conclusion, repurposing of compounds from the BARI class as novel HBV/HDV entry inhibitors seems possible and even enables certain virus selectivity based on structure-activity relationships. Full article
(This article belongs to the Special Issue RNA Viruses and Membranes)
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9 pages, 1402 KiB  
Article
Super-Resolution STED Microscopy-Based Mobility Studies of the Viral Env Protein at HIV-1 Assembly Sites of Fully Infected T-Cells
by Jakub Chojnacki and Christian Eggeling
Viruses 2021, 13(4), 608; https://doi.org/10.3390/v13040608 - 2 Apr 2021
Cited by 4 | Viewed by 3376
Abstract
The ongoing threat of human immunodeficiency virus (HIV-1) requires continued, detailed investigations of its replication cycle, especially when combined with the most physiologically relevant, fully infectious model systems. Here, we demonstrate the application of the combination of stimulated emission depletion (STED) super-resolution microscopy [...] Read more.
The ongoing threat of human immunodeficiency virus (HIV-1) requires continued, detailed investigations of its replication cycle, especially when combined with the most physiologically relevant, fully infectious model systems. Here, we demonstrate the application of the combination of stimulated emission depletion (STED) super-resolution microscopy with beam-scanning fluorescence correlation spectroscopy (sSTED-FCS) as a powerful tool for the interrogation of the molecular dynamics of HIV-1 virus assembly on the cell plasma membrane in the context of a fully infectious virus. In this process, HIV-1 envelope glycoprotein (Env) becomes incorporated into the assembling virus by interacting with the nascent Gag structural protein lattice. Molecular dynamics measurements at these distinct cell surface sites require a guiding strategy, for which we have used a two-colour implementation of sSTED-FCS to simultaneously target individual HIV-1 assembly sites via the aggregated Gag signal. We then compare the molecular mobility of Env proteins at the inside and outside of the virus assembly area. Env mobility was shown to be highly reduced at the assembly sites, highlighting the distinct trapping of Env as well as the usefulness of our methodological approach to study the molecular mobility of specifically targeted sites at the plasma membrane, even under high-biosafety conditions. Full article
(This article belongs to the Special Issue RNA Viruses and Membranes)
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14 pages, 2557 KiB  
Article
The Minor Matrix Protein VP24 from Ebola Virus Lacks Direct Lipid-Binding Properties
by Yuan Su and Robert V. Stahelin
Viruses 2020, 12(8), 869; https://doi.org/10.3390/v12080869 - 8 Aug 2020
Cited by 2 | Viewed by 4520
Abstract
Viral protein 24 (VP24) from Ebola virus (EBOV) was first recognized as a minor matrix protein that associates with cellular membranes. However, more recent studies shed light on its roles in inhibiting viral genome transcription and replication, facilitating nucleocapsid assembly and transport, and [...] Read more.
Viral protein 24 (VP24) from Ebola virus (EBOV) was first recognized as a minor matrix protein that associates with cellular membranes. However, more recent studies shed light on its roles in inhibiting viral genome transcription and replication, facilitating nucleocapsid assembly and transport, and interfering with immune responses in host cells through downregulation of interferon (IFN)-activated genes. Thus, whether VP24 is a peripheral protein with lipid-binding ability for matrix layer recruitment has not been explored. Here, we examined the lipid-binding ability of VP24 with a number of lipid-binding assays. The results indicated that VP24 lacked the ability to associate with lipids tested regardless of VP24 posttranslational modifications. We further demonstrate that the presence of the EBOV major matrix protein VP40 did not promote VP24 membrane association in vitro or in cells. Further, no protein–protein interactions between VP24 and VP40 were detected by co-immunoprecipitation. Confocal imaging and cellular membrane fractionation analyses in human cells suggested VP24 did not specifically localize at the plasma membrane inner leaflet. Overall, we provide evidence that EBOV VP24 is not a lipid-binding protein and its presence in the viral matrix layer is likely not dependent on direct lipid interactions. Full article
(This article belongs to the Special Issue RNA Viruses and Membranes)
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Review

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20 pages, 2279 KiB  
Review
Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses
by Lisa Welker, Jean-Christophe Paillart and Serena Bernacchi
Viruses 2021, 13(8), 1559; https://doi.org/10.3390/v13081559 - 6 Aug 2021
Cited by 20 | Viewed by 4287
Abstract
Late assembly (L) domains are conserved sequences that are necessary for the late steps of viral replication, acting like cellular adaptors to engage the ESCRT membrane fission machinery that promote virion release. These short sequences, whose mutation or deletion produce the accumulation of [...] Read more.
Late assembly (L) domains are conserved sequences that are necessary for the late steps of viral replication, acting like cellular adaptors to engage the ESCRT membrane fission machinery that promote virion release. These short sequences, whose mutation or deletion produce the accumulation of immature virions at the plasma membrane, were firstly identified within retroviral Gag precursors, and in a further step, also in structural proteins of many other enveloped RNA viruses including arenaviruses, filoviruses, rhabdoviruses, reoviruses, and paramyxoviruses. Three classes of L domains have been identified thus far (PT/SAP, YPXnL/LXXLF, and PPxY), even if it has recently been suggested that other motifs could act as L domains. Here, we summarize the current state of knowledge of the different types of L domains and their cellular partners in the budding events of RNA viruses, with a particular focus on retroviruses. Full article
(This article belongs to the Special Issue RNA Viruses and Membranes)
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