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Viruses
Special Issues
Influenza Virus and SARS-CoV-2 Structures: Entry, Replication, and Assembly
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Influenza Virus and SARS-CoV-2 Structures: Entry, Replication, and Assembly

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "SARS-CoV-2 and COVID-19".

Deadline for manuscript submissions: closed (31 May 2023) | Viewed by 9626

Special Issue Editor

Dr. Michael D. Vahey

E-Mail Website
Guest Editor
Department of Biomedical Engineering, Washington University in St. Louis, St. Louis, MO 63110-1093, USA
Interests: influenza a virus; virus assembly; fluorescence microscopy; antibody-virus interactions; biophysics; chemical biology

Special Issue Information

Dear Colleagues,

Influenza viruses cause recurring epidemics and occasional pandemics, producing mild to severe respiratory infections in millions of people worldwide each year. The virions that cause these infections are structurally complex. Influenza virus particles are composed of a host-derived lipid envelope containing viral membrane proteins, an interior matrix layer that lines the viral envelope, and an organized bundle of viral ribonucleoprotein complexes, the virus’s transcription and replication machinery. In addition to these viral factors, influenza virions also incorporate proteins from the host during assembly. The structure and the molecular composition of the virion is fundamental to its ability to transmit throughout the environment and to infect new cells. Recent developments in methodology, including light and electron microscopy, have advanced our knowledge of the structure and function of the influenza virus. This work has begun to uncover how the structure and composition of the virion is established during assembly and how it contributes to viral transmission and cellular infection.

This Special Issue invites both updated reviews and original research articles on topics relating to the structure and molecular organization of influenza viruses and SARS-CoV-2, including insights into virus assembly and the contributions of virion structure to viral attachment, entry, and uncoating.

Dr. Michael D. Vahey
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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

  • influenza viruses
  • virus structure
  • virus assembly
  • genome packaging
  • viral entry
  • membrane fusion
  • uncoating
  • host-virus interactions
  • fluorescence microscopy
  • electron microscopy
  • SARS-CoV-2

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Published Papers (3 papers)

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Research

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23 pages, 4581 KiB  
Article
Phosphatidylinositol 4,5-Bisphosphate Mediates the Co-Distribution of Influenza A Hemagglutinin and Matrix Protein M1 at the Plasma Membrane
by Prakash Raut, Bright Obeng, Hang Waters, Joshua Zimmerberg, Julie A. Gosse and Samuel T. Hess
Viruses 2022, 14(11), 2509; https://doi.org/10.3390/v14112509 - 12 Nov 2022
Cited by 5 | Viewed by 2289
Abstract
The fully assembled influenza A virus (IAV) has on its surface the highest density of a single membrane protein found in nature—the glycoprotein hemagglutinin (HA) that mediates viral binding, entry, and assembly. HA clusters at the plasma membrane of infected cells, and the [...] Read more.
The fully assembled influenza A virus (IAV) has on its surface the highest density of a single membrane protein found in nature—the glycoprotein hemagglutinin (HA) that mediates viral binding, entry, and assembly. HA clusters at the plasma membrane of infected cells, and the HA density (number of molecules per unit area) of these clusters correlates with the infectivity of the virus. Dense HA clusters are considered to mark the assembly site and ultimately lead to the budding of infectious IAV. The mechanism of spontaneous HA clustering, which occurs with or without other viral components, has not been elucidated. Using super-resolution fluorescence photoactivation localization microscopy (FPALM), we have previously shown that these HA clusters are interdependent on phosphatidylinositol 4,5-biphosphate (PIP2). Here, we show that the IAV matrix protein M1 co-clusters with PIP2, visualized using the pleckstrin homology domain. We find that cetylpyridinium chloride (CPC), which is a positively charged quaternary ammonium compound known for its antibacterial and antiviral properties at millimolar concentrations, disrupts M1 clustering and M1-PIP2 co-clustering at micromolar concentrations well below the critical micelle concentration (CMC). CPC also disrupts the co-clustering of M1 with HA at the plasma membrane, suggesting the role of host cell PIP2 clusters as scaffolds for gathering and concentrating M1 and HA to achieve their unusually high cluster densities in the IAV envelope. Full article
(This article belongs to the Special Issue Influenza Virus and SARS-CoV-2 Structures: Entry, Replication, and Assembly)
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21 pages, 3926 KiB  
Article
(+)-Usnic Acid and Its Derivatives as Inhibitors of a Wide Spectrum of SARS-CoV-2 Viruses
by Aleksandr S. Filimonov, Olga I. Yarovaya, Anna V. Zaykovskaya, Nadezda B. Rudometova, Dmitriy N. Shcherbakov, Varvara Yu. Chirkova, Dmitry S. Baev, Sophia S. Borisevich, Olga A. Luzina, Oleg V. Pyankov, Rinat A. Maksyutov and Nariman F. Salakhutdinov
Viruses 2022, 14(10), 2154; https://doi.org/10.3390/v14102154 - 29 Sep 2022
Cited by 11 | Viewed by 4202
Abstract
In order to test the antiviral activity, a series of usnic acid derivatives were synthesized, including new, previously undescribed compounds. The activity of the derivatives against three strains of SARS-CoV-2 virus was studied. To understand the mechanism of antiviral action, the inhibitory activity [...] Read more.
In order to test the antiviral activity, a series of usnic acid derivatives were synthesized, including new, previously undescribed compounds. The activity of the derivatives against three strains of SARS-CoV-2 virus was studied. To understand the mechanism of antiviral action, the inhibitory activity of the main protease of SARS-CoV-2 virus was studied using the developed model as well as the antiviral activity against the pseudoviral system with glycoprotein S of SARS-CoV-2 virus on its surface. It was shown that usnic acid exhibits activity against three strains of SARS-CoV-2 virus: Wuhan, Delta, and Omicron. Compounds 10 and 13 also showed high activity against the three strains. The performed biological studies and molecular modeling allowed us to assume that the derivatives of usnic acid bind in the N-terminal domain of the surface glycoprotein S at the binding site of the hemoglobin decay metabolite. Full article
(This article belongs to the Special Issue Influenza Virus and SARS-CoV-2 Structures: Entry, Replication, and Assembly)
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Review

Jump to: Research

32 pages, 4982 KiB  
Review
Structural Investigations of Interactions between the Influenza a Virus NS1 and Host Cellular Proteins
by Morgan E. Blake, Alex B. Kleinpeter, Alexander S. Jureka and Chad M. Petit
Viruses 2023, 15(10), 2063; https://doi.org/10.3390/v15102063 - 7 Oct 2023
Cited by 4 | Viewed by 2518
Abstract
The Influenza A virus is a continuous threat to public health that causes yearly epidemics with the ever-present threat of the virus becoming the next pandemic. Due to increasing levels of resistance, several of our previously used antivirals have been rendered useless. There [...] Read more.
The Influenza A virus is a continuous threat to public health that causes yearly epidemics with the ever-present threat of the virus becoming the next pandemic. Due to increasing levels of resistance, several of our previously used antivirals have been rendered useless. There is a strong need for new antivirals that are less likely to be susceptible to mutations. One strategy to achieve this goal is structure-based drug development. By understanding the minute details of protein structure, we can develop antivirals that target the most conserved, crucial regions to yield the highest chances of long-lasting success. One promising IAV target is the virulence protein non-structural protein 1 (NS1). NS1 contributes to pathogenicity through interactions with numerous host proteins, and many of the resulting complexes have been shown to be crucial for virulence. In this review, we cover the NS1-host protein complexes that have been structurally characterized to date. By bringing these structures together in one place, we aim to highlight the strength of this field for drug discovery along with the gaps that remain to be filled. Full article
(This article belongs to the Special Issue Influenza Virus and SARS-CoV-2 Structures: Entry, Replication, and Assembly)
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