Special Issue "Mechanisms of Viral Fusion and Applications in Antivirals"

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

Deadline for manuscript submissions: 31 December 2019.

Special Issue Editors

Dr. Sergi Padilla-Parra
E-Mail Website
Guest Editor
Head of Core in Cellular Imaging and Principal Investigator at Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford, OX3 7BN, UK
Interests: mechanism of HIV-1 virus fusion employing single molecule approaches
Prof. Shan-Lu Liu
E-Mail Website
Guest Editor
Director, Viruses and Emerging Pathogens Program, Infectious Diseases Institute, The Ohio State University;
Professor, Center for Retrovirus Research, Department of Veterinary Biosciences, Department of Microbial Infection and Immunity, The Ohio State University, 1900 Coffey Rd., Columbus, OH 43210, USA
Interests: viral membrane fusion and entry; cellular restriction factors against viral infection; retroviral oncogenesis; viral envelope glycoproteins; lentiviral vectors and gene therapy

Special Issue Information

Dear colleague,

Virus-cell fusion is essential for enveloped viruses to enter host cells. Enveloped viruses acquire their membrane from infected host cells during the budding process. Many important human pathogens are enveloped viruses, such as human immunodeficiency virus (HIV), Hepatitis C (HCV), and Ebola virus (EBOV). The virus–cell fusion process is carried out by one or more viral envelope glycoprotein or fusion proteins. Viral fusion proteins contain a typical fusion peptide or a fusion loop that is responsible for initial insertion into host membrane, and they are normally present in virions as a prefusion state, which must be triggered to mediate fusion and viral entry. The current known triggers include receptor binding, low pH, receptor-binding plus low pH, and cellular cathepsins, but may also include calcium and certain lipids. However, regardless of distinct prefusion structures and triggers, the post-fusion state of all viral fusion proteins is a trimer of hairpin.

In this Special Issue, we will focus on the most recent advances in understanding the mechanism of virus–cell fusion, with a special emphasis on advanced imaging approaches (single molecule techniques and super-resolution) and viral fusion triggers. We will also focus on new developments on neutralizing antibodies, antivirals, and vaccine development.

Dr. Sergi Padilla-Parra
Prof. Shan-Lu Liu
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 1800 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

  • virus–cell fusion mechanism 
  • fusion triggers 
  • single viral particle imaging 
  • membrane fusion kinetics
  • advanced microscopy
  • neutralizing antibodies 
  • small molecule fusion inhibitors 
  • antiviral drugs

Published Papers (3 papers)

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Research

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Open AccessArticle
EWI-2 Inhibits Cell–Cell Fusion at the HIV-1 Virological Presynapse
Viruses 2019, 11(12), 1082; https://doi.org/10.3390/v11121082 - 20 Nov 2019
Abstract
Cell-to-cell transfer of virus particles at the Env-dependent virological synapse (VS) is a highly efficient mode of HIV-1 transmission. While cell–cell fusion could be triggered at the VS, leading to the formation of syncytia and preventing exponential growth of the infected cell population, [...] Read more.
Cell-to-cell transfer of virus particles at the Env-dependent virological synapse (VS) is a highly efficient mode of HIV-1 transmission. While cell–cell fusion could be triggered at the VS, leading to the formation of syncytia and preventing exponential growth of the infected cell population, this is strongly inhibited by both viral (Gag) and host (ezrin and tetraspanins) proteins. Here, we identify EWI-2, a protein that was previously shown to associate with ezrin and tetraspanins, as a host factor that contributes to the inhibition of Env-mediated cell–cell fusion. Using quantitative fluorescence microscopy, shRNA knockdowns, and cell–cell fusion assays, we show that EWI-2 accumulates at the presynaptic terminal (i.e., the producer cell side of the VS), where it contributes to the fusion-preventing activities of the other viral and cellular components. We also find that EWI-2, like tetraspanins, is downregulated upon HIV-1 infection, most likely by Vpu. Despite the strong inhibition of fusion at the VS, T cell-based syncytia do form in vivo and in physiologically relevant culture systems, but they remain small. In regard to that, we demonstrate that EWI-2 and CD81 levels are restored on the surface of syncytia, where they (presumably) continue to act as fusion inhibitors. This study documents a new role for EWI-2 as an inhibitor of HIV-1-induced cell–cell fusion and provides novel insight into how syncytia are prevented from fusing indefinitely. Full article
(This article belongs to the Special Issue Mechanisms of Viral Fusion and Applications in Antivirals)

Review

Jump to: Research

Open AccessReview
Relating GPI-Anchored Ly6 Proteins uPAR and CD59 to Viral Infection
Viruses 2019, 11(11), 1060; https://doi.org/10.3390/v11111060 - 14 Nov 2019
Abstract
The Ly6 (lymphocyte antigen-6)/uPAR (urokinase-type plasminogen activator receptor) superfamily protein is a group of molecules that share limited sequence homology but conserved three-fingered structures. Despite diverse cellular functions, such as in regulating host immunity, cell adhesion, and migration, the physiological roles of these [...] Read more.
The Ly6 (lymphocyte antigen-6)/uPAR (urokinase-type plasminogen activator receptor) superfamily protein is a group of molecules that share limited sequence homology but conserved three-fingered structures. Despite diverse cellular functions, such as in regulating host immunity, cell adhesion, and migration, the physiological roles of these factors in vivo remain poorly characterized. Notably, increasing research has focused on the interplays between Ly6/uPAR proteins and viral pathogens, the results of which have provided new insight into viral entry and virus–host interactions. While LY6E (lymphocyte antigen 6 family member E), one key member of the Ly6E/uPAR-family proteins, has been extensively studied, other members have not been well characterized. Here, we summarize current knowledge of Ly6/uPAR proteins related to viral infection, with a focus on uPAR and CD59. Our goal is to provide an up-to-date view of the Ly6/uPAR-family proteins and associated virus–host interaction and viral pathogenesis. Full article
(This article belongs to the Special Issue Mechanisms of Viral Fusion and Applications in Antivirals)
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Open AccessReview
Emerging Role of LY6E in Virus–Host Interactions
Viruses 2019, 11(11), 1020; https://doi.org/10.3390/v11111020 - 03 Nov 2019
Cited by 1
Abstract
As a canonical lymphocyte antigen-6/urokinase-type plasminogen activator receptor Ly6/uPAR family protein, lymphocyte antigen 6 complex, locus E (LY6E), plays important roles in immunological regulation, T cell physiology, and oncogenesis. Emerging evidence indicates that LY6E is also involved in the modulation of viral infection. [...] Read more.
As a canonical lymphocyte antigen-6/urokinase-type plasminogen activator receptor Ly6/uPAR family protein, lymphocyte antigen 6 complex, locus E (LY6E), plays important roles in immunological regulation, T cell physiology, and oncogenesis. Emerging evidence indicates that LY6E is also involved in the modulation of viral infection. Consequently, viral infection and associated pathogenesis have been associated with altered LY6E gene expression. The interaction between viruses and the host immune system has offered insights into the biology of LY6E. In this review, we summarize the current knowledge of LY6E in the context of viral infection, particularly viral entry. Full article
(This article belongs to the Special Issue Mechanisms of Viral Fusion and Applications in Antivirals)
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