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Viruses
Special Issues
Biology of Viral Surface Glycoproteins
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Biology of Viral Surface Glycoproteins

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

Deadline for manuscript submissions: closed (15 December 2021) | Viewed by 7014

Special Issue Editors

Dr. François-Loïc Cosset

E-Mail Website
Guest Editor
CIRI—Centre International de Recherche en Infectiologie, Université de Lyon, Université Claude Bernard Lyon 1, Inserm, U1111, CNRS, UMR5308, ENS Lyon, 46 allée d’Italie, F-69007 Lyon, France
Interests: emerging infectious diseases; hepatitis viruses; viral vectors
Special Issues, Collections and Topics in MDPI journals
Dr. Solène Denolly

E-Mail Website
Guest Editor
CIRI—Centre International de Recherche en Infectiologie
Interests: molecular virology; hepatitis C virus; flavivirus
Dr. Pierre-Yves Lozach

E-Mail Website
Guest Editor
CellNetworks—Cluster of Excellence and Center for Integrative Infectious Diseases Research (CIID), Department of Infectious Diseases, Virology, University Hospital Heidelberg, 69120 Heidelberg, Germany
Interests: amyloids; arbovirus; cell biology of virus entry; viral virulence factors
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The first challenge that viruses need to overcome when infecting host cells is to access the intracellular compartment. The surface glycoproteins of enveloped viruses play a major role in this process as they drive virus contact with host cell surface receptors and penetration into the cytosol. As such, viral glycoproteins are critical determinants of host range and tropism. Viral surface glycoproteins are also the primary targets of innate and adaptive immunity. Together, they represent important targets for vaccine development. In this Special Issue of Viruses, we would like to include opinions, reviews, and research articles that together not only provide a glance into the latest research in virus glycoprotein structure, virus–receptor interactions, and viral fusion, but also highlight the major achievements in the field of biology of virus surface glycoproteins made in recent years. All enveloped viruses will be considered. Studies on any aspect of the folding, maturation, glycans, and structure of viral glycoproteins are welcome, including novel technological approaches. Invited are also functional studies that provide new insights into the way viral glycoproteins contribute to signaling, penetration, fusion, and escape from immune effectors and responses. With this Special Issue, we aim to offer a space for enthusiastic discussions on future directions of research on viral glycoproteins and promote some areas that are understudied or emerging.

Dr. François-Loïc Cosset
Dr. Solène Denolly
Dr. Pierre-Yves Lozach
Guest Editors

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

  • enveloped virus
  • folding
  • glycan
  • structure
  • viral glycoprotein
  • virus assembly
  • virus entry
  • virus fusion
  • neutralization
  • immunity
  • immune escape

Published Papers (2 papers)

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Research

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17 pages, 46566 KiB  
Article
An Absolutely Conserved Tryptophan in the Stem of the Envelope Protein E of Flaviviruses Is Essential for the Formation of Stable Particles
by Iris Medits, Franz X. Heinz and Karin Stiasny
Viruses 2021, 13(9), 1727; https://doi.org/10.3390/v13091727 - 30 Aug 2021
Cited by 1 | Viewed by 2706
Abstract
The major envelope protein E of flaviviruses contains an ectodomain that is connected to the transmembrane domain by the so-called “stem” region. In mature flavivirus particles, the stem is composed of two or three mostly amphipathic α-helices and a conserved sequence element (CS) [...] Read more.
The major envelope protein E of flaviviruses contains an ectodomain that is connected to the transmembrane domain by the so-called “stem” region. In mature flavivirus particles, the stem is composed of two or three mostly amphipathic α-helices and a conserved sequence element (CS) with an undefined role in the viral life cycle. A tryptophan is the only residue within this region which is not only conserved in all vector-borne flaviviruses, but also in the group with no known vector. We investigated the importance of this residue in different stages of the viral life cycle by a mutagenesis-based approach using tick-borne encephalitis virus (TBEV). Replacing W421 by alanine or histidine strongly reduced the release of infectious virions and their thermostability, whereas fusion-related entry functions and virus maturation were still intact. Serial passaging of the mutants led to the emergence of a same-site compensatory mutation to leucine that largely restored these properties of the wildtype. The conserved tryptophan in CS (or another big hydrophobic amino acid at the same position) is thus essential for the assembly and infectivity of flaviviruses by being part of a network required for conferring stability to infectious particles. Full article
(This article belongs to the Special Issue Biology of Viral Surface Glycoproteins)
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Review

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18 pages, 3754 KiB  
Review
The Viral Class II Membrane Fusion Machinery: Divergent Evolution from an Ancestral Heterodimer
by Pablo Guardado-Calvo and Félix A. Rey
Viruses 2021, 13(12), 2368; https://doi.org/10.3390/v13122368 - 26 Nov 2021
Cited by 14 | Viewed by 2917
Abstract
A key step during the entry of enveloped viruses into cells is the merger of viral and cell lipid bilayers. This process is driven by a dedicated membrane fusion protein (MFP) present at the virion surface, which undergoes a membrane–fusogenic conformational change triggered [...] Read more.
A key step during the entry of enveloped viruses into cells is the merger of viral and cell lipid bilayers. This process is driven by a dedicated membrane fusion protein (MFP) present at the virion surface, which undergoes a membrane–fusogenic conformational change triggered by interactions with the target cell. Viral MFPs have been extensively studied structurally, and are divided into three classes depending on their three-dimensional fold. Because MFPs of the same class are found in otherwise unrelated viruses, their intra-class structural homology indicates horizontal gene exchange. We focus this review on the class II fusion machinery, which is composed of two glycoproteins that associate as heterodimers. They fold together in the ER of infected cells such that the MFP adopts a conformation primed to react to specific clues only upon contact with a target cell, avoiding premature fusion in the producer cell. We show that, despite having diverged in their 3D fold during evolution much more than the actual MFP, the class II accompanying proteins (AP) also derive from a distant common ancestor, displaying an invariant core formed by a β-ribbon and a C-terminal immunoglobulin-like domain playing different functional roles—heterotypic interactions with the MFP, and homotypic AP/AP contacts to form spikes, respectively. Our analysis shows that class II APs are easily identifiable with modern structural prediction algorithms, providing useful information in devising immunogens for vaccine design. Full article
(This article belongs to the Special Issue Biology of Viral Surface Glycoproteins)
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