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Special Issue "Viral Glycoprotein Incorporation"

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

Deadline for manuscript submissions: closed (30 September 2014)

Special Issue Editors

Guest Editor
Prof. Dr. Marc Johnson

Molecular Microbiology & Immunology, University of Missouri, USA
Website | E-Mail
Co-Guest Editor
Prof. Dr. Shan-Lu Liu

Center for Retrovirus Research and Department of Veterinary Biosciences, The Ohio State University, 1900 Coffey Rd., Columbus, OH 43210, USA
Website | E-Mail
Phone: (614) 292-8690
Fax: (614) 292-6473
Interests: cellular restriction factors against viral infection; retroviral entry and oncogenesis; membrane fusion and cell entry of Ebolavirus and Zika virus; viral envelope glycoproteins; lentiviral vectors and gene therapy

Special Issue Information

Dear Colleagues,

This special issue will overview the mechanisms by which viral envelope glycoproteins are acquired by different viruses in order to generate infectious viral particles. It will highlight both the common and divergent strategies evolved by viruses that facilitate the translocation of the viral transmembrane glycoproteins to the viral assembly sites. All enveloped viruses are considered. We shall explore how the varied life cycles of different enveloped viruses results in different mechanisms for glycoprotein acquisition. Cellular factors that modulate the viral glycoprotein expression, trafficking, and incorporation are also included.

Dr. Marc Johnson
Dr. Shan-Lu Liu
Guest Editors

Submission

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. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as 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 refereed through a 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 1500 CHF (Swiss Francs).

Keywords

  • viral glycoprotein
  • enveloped virus
  • env
  • protein trafficking
  • viral assembly sites
  • membrane dynamics
  • vesicular trafficking
  • cellular factors

Published Papers (7 papers)

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Research

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Open AccessArticle HSV-1 gM and the gK/pUL20 Complex Are Important for the Localization of gD and gH/L to Viral Assembly Sites
Viruses 2015, 7(3), 915-938; doi:10.3390/v7030915
Received: 22 December 2014 / Revised: 6 February 2015 / Accepted: 22 February 2015 / Published: 4 March 2015
Cited by 7 | PDF Full-text (2279 KB) | HTML Full-text | XML Full-text
Abstract
Herpes simplex virus-1 (HSV-1), like all herpesviruses, is a large complex DNA virus containing up to 16 different viral membrane proteins in its envelope. The assembly of HSV-1 particles occurs by budding/wrapping at intracellular membranes producing infectious virions contained within the lumen of
[...] Read more.
Herpes simplex virus-1 (HSV-1), like all herpesviruses, is a large complex DNA virus containing up to 16 different viral membrane proteins in its envelope. The assembly of HSV-1 particles occurs by budding/wrapping at intracellular membranes producing infectious virions contained within the lumen of cytoplasmic membrane-bound compartments that are then released by secretion. To ensure incorporation of all viral membrane proteins into the envelope, they need to be localized to the appropriate intracellular membranes either via the endocytic pathway or by direct targeting to assembly sites from the biosynthetic secretory pathway. Many HSV-1 envelope proteins encode targeting motifs that direct their endocytosis and targeting, while others do not, including the essential entry proteins gD and the gH/gL complex, and so it has been unclear how these envelope proteins reach the appropriate assembly compartments. We now show that efficient endocytosis of gD and gH/gL and their incorporation into mature virions relies upon the presence of the HSV-1 envelope proteins gM and the gK/pUL20 complex. Our data demonstrate both redundant and synergistic roles for gM and gK/pUL20 in controlling the targeting of gD and gH/L to the appropriate intracellular virus assembly compartments. Full article
(This article belongs to the Special Issue Viral Glycoprotein Incorporation)
Open AccessArticle Comparative Analysis of Glycoprotein B (gB) of Equine Herpesvirus Type 1 and Type 4 (EHV-1 and EHV-4) in Cellular Tropism and Cell-to-Cell Transmission
Viruses 2015, 7(2), 522-542; doi:10.3390/v7020522
Received: 3 December 2014 / Revised: 4 January 2015 / Accepted: 27 January 2015 / Published: 3 February 2015
Cited by 2 | PDF Full-text (1848 KB) | HTML Full-text | XML Full-text
Abstract
Glycoprotein B (gB) plays an important role in alphaherpesvirus cellular entry and acts in concert with gD and the gH/gL complex. To evaluate whether functional differences exist between gB1 and gB4, the corresponding genes were exchanged between the two viruses. The gB4-containing-EHV-1 (EHV-1_gB4)
[...] Read more.
Glycoprotein B (gB) plays an important role in alphaherpesvirus cellular entry and acts in concert with gD and the gH/gL complex. To evaluate whether functional differences exist between gB1 and gB4, the corresponding genes were exchanged between the two viruses. The gB4-containing-EHV-1 (EHV-1_gB4) recombinant virus was analyzed for growth in culture, cell tropism, and cell entry rivaling no significant differences when compared to parental virus. We also disrupted a potential integrin-binding motif, which did not affect the function of gB in culture. In contrast, a significant reduction of plaque sizes and growth kinetics of gB1-containing-EHV-4 (EHV-4_gB1) was evident when compared to parental EHV-4 and revertant viruses. The reduction in virus growth may be attributable to the loss of functional interaction between gB and the other envelope proteins involved in virus entry, including gD and gH/gL. Alternatively, gB4 might have an additional function, required for EHV-4 replication, which is not fulfilled by gB1. In conclusion, our results show that the exchange of gB between EHV-1 and EHV-4 is possible, but results in a significant attenuation of virus growth in the case of EHV-4_gB1. The generation of stable recombinant viruses is a valuable tool to address viral entry in a comparative fashion and investigate this aspect of virus replication further. Full article
(This article belongs to the Special Issue Viral Glycoprotein Incorporation)

Review

Jump to: Research

Open AccessReview Incorporation of Spike and Membrane Glycoproteins into Coronavirus Virions
Viruses 2015, 7(4), 1700-1725; doi:10.3390/v7041700
Received: 25 November 2014 / Revised: 23 March 2015 / Accepted: 24 March 2015 / Published: 3 April 2015
Cited by 3 | PDF Full-text (863 KB) | HTML Full-text | XML Full-text
Abstract
The envelopes of coronaviruses (CoVs) contain primarily three proteins; the two major glycoproteins spike (S) and membrane (M), and envelope (E), a non-glycosylated protein. Unlike other enveloped viruses, CoVs bud and assemble at the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC). For efficient virion
[...] Read more.
The envelopes of coronaviruses (CoVs) contain primarily three proteins; the two major glycoproteins spike (S) and membrane (M), and envelope (E), a non-glycosylated protein. Unlike other enveloped viruses, CoVs bud and assemble at the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC). For efficient virion assembly, these proteins must be targeted to the budding site and to interact with each other or the ribonucleoprotein. Thus, the efficient incorporation of viral envelope proteins into CoV virions depends on protein trafficking and protein–protein interactions near the ERGIC. The goal of this review is to summarize recent findings on the mechanism of incorporation of the M and S glycoproteins into the CoV virion, focusing on protein trafficking and protein–protein interactions. Full article
(This article belongs to the Special Issue Viral Glycoprotein Incorporation)
Open AccessReview Paramyxovirus Glycoprotein Incorporation, Assembly and Budding: A Three Way Dance for Infectious Particle Production
Viruses 2014, 6(8), 3019-3054; doi:10.3390/v6083019
Received: 27 June 2014 / Revised: 24 July 2014 / Accepted: 25 July 2014 / Published: 7 August 2014
Cited by 9 | PDF Full-text (1462 KB) | HTML Full-text | XML Full-text
Abstract
Paramyxoviruses are a family of negative sense RNA viruses whose members cause serious diseases in humans, such as measles virus, mumps virus and respiratory syncytial virus; and in animals, such as Newcastle disease virus and rinderpest virus. Paramyxovirus particles form by assembly of
[...] Read more.
Paramyxoviruses are a family of negative sense RNA viruses whose members cause serious diseases in humans, such as measles virus, mumps virus and respiratory syncytial virus; and in animals, such as Newcastle disease virus and rinderpest virus. Paramyxovirus particles form by assembly of the viral matrix protein, the ribonucleoprotein complex and the surface glycoproteins at the plasma membrane of infected cells and subsequent viral budding. Two major glycoproteins expressed on the viral envelope, the attachment protein and the fusion protein, promote attachment of the virus to host cells and subsequent virus-cell membrane fusion. Incorporation of the surface glycoproteins into infectious progeny particles requires coordinated interplay between the three viral structural components, driven primarily by the matrix protein. In this review, we discuss recent progress in understanding the contributions of the matrix protein and glycoproteins in driving paramyxovirus assembly and budding while focusing on the viral protein interactions underlying this process and the intracellular trafficking pathways for targeting viral components to assembly sites. Differences in the mechanisms of particle production among the different family members will be highlighted throughout. Full article
(This article belongs to the Special Issue Viral Glycoprotein Incorporation)
Figures

Open AccessReview Incorporation of Hepatitis C Virus E1 and E2 Glycoproteins: The Keystones on a Peculiar Virion
Viruses 2014, 6(3), 1149-1187; doi:10.3390/v6031149
Received: 18 December 2013 / Revised: 21 February 2014 / Accepted: 27 February 2014 / Published: 11 March 2014
Cited by 18 | PDF Full-text (1881 KB) | HTML Full-text | XML Full-text
Abstract
Hepatitis C virus (HCV) encodes two envelope glycoproteins, E1 and E2. Their structure and mode of fusion remain unknown, and so does the virion architecture. The organization of the HCV envelope shell in particular is subject to discussion as it incorporates or associates
[...] Read more.
Hepatitis C virus (HCV) encodes two envelope glycoproteins, E1 and E2. Their structure and mode of fusion remain unknown, and so does the virion architecture. The organization of the HCV envelope shell in particular is subject to discussion as it incorporates or associates with host-derived lipoproteins, to an extent that the biophysical properties of the virion resemble more very-low-density lipoproteins than of any virus known so far. The recent development of novel cell culture systems for HCV has provided new insights on the assembly of this atypical viral particle. Hence, the extensive E1E2 characterization accomplished for the last two decades in heterologous expression systems can now be brought into the context of a productive HCV infection. This review describes the biogenesis and maturation of HCV envelope glycoproteins, as well as the interplay between viral and host factors required for their incorporation in the viral envelope, in a way that allows efficient entry into target cells and evasion of the host immune response. Full article
(This article belongs to the Special Issue Viral Glycoprotein Incorporation)
Open AccessReview Understanding the Process of Envelope Glycoprotein Incorporation into Virions in Simian and Feline Immunodeficiency Viruses
Viruses 2014, 6(1), 264-283; doi:10.3390/v6010264
Received: 4 November 2013 / Revised: 1 January 2014 / Accepted: 6 January 2014 / Published: 16 January 2014
Cited by 4 | PDF Full-text (388 KB) | HTML Full-text | XML Full-text
Abstract
The lentiviral envelope glycoproteins (Env) mediate virus entry by interacting with specific receptors present at the cell surface, thereby determining viral tropism and pathogenesis. Therefore, Env incorporation into the virions formed by assembly of the viral Gag polyprotein at the plasma membrane of
[...] Read more.
The lentiviral envelope glycoproteins (Env) mediate virus entry by interacting with specific receptors present at the cell surface, thereby determining viral tropism and pathogenesis. Therefore, Env incorporation into the virions formed by assembly of the viral Gag polyprotein at the plasma membrane of the infected cells is a key step in the replication cycle of lentiviruses. Besides being useful models of human immunodeficiency virus (HIV) infections in humans and valuable tools for developing AIDS therapies and vaccines, simian and feline immunodeficiency viruses (SIV and FIV, respectively) are relevant animal retroviruses; the study of which provides important information on how lentiviral replication strategies have evolved. In this review, we discuss the molecular mechanisms underlying the incorporation of the SIV and FIV Env glycoproteins into viral particles. Full article
(This article belongs to the Special Issue Viral Glycoprotein Incorporation)
Open AccessReview Structural and Functional Comparisons of Retroviral Envelope Protein C-Terminal Domains: Still Much to Learn
Viruses 2014, 6(1), 284-300; doi:10.3390/v6010284
Received: 31 October 2013 / Accepted: 6 January 2014 / Published: 16 January 2014
PDF Full-text (363 KB) | HTML Full-text | XML Full-text
Abstract
Retroviruses are a family of viruses that cause a broad range of pathologies in animals and humans, from the apparently harmless, long-term genomic insertion of endogenous retroviruses, to tumors induced by the oncogenic retroviruses and acquired immunodeficiency syndrome (AIDS) resulting from human immunodeficiency
[...] Read more.
Retroviruses are a family of viruses that cause a broad range of pathologies in animals and humans, from the apparently harmless, long-term genomic insertion of endogenous retroviruses, to tumors induced by the oncogenic retroviruses and acquired immunodeficiency syndrome (AIDS) resulting from human immunodeficiency virus infection. Disease can be the result of diverse mechanisms, including tumorigenesis induced by viral oncogenes or immune destruction, leading to the gradual loss of CD4 T-cells. Of the virally encoded proteins common to all retroviruses, the envelope (Env) displays perhaps the most diverse functionality. Env is primarily responsible for binding the cellular receptor and for effecting the fusion process, with these functions mediated by protein domains localized to the exterior of the virus. The remaining C-terminal domain may have the most variable functionality of all retroviral proteins. The C-terminal domains from three prototypical retroviruses are discussed, focusing on the different structures and functions, which include fusion activation, tumorigenesis and viral assembly and lifecycle influences. Despite these genetic and functional differences, however, the C-terminal domains of these viruses share a common feature in the modulation of Env ectodomain conformation. Despite their differences, perhaps each system still has information to share with the others. Full article
(This article belongs to the Special Issue Viral Glycoprotein Incorporation)

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