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Viruses
Special Issues
Synthesis, Assembly and Processing of Viral Proteins
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Synthesis, Assembly and Processing of Viral Proteins

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

Deadline for manuscript submissions: closed (1 July 2023) | Viewed by 11851

Special Issue Editors

Dr. Sheng-Fan Wang

E-Mail Website
Guest Editor
Department of Medical Laboratory Science and Biotechnology, Kaohsiung Medical University, Kaohsiung 80708, Taiwan
Interests: virology; immunology; viral pathogenesis; emerging diseases; re-emerging disease; influenza virus; dengue virus; HIV-1
Special Issues, Collections and Topics in MDPI journals
Dr. Wen-Hung Wang

E-Mail Website
Guest Editor
Division of Infectious Disease, Department of Internal Medicine, Kaohsiung Medical, University Hospital, Kaohsiung Medical University, Kaohsiung 80708, Taiwan
Interests: virology; immunology; tropical medicine; virus–host interaction
Special Issues, Collections and Topics in MDPI journals
Dr. Arunee Thitithanyanont

E-Mail Website
Guest Editor
Department of Microbiology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand
Interests: molecular epidemiology; evolution; avian influenza; pathogenicity; drug screening
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Viruses are obligate parasites equipped with minimal tools in order to replicate themselves within the cells. They circumvent and appropriate every possible resource available to them from the host.

Viral replication is varied and depends on the type of genes involved. Most DNA viruses assemble in the nucleus, whereas most RNA viruses develop solely in the cytoplasm. During viral replication, several viral proteins are synthesized and processed. Some of these proteins hijack the machinery and metabolism of a host cell to produce multiple copies of viruses and further assist viral assembly and budding. In addition, some of the viral proteins have interactions with host factors to evade host cellular or immune defense or enhance virus propagation. Accordingly, understanding the mechanism and process of these viral proteins is essential for control and therapeutic application toward virus disease.  

In this Special Issue, we aim to assemble a collection of short-report, communication, research, and review articles that highlight critical advancements in our understanding of the synthesis, assembly and processing of viral proteins and interactions between these protein and host factors. We look forward to your submissions.

Dr. Sheng-Fan Wang
Dr. Wen-Hung Wang
Dr. Arunee Thitithanyanont
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

  • synthesis
  • assembly
  • processing
  • viral protein
  • host factor
  • DNA virus
  • RNA virus

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Published Papers (5 papers)

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Editorial

Jump to: Research

2 pages, 172 KiB  
Editorial
Synthesis, Assembly and Processing of Viral Proteins
by Wen-Hung Wang, Arunee Thitithanyanont and Sheng-Fan Wang
Viruses 2022, 14(8), 1650; https://doi.org/10.3390/v14081650 - 27 Jul 2022
Cited by 2 | Viewed by 1663
Abstract
The papers published in this Special Issue include various essential steps and regulatory mechanisms involved in viral protein synthesis, protein processing, glycosylation, and assembly [...] Full article
(This article belongs to the Special Issue Synthesis, Assembly and Processing of Viral Proteins)
6 pages, 1028 KiB  
Editorial
Virus Hijacks Host Proteins and Machinery for Assembly and Budding, with HIV-1 as an Example
by Chih-Yen Lin, Aspiro Nayim Urbina, Wen-Hung Wang, Arunee Thitithanyanont and Sheng-Fan Wang
Viruses 2022, 14(7), 1528; https://doi.org/10.3390/v14071528 - 13 Jul 2022
Cited by 6 | Viewed by 2566
Abstract
Viral assembly and budding are the final steps and key determinants of the virus life cycle and are regulated by virus–host interaction. Several viruses are known to use their late assembly (L) domains to hijack host machinery and cellular adaptors to be used [...] Read more.
Viral assembly and budding are the final steps and key determinants of the virus life cycle and are regulated by virus–host interaction. Several viruses are known to use their late assembly (L) domains to hijack host machinery and cellular adaptors to be used for the requirement of virus replication. The L domains are highly conserved short sequences whose mutation or deletion may lead to the accumulation of immature virions at the plasma membrane. The L domains were firstly identified within retroviral Gag polyprotein and later detected in structural proteins of many other enveloped RNA viruses. Here, we used HIV-1 as an example to describe how the HIV-1 virus hijacks ESCRT membrane fission machinery to facilitate virion assembly and release. We also introduce galectin-3, a chimera type of the galectin family that is up-regulated by HIV-1 during infection and further used to promote HIV-1 assembly and budding via the stabilization of Alix–Gag interaction. It is worth further dissecting the details and finetuning the regulatory mechanism, as well as identifying novel candidates involved in this final step of replication cycle. Full article
(This article belongs to the Special Issue Synthesis, Assembly and Processing of Viral Proteins)
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Research

Jump to: Editorial

15 pages, 7118 KiB  
Article
Development of Fluorescence-Tagged SARS-CoV-2 Virus-like Particles by a Tri-Cistronic Vector Expression System for Investigating the Cellular Entry of SARS-CoV-2
by Young-Sheng Chang, Li-Wei Chu, Zan-Yu Chen, Joh-Sin Wu, Wen-Chi Su, Chia-Jui Yang, Yueh-Hsin Ping and Cheng-Wen Lin
Viruses 2022, 14(12), 2825; https://doi.org/10.3390/v14122825 - 19 Dec 2022
Cited by 9 | Viewed by 2776
Abstract
Severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) has caused the pandemic that began late December 2019. The co-expression of SARS-CoV-2 structural proteins in cells could assemble into several types of virus-like particles (VLPs) without a viral RNA genome. VLPs containing S proteins with the [...] Read more.
Severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) has caused the pandemic that began late December 2019. The co-expression of SARS-CoV-2 structural proteins in cells could assemble into several types of virus-like particles (VLPs) without a viral RNA genome. VLPs containing S proteins with the structural and functional properties of authentic virions are safe materials to exploit for virus-cell entry and vaccine development. In this study, to generate SARS-CoV-2 VLPs (SCoV2-SEM VLPs) composed of three structural proteins including spike (S), envelop (E) protein and membrane (M) protein, a tri-cistronic vector expression system was established in a cell line co-expressing SARS-CoV-2 S, E and M proteins. The SCoV2-SEM VLPs were harvested from the cultured medium, and three structure proteins were confirmed by Western blot assay. A negative-stain TEM assay demonstrated the size of the SCoV2-SEM VLPs with a diameter of about 90 nm. To further characterize the infectious properties of SCoV2-SEM VLPs, the VLPs (atto647N-SCoV2-SEM VLPs) were fluorescence-labeled by conjugation with atto-647N and visualized under confocal microscopy at a single-particle resolution. The results of the infection assay revealed that atto647N-SCoV2-SEM VLPs attached to the surface of the HEK293T cells at the pre-binding phase in a ACE2-dependent manner. At the post-infection phase, atto647N-SCoV2-SEM VLPs either fused with the cellular membrane or internalized into the cytoplasm with mCherry-rab5-positive early endosomes. Moreover, fusion with the cellular membrane and the internalization with early endosomes could be inhibited by the treatment of camostat (a pharmacological inhibitor of TMPRSS2) and chlorpromazine (an endocytosis inhibitor), respectively. These results elucidated that SCoV2-SEM VLPs behave similarly to the authentic live SARS-CoV-2 virus, suggesting that the development of SCoV2-SEM VLPs provide a realistic and safe experimental model for studying the infectious mechanism of SARS-CoV-2. Full article
(This article belongs to the Special Issue Synthesis, Assembly and Processing of Viral Proteins)
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14 pages, 2585 KiB  
Article
Simultaneous Production of a Virus-Like Particle Linked to dsRNA to Enhance dsRNA Delivery for Yellow Head Virus Inhibition
by Jaruwan Worawittayatada, Kitipong Angsujinda, Rapee Sinnuengnong, Pongsopee Attasart, Duncan R. Smith and Wanchai Assavalapsakul
Viruses 2022, 14(12), 2594; https://doi.org/10.3390/v14122594 - 22 Nov 2022
Cited by 2 | Viewed by 2026
Abstract
A co-expressed Penaeus stylirostris densovirus (PstDNV) capsid and dsRNA specific to the yellow head virus (YHV) protease (CoEx cpPstDNV/dspro) has been shown to suppress YHV replication in the Pacific white-legged shrimp (Litopenaeus vannamei). However, maintaining [...] Read more.
A co-expressed Penaeus stylirostris densovirus (PstDNV) capsid and dsRNA specific to the yellow head virus (YHV) protease (CoEx cpPstDNV/dspro) has been shown to suppress YHV replication in the Pacific white-legged shrimp (Litopenaeus vannamei). However, maintaining two plasmids in a single bacterial cell is not desirable; therefore, a single plasmid harboring both the PstDNV capsid and the dsRNA-YHV-pro gene was constructed under the regulation of a single T7 promoter, designated pET28a-Linked cpPstDNV-dspro. Following induction, this novel construct expressed an approximately 37-kDa recombinant protein associated with a roughly 400-bp dsRNA (Linked cpPstDNV-dspro). Under a transmission electron microscope, the virus-like particles (VLP; Linked PstDNV VLPs-dspro) obtained were seen to be monodispersed, similar to the native PstDNV virion. A nuclease digestion assay indicated dsRNA molecules were both encapsulated and present outside the Linked PstDNV VLPs-dspro. In addition, the amount of dsRNA produced from this strategy was higher than that obtained with a co-expression strategy. In a YHV infection challenge, the Linked PstDNV VLPs-dspro was more effective in delaying and reducing mortality than other constructs tested. Lastly, the linked construct provides protection for the dsRNA cargo from nucleolytic enzymes present in the shrimp hemolymph. This is the first report of a VLP carrying virus-inhibiting dsRNA that could be produced without disassembly and reassembly to control virus infection in shrimp. Full article
(This article belongs to the Special Issue Synthesis, Assembly and Processing of Viral Proteins)
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20 pages, 5262 KiB  
Article
Bovine Herpesvirus-1 Glycoprotein M Mediates the Translocation to the Golgi Apparatus and Packaging of VP8
by Soumya Sucharita, Suresh Tikoo and Sylvia van Drunen Littel-van den Hurk
Viruses 2022, 14(9), 1985; https://doi.org/10.3390/v14091985 - 8 Sep 2022
Cited by 4 | Viewed by 1746
Abstract
VP8, the most abundant tegument protein of bovine herpesvirus-1 (BoHV-1), plays an important role in viral replication. According to our previous studies, VP8 localizes to the Golgi apparatus of BoHV-1-infected cells where it can be packaged into the virus; however, Golgi localization of [...] Read more.
VP8, the most abundant tegument protein of bovine herpesvirus-1 (BoHV-1), plays an important role in viral replication. According to our previous studies, VP8 localizes to the Golgi apparatus of BoHV-1-infected cells where it can be packaged into the virus; however, Golgi localization of VP8 does not occur outside of the context of infection. The goal of this study was to identify the viral factor(s) involved in the tropism of VP8 towards the Golgi. VP8 was found to interact with glycoprotein M (gM), and the VP8 and gM domains that are essential for this interaction were identified. VP8 and gM colocalized to the Golgi apparatus in BoHV-1-infected cells. In cells co-transfected with VP8- and gM-encoding plasmids, VP8 was also found to be localized to the Golgi, suggesting gM to be sufficient. The localization of VP8 to the Golgi was lost in cells infected with a gM deletion mutant, and the amount of VP8 incorporated into mature virus was significantly reduced. However, with the restoration of gM in a revertant virus, the localization to the Golgi and the amount of VP8 incorporated in the virions were restored. These results indicate that gM plays a critical role in VP8 subcellular localization to the Golgi and packaging into mature virions. Full article
(This article belongs to the Special Issue Synthesis, Assembly and Processing of Viral Proteins)
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