Assembly of RNA Viruses

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

Deadline for manuscript submissions: closed (31 October 2024) | Viewed by 7127

Special Issue Editor


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Guest Editor
AIDS Research Center, National Institute of Infectious Diseases, Tokyo, Japan
Interests: retroviruses; HIV-1; entry; assembly; gag; capsid; anti-HIV-1 compounds; mechanism of action

Special Issue Information

Dear Colleagues,

Many emerging/re-emerging infectious diseases are caused by RNA viruses able to adapt to a rapidly changing globalized world, also capable of altering their structures and biological phenotypes quickly due to the high error rate of their RNA polymerases. Thus, obtaining new information on the assembly of RNA viruses is not only important for a deeper fundamental understanding of the viruses, but also crucial for tackling new viruses generated through mutation, reassortment, and recombination.

In this Special Issue, we welcome a wide range of articles, including original research, short communications, and reviews, focusing on the virus assembly of RNA viruses. Topics of interest include the assembly of viral structural proteins, selective packaging of genomic RNAs, acquisition of viral envelope glycoproteins, release/maturation of virus particles, host factors involved in virus assembly, antiviral compounds targeting the assembly process, new methodologies for elucidating virus assembly, etc.

We look forward to receiving your submissions for this Special Issue.

Dr. Tsutomu Murakami
Guest Editor

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Keywords

  • RNA viruses
  • assembly
  • genome packaging
  • envelope incorporation
  • release
  • maturation
  • host factors
  • antivirals

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Published Papers (3 papers)

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Research

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19 pages, 3263 KiB  
Article
Human Mannose Receptor 1 Attenuates HIV-1 Infectivity in a Virus Isolate-Specific Manner
by Hideki Saito, Sayaka Sukegawa, Sandra Kao and Klaus Strebel
Viruses 2023, 15(10), 2057; https://doi.org/10.3390/v15102057 - 6 Oct 2023
Cited by 1 | Viewed by 1839
Abstract
Human mannose receptor 1 (hMRC1) is a transmembrane glycoprotein that belongs to the C-type lectin family and is expressed on the surface of most tissue macrophages. hMRC1 contributes to the binding and transmission of HIV-1 and is involved in the endocytic uptake of [...] Read more.
Human mannose receptor 1 (hMRC1) is a transmembrane glycoprotein that belongs to the C-type lectin family and is expressed on the surface of most tissue macrophages. hMRC1 contributes to the binding and transmission of HIV-1 and is involved in the endocytic uptake of HIV-1 for subsequent antigen presentation. We previously reported that hMRC1 functions as an antiviral factor by inhibiting virus release through a BST-2-like mechanism. The inhibition of virus release was not virus isolate-specific and, surprisingly, was not Env-dependent. We now report on another hMRC1 antiviral function that affects the infectivity of viral particles. Unlike its effect on virus release, the inhibition of viral infectivity by hMRC1 was virus isolate-specific. An analysis of chimeric Env revealed that the Env V3 region was a critical determinant for the inhibitory effect of hMRC1. Of note, exogenously expressed hMRC1 was packaged into viral particles in an Env-independent manner. Co-immunoprecipitation studies revealed a strong interaction of the hMRC1-sensitive NL43 Env with hMRC1, while the hMRC1-insensitive Envs of AD8 and 49.5 isolates interacted poorly if at all with hMRC1. An analysis of a panel of Transmitted/Founder (T/F) viruses revealed that all of them were R5-tropic, and more than half of them were inhibited by hMRC1. The detailed mechanism of how hMRC1 inhibits viral infectivity remains to be investigated. However, the high-affinity binding of hMRC1 to Env may cause a conformational change around the Env V3 region or obstruct the Env V3 region and may make it inaccessible for subsequent interaction with the coreceptor during virus entry. Full article
(This article belongs to the Special Issue Assembly of RNA Viruses)
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10 pages, 1488 KiB  
Article
Development of Parallel Reaction Monitoring Mass Spectrometry Assay for the Detection of Human Norovirus Major Capsid Protein
by Yayoi Kimura, Jihye Shin, Yusuke Nakai, Masaya Takahashi, Yoko Ino, Tomoko Akiyama, Keiko Goto, Noriko Nagata, Yutaro Yamaoka, Kei Miyakawa, Hirokazu Kimura and Akihide Ryo
Viruses 2022, 14(7), 1416; https://doi.org/10.3390/v14071416 - 28 Jun 2022
Cited by 1 | Viewed by 2313
Abstract
Human Norwalk viruses (HuNoVs), the most common etiological agents of acute gastroenteritis, are genetically diverse RNA viruses that frequently cause mass food poisoning internationally. Although nucleic acid detection methods, such as reverse transcription–quantitative polymerase chain reaction (RT-qPCR), are the gold standard for the [...] Read more.
Human Norwalk viruses (HuNoVs), the most common etiological agents of acute gastroenteritis, are genetically diverse RNA viruses that frequently cause mass food poisoning internationally. Although nucleic acid detection methods, such as reverse transcription–quantitative polymerase chain reaction (RT-qPCR), are the gold standard for the diagnosis of norovirus infection, alternative methods are needed for the specific and sensitive viral protein detection for rapid diagnosis and surveillance. In this study, we developed a robust and high-throughput targeted proteomic assay workflow to directly detect the VP1 major capsid protein of HuNoVs. A parallel reaction monitoring (PRM) assay using a high-resolution mass spectrometer was used to detect representative peptides derived from VP1 in six different HuNoV genotypes. An optimized protocol using synthesized heavy isotope-labeled peptides as internal standards was also used to simultaneously genotype and quantify the VP1 protein in human stool specimens. This method is expected to become a new tool for studying the molecular epidemiology of HuNoV and to shed new light on targeted proteomics in clinical practice. Full article
(This article belongs to the Special Issue Assembly of RNA Viruses)
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Review

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12 pages, 1939 KiB  
Review
Cellular Release of Infectious Hepatitis C Virus Particles via Endosomal Pathways
by Lin Deng, Muchamad Ridotu Solichin, Dewa Nyoman Murti Adyaksa, Maria Alethea Septianastiti, Rhamadianti Aulia Fitri, Gede Ngurah Rsi Suwardan, Chieko Matsui, Takayuki Abe and Ikuo Shoji
Viruses 2023, 15(12), 2430; https://doi.org/10.3390/v15122430 - 14 Dec 2023
Viewed by 1903
Abstract
Hepatitis C virus (HCV) is a positive-sense, single-stranded RNA virus that causes chronic hepatitis, liver cirrhosis and hepatocellular carcinoma. The release of infectious HCV particles from infected hepatocytes is a crucial step in viral dissemination and disease progression. While the exact mechanisms of [...] Read more.
Hepatitis C virus (HCV) is a positive-sense, single-stranded RNA virus that causes chronic hepatitis, liver cirrhosis and hepatocellular carcinoma. The release of infectious HCV particles from infected hepatocytes is a crucial step in viral dissemination and disease progression. While the exact mechanisms of HCV particle release remain poorly understood, emerging evidence suggests that HCV utilizes intracellular membrane trafficking and secretory pathways. These pathways include the Golgi secretory pathway and the endosomal trafficking pathways, such as the recycling endosome pathway and the endosomal sorting complex required for transport (ESCRT)-dependent multivesicular bodies (MVBs) pathway. This review provides an overview of recent advances in understanding the release of infectious HCV particles, with a particular focus on the involvement of the host cell factors that participate in HCV particle release. By summarizing the current knowledge in this area, this review aims to contribute to a better understanding of endosomal pathways involved in the extracellular release of HCV particles and the development of novel antiviral strategies. Full article
(This article belongs to the Special Issue Assembly of RNA Viruses)
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