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Special Issue "Human Picornaviruses"

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

Deadline for manuscript submissions: 30 September 2019.

Special Issue Editor

Guest Editor
Dr. Petri Susi

Institute of Biomedicine, University of Turku, Turku, Finland
Website | E-Mail
Interests: enterovirus, rhinovirus, parechovirus, bioprocess, cell culture techniques, virus evolution, clinical virology, diagnostics, oncolytic virotherapy, antibody technologies

Special Issue Information

Dear Colleagues,

Over the past two decades, we have witnessed a revolution in molecular techniques that have enabled unprecedented molecular diagnostics, genetic analysis, and the structural determination of human picornaviruses. Consequently, the number of novel and genome-sequenced picornavirus types and high-resolution picornavirus structures has increased tremendously over the years. At the same time, we have also witnessed uncontrolled outbreaks of emerging pathogenic picornaviruses that have attracted media attention and public concern. The grand challenge in picornavirus research is whether we can employ the current technologies and information to improve surveillance, predict epidemics, understand picornavirus life cycle and pathogenicity, and develop effective countermeasures against these ever-increasing viruses.

In this Special Issue of Viruses, we aim to discuss the recent developments and breakthroughs in structural determination, viral genome sequencing, epidemiology, evolution, diagnostics, and pathogenesis, receptor tropism and cellular life cycles, immunology, and therapy including the progress in the development of therapeutic antibodies and vaccines. I cordially invite you to contribute your most recent research findings and/or insights into this topic. We welcome reviews and original research articles including technical aspects.

Dr. Petri Susi
Guest Editor

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 papers will be 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 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

  • enterovirus
  • picornaviral epidemiology
  • viral diagnostics
  • viral evolution
  • parechovirus
  • pathogenesis
  • receptor
  • recombination
  • rhinovirus
  • genome sequencing
  • structure

Published Papers (4 papers)

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Research

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Open AccessArticle
Recombinant Strains of Human Parechovirus in Rural Areas in the North of Brazil
Viruses 2019, 11(6), 488; https://doi.org/10.3390/v11060488
Received: 7 April 2019 / Revised: 30 April 2019 / Accepted: 3 May 2019 / Published: 29 May 2019
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Abstract
We characterized the 24 nearly full-length genomes of human parechoviruses (PeV) from children in the north of Brazil. The initial phylogenetic analysis indicated that 17 strains belonged to genotype 1, 5 to genotype 4, and 1 to genotype 17. A more detailed analysis [...] Read more.
We characterized the 24 nearly full-length genomes of human parechoviruses (PeV) from children in the north of Brazil. The initial phylogenetic analysis indicated that 17 strains belonged to genotype 1, 5 to genotype 4, and 1 to genotype 17. A more detailed analysis revealed a high frequency of recombinant strains (58%): A total of 14 of our PeV-As were chimeric, with four distinct recombination patterns identified. Five strains were composed of genotypes 1 and 5 (Rec1/5); five strains shared a complex mosaic pattern formed by genotypes 4, 5, and 17 (Rec4/17/5); two strains were composed of genotypes 1 and 17 (Rec1/17); and two strains were composed of genotype 1 and an undetermined strain (Rec1/und). Coalescent analysis based on the Vp1 gene, which is free of recombination, indicated that the recombinant strains most likely arose in this region approximately 30 years ago. They are present in high frequencies and are circulating in different small and isolated cities in the state of Tocantins. Further studies will be needed to establish whether the detected recombinant strains have been replacing parental strains or if they are co-circulating in distinct frequencies in Tocantins. Full article
(This article belongs to the Special Issue Human Picornaviruses)
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Review

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Open AccessReview
Heparan Sulfate Proteoglycans and Viral Attachment: True Receptors or Adaptation Bias?
Viruses 2019, 11(7), 596; https://doi.org/10.3390/v11070596
Received: 17 June 2019 / Revised: 28 June 2019 / Accepted: 29 June 2019 / Published: 1 July 2019
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Abstract
Heparan sulfate proteoglycans (HSPG) are composed of unbranched, negatively charged heparan sulfate (HS) polysaccharides attached to a variety of cell surface or extracellular matrix proteins. Widely expressed, they mediate many biological activities, including angiogenesis, blood coagulation, developmental processes, and cell homeostasis. HSPG are [...] Read more.
Heparan sulfate proteoglycans (HSPG) are composed of unbranched, negatively charged heparan sulfate (HS) polysaccharides attached to a variety of cell surface or extracellular matrix proteins. Widely expressed, they mediate many biological activities, including angiogenesis, blood coagulation, developmental processes, and cell homeostasis. HSPG are highly sulfated and broadly used by a range of pathogens, especially viruses, to attach to the cell surface. In this review, we summarize the current knowledge on HSPG–virus interactions and distinguish viruses with established HS binding, viruses that bind HS only after intra-host or cell culture adaptation, and finally, viruses whose dependence on HS for infection is debated. We also provide an overview of the antiviral compounds designed to interfere with HS binding. Many questions remain about the true importance of these receptors in vivo, knowledge that is critical for the design of future antiviral therapies. Full article
(This article belongs to the Special Issue Human Picornaviruses)
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Open AccessReview
Biological Function and Application of Picornaviral 2B Protein: A New Target for Antiviral Drug Development
Viruses 2019, 11(6), 510; https://doi.org/10.3390/v11060510
Received: 13 May 2019 / Revised: 31 May 2019 / Accepted: 2 June 2019 / Published: 4 June 2019
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Abstract
Picornaviruses are associated with acute and chronic diseases. The clinical manifestations of infections are often mild, but infections may also lead to respiratory symptoms, gastroenteritis, myocarditis, meningitis, hepatitis, and poliomyelitis, with serious impacts on human health and economic losses in animal husbandry. Thus [...] Read more.
Picornaviruses are associated with acute and chronic diseases. The clinical manifestations of infections are often mild, but infections may also lead to respiratory symptoms, gastroenteritis, myocarditis, meningitis, hepatitis, and poliomyelitis, with serious impacts on human health and economic losses in animal husbandry. Thus far, research on picornaviruses has mainly focused on structural proteins such as VP1, whereas the non-structural protein 2B, which plays vital roles in the life cycle of the viruses and exhibits a viroporin or viroporin-like activity, has been overlooked. Viroporins are viral proteins containing at least one amphipathic α-helical structure, which oligomerizes to form transmembrane hydrophilic pores. In this review, we mainly summarize recent research data on the viroporin or viroporin-like activity of 2B proteins, which affects the biological function of the membrane, regulates cell death, and affects the host immune response. Considering these mechanisms, the potential application of the 2B protein as a candidate target for antiviral drug development is discussed, along with research challenges and prospects toward realizing a novel treatment strategy for picornavirus infections. Full article
(This article belongs to the Special Issue Human Picornaviruses)
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Other

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Open AccessBrief Report
Coxsackievirus-B4 Infection of Human Primary Pancreatic Ductal Cell Cultures Results in Impairment of Differentiation into Insulin-Producing Cells
Viruses 2019, 11(7), 597; https://doi.org/10.3390/v11070597
Received: 11 April 2019 / Revised: 11 June 2019 / Accepted: 27 June 2019 / Published: 2 July 2019
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Abstract
Coxsackievirus-B4 (CV-B4) E2 can persist in the pancreatic ductal-like cells (Panc-1 cell line), which results in an impaired differentiation of these cells into islet-like cell aggregates (ICA). In this study, primary pancreatic ductal cells obtained as a by-product of islet isolation from the [...] Read more.
Coxsackievirus-B4 (CV-B4) E2 can persist in the pancreatic ductal-like cells (Panc-1 cell line), which results in an impaired differentiation of these cells into islet-like cell aggregates (ICA). In this study, primary pancreatic ductal cells obtained as a by-product of islet isolation from the pancreas of seven brain-dead adults were inoculated with CV-B4 E2, followed-up for 29 days, and the impact was investigated. Viral titers in culture supernatants were analyzed throughout the culture. Intracellular viral RNA was detected by RT-PCR. Levels of ductal cell marker CK19 mRNA and of insulin mRNA were evaluated by qRT-PCR. The concentration of c-peptide in supernatants was determined by ELISA. Ductal cells exposed to trypsin and serum-free medium formed ICA and resulted in an increased insulin secretion. Ductal cells from five brain-dead donors were severely damaged by CV-B4 E2, whereas the virus persisted in cultures of cells obtained from the other two. The ICAs whose formation was induced on day 14 post-inoculation were scarce and appeared tiny in infected cultures. Also, insulin mRNA expression and c-peptide levels were strongly reduced compared to the controls. In conclusion, CV-B4 E2 lysed human primary pancreatic ductal cells or persisted in these cells, which resulted in the impairment of differentiation into insulin-producing cells. Full article
(This article belongs to the Special Issue Human Picornaviruses)
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