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Pathogens
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Advances in Important Mammalian Viruses: Infection, Pathogenesis and Drugs
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Advances in Important Mammalian Viruses: Infection, Pathogenesis and Drugs

A special issue of Pathogens (ISSN 2076-0817). This special issue belongs to the section "Viral Pathogens".

Deadline for manuscript submissions: closed (30 January 2024) | Viewed by 5247

Special Issue Editor

Prof. Dr. Guihong Zhang

E-Mail Website
Guest Editor
College of Veterinary Medicine, South China Agricultural University, Guangzhou, China
Interests: epidemiology; virus pathogenesis; farm biosecurity

Special Issue Information

Dear Colleagues,

Some of the important viruses in mammalian animals threaten the development of the economy and industry in many aspects.  Although genetically related to other common viruses, those important viruses consist of unique characteristics in the process of infection, showing them out from the vast majority of viruses. However, insights into detailed infection, reproduction, and transmission pathways of the viruses, usually provide specific cell receptors and molecule targets for more powerful vaccination and antiviral medication, that leads to better control and prevention for these important mammalian viruses. Researches on the infection process, pathogenesis, and antiviral drugs of these viruses are suitable for this special issue.

Prof. Dr. Guihong Zhang
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 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. Pathogens 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 2700 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

  • virus pathogenesis
  • antiviral medication
  • infection immunology
  • infection pathology
  • antiviral drugs

Published Papers (3 papers)

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Research

18 pages, 7861 KiB  
Article
Molecular Structural Analysis of Porcine CMAH–Native Ligand Complex and High Throughput Virtual Screening to Identify Novel Inhibitors
by Oluwamayowa Joshua Ogun, Georg Thaller and Doreen Becker
Pathogens 2023, 12(5), 684; https://doi.org/10.3390/pathogens12050684 - 5 May 2023
Viewed by 1582
Abstract
Porcine meat is the most consumed red meat worldwide. Pigs are also vital tools in biological and medical research. However, xenoreactivity between porcine’s N-glycolylneuraminic acid (Neu5Gc) and human anti-Neu5Gc antibodies poses a significant challenge. On the one hand, dietary Neu5Gc intake has been [...] Read more.
Porcine meat is the most consumed red meat worldwide. Pigs are also vital tools in biological and medical research. However, xenoreactivity between porcine’s N-glycolylneuraminic acid (Neu5Gc) and human anti-Neu5Gc antibodies poses a significant challenge. On the one hand, dietary Neu5Gc intake has been connected to particular human disorders. On the other hand, some pathogens connected to pig diseases have a preference for Neu5Gc. The Cytidine monophospho-N-acetylneuraminic acid hydroxylase (CMAH) catalyses the conversion of N-acetylneuraminic acid (Neu5Ac) to Neu5Gc. In this study, we predicted the tertiary structure of CMAH, performed molecular docking, and analysed the protein–native ligand complex. We performed a virtual screening from a drug library of 5M compounds and selected the two top inhibitors with Vina scores of −9.9 kcal/mol for inhibitor 1 and −9.4 kcal/mol for inhibitor 2. We further analysed their pharmacokinetic and pharmacophoric properties. We conducted stability analyses of the complexes with molecular dynamic simulations of 200 ns and binding free energy calculations. The overall analyses revealed the inhibitors’ stable binding, which was further validated by the MMGBSA studies. In conclusion, this result may pave the way for future studies to determine how to inhibit CMAH activities. Further in vitro studies can provide in-depth insight into these compounds’ therapeutic potential. Full article
(This article belongs to the Special Issue Advances in Important Mammalian Viruses: Infection, Pathogenesis and Drugs)
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17 pages, 2704 KiB  
Article
An In Silico Functional Analysis of Non-Synonymous Single-Nucleotide Polymorphisms of Bovine CMAH Gene and Potential Implication in Pathogenesis
by Oluwamayowa Joshua Ogun, Opeyemi S. Soremekun, Georg Thaller and Doreen Becker
Pathogens 2023, 12(4), 591; https://doi.org/10.3390/pathogens12040591 - 13 Apr 2023
Cited by 2 | Viewed by 1746
Abstract
The sugar molecule N-glycolylneuraminic acid (Neu5Gc) is one of the most common sialic acids discovered in mammals. Cytidine monophospho-N-acetylneuraminic acid hydroxylase (CMAH) catalyses the conversion of N-acetylneuraminic acid (Neu5Ac) to Neu5Gc, and it is encoded by the CMAH gene. On the one hand, [...] Read more.
The sugar molecule N-glycolylneuraminic acid (Neu5Gc) is one of the most common sialic acids discovered in mammals. Cytidine monophospho-N-acetylneuraminic acid hydroxylase (CMAH) catalyses the conversion of N-acetylneuraminic acid (Neu5Ac) to Neu5Gc, and it is encoded by the CMAH gene. On the one hand, food metabolic incorporation of Neu5Gc has been linked to specific human diseases. On the other hand, Neu5Gc has been shown to be highly preferred by some pathogens linked to certain bovine diseases. We used various computational techniques to perform an in silico functional analysis of five non-synonymous single-nucleotide polymorphisms (nsSNPs) of the bovine CMAH (bCMAH) gene identified from the 1000 Bull Genomes sequence data. The c.1271C>T (P424L) nsSNP was predicted to be pathogenic based on the consensus result from different computational tools. The nsSNP was also predicted to be critical based on sequence conservation, stability, and post-translational modification site analysis. According to the molecular dynamic simulation and stability analysis, all variations promoted stability of the bCMAH protein, but mutation A210S significantly promoted CMAH stability. In conclusion, c.1271C>T (P424L) is expected to be the most harmful nsSNP among the five detected nsSNPs based on the overall studies. This research could pave the way for more research associating pathogenic nsSNPs in the bCMAH gene with diseases. Full article
(This article belongs to the Special Issue Advances in Important Mammalian Viruses: Infection, Pathogenesis and Drugs)
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12 pages, 2897 KiB  
Article
HSP27 Interacts with Nonstructural Proteins of Porcine Reproductive and Respiratory Syndrome Virus and Promotes Viral Replication
by Chunhui Song, Hanze Liu, Zhi Cao, Hu Shan and Qiaoya Zhang
Pathogens 2023, 12(1), 91; https://doi.org/10.3390/pathogens12010091 - 5 Jan 2023
Cited by 1 | Viewed by 1377
Abstract
Heat shock protein 27 (HSP27) is a multifunctional protein and belongs to the small HSP family. It has been shown that HSP27 is involved in viral replication as a cellular chaperone, but the function of HSP27 during porcine reproductive and respiratory syndrome virus [...] Read more.
Heat shock protein 27 (HSP27) is a multifunctional protein and belongs to the small HSP family. It has been shown that HSP27 is involved in viral replication as a cellular chaperone, but the function of HSP27 during porcine reproductive and respiratory syndrome virus (PRRSV) infections remains unexplored. Here, we found that PRRSV replication can induce HSP27 expression and phosphorylation in vitro. HSP27 overexpression promoted PRRSV replication, whereas its knockdown reduced PRRSV proliferation. Additionally, suppressing HSP27 phosphorylation reduced PRRSV replication and the level of viral double-stranded RNA (dsRNA), a marker of the viral replication and transcription complexes (RTCs). Furthermore, HSP27 can interact with multiple viral nonstructural proteins (nsps), including nsp1α, nsp1β, nsp5, nsp9, nsp11 and nsp12. Suppressing the phosphorylation of HSP27 almost completely disrupted its interaction with nsp1β and nsp12. Altogether, our study revealed that HSP27 plays an important role in PRRSV replication. Full article
(This article belongs to the Special Issue Advances in Important Mammalian Viruses: Infection, Pathogenesis and Drugs)
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