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  • 1
    Online Resource
    Online Resource
    Cham :Springer International Publishing :
    Keywords: Virology. ; Clinical biochemistry. ; Diseases Causes and theories of causation. ; Microbiology. ; Molecular biology. ; Biology Technique. ; Virology. ; Medical Biochemistry. ; Pathogenesis. ; Microbiology. ; Molecular Biology. ; Biological Techniques.
    Description / Table of Contents: Part 1: General / Technical Aspects -- Chapter 1: In Situ Imaging Of Virus Infected Cells By Cryo-Electron Tomography: An Overview -- Chapter 2: Approaches To Evaluating Necroptosis In Virus Infected Cells -- Chapter 3: Apoptosis And Phagocytosis As Antiviral Mechanisms -- Chapter 4: The Art Of Viral Membrane Fusion And Penetration -- Chapter 5: Single Particle Tracking Of Virus Entry In Live Cells -- Chapter 6: Correlative Cryo-Imaging Using Soft X-Ray Tomography For The Study Of Virus Biology In Cells And Tissues -- Chapter 7: The Virus-Induced Cytopathic Effect -- Part 2: Specific Viruses -- Chapter 8: Human Papilloma Virus-Infected Cells -- Chapter 9: Defining The Assembleome Of The Respiratory Syncytial Virus -- Chapter 10: Japanese Encephalitis Virus Infected Cells -- Chapter 11: African Swine Fever Virus Host-Pathogen Interactions -- Chapter 12: Coronavirus And The Cytoskeleton Of Virus-Infected Cells -- Chapter 13: Viral Rna Is A Hub For Critical Host-Virus Interactions -- Chapter 14: Influenza A Virus: Cellular Entry -- Chapter 15: Human Endogenous Retroviruses In Diseases -- Chapter 16: Cholesterol And M2 Rendezvous In Budding And Scission Of Influenza A Virus.
    Abstract: Virus-infected Cells is a comprehensive and technical exploration of the intricate interactions between viruses and host cells. This book delves into the molecular and cellular aspects of viral infections, providing a wealth of knowledge about various viruses and their effects on cellular mechanisms. The first part of the book covers general/technical aspects, introducing the reader to the field of virology and providing an overview of the techniques used to study virus-infected cells. It covers topics such as the visualisation of virus-infected cells by cryo-electron tomography and the assessment of necroptosis, a type of programmed cell death, in virus-infected cells. In addition, the book explores the role of apoptosis and phagocytosis as antiviral mechanisms, as well as the intricate process of viral membrane fusion and penetration. It also discusses the tracking of viral entry into living cells and the use of correlative cryo-imaging to study the biology of viruses in cells and tissues. Finally, the book examines the cytopathic effect induced by viruses, shedding light on the damage caused to infected cells. The second section of the book explores specific viruses and their interactions with host cells. Each chapter focuses on a specific virus and provides an in-depth look at its behaviour within infected cells. The book covers a wide range of viruses, including human papillomavirus, respiratory syncytial virus, Japanese encephalitis virus, African swine fever virus, coronavirus, influenza A virus and human endogenous retroviruses. Each chapter examines unique aspects of virus-host interactions, such as viral assembly, impact on the cytoskeleton, critical host-virus interactions mediated by viral RNA, mechanisms of cell entry, and the involvement of cholesterol in virus budding and scission. This volume in the Subcellular Biochemistry series is a valuable resource for researchers, virologists and students interested in understanding the complex dynamics between viruses and the cells they infect. With its detailed exploration of general and specific aspects of virus-host interactions, this book provides a comprehensive understanding of the molecular and cellular mechanisms involved in viral infections.
    Type of Medium: Online Resource
    Pages: VIII, 459 p. 70 illus., 68 illus. in color. , online resource.
    Edition: 1st ed. 2023.
    ISBN: 9783031400865
    Series Statement: Subcellular Biochemistry, 106
    DDC: 579.2
    Language: English
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  • 2
    Publication Date: 2020-06-14
    Description: Influenza A virus (IAV) and respiratory syncytial virus (RSV) are important respiratory pathogens that share common epidemiological features and cellular tropism within the respiratory tract. This gives rise to the potential for biological interactions between IAV and RSV during coinfection of hosts. Virus–virus interactions are increasingly recognised for their contribution to viral dynamics during infection, however, the molecular processes underpinning these interactions are unknown. Here, we developed an in vitro coinfection system to characterise the infection dynamics of IAV (A/Puerto Rico/8/34, H1N1) and RSV (A2) in single virus infection or coinfection in lung epithelial cells, with the aim to identify biological processes that drive virus–virus interactions during coinfection. We compared viral replication kinetics at different multiplicities of infection and observed that RSV replication was inhibited during coinfection with IAV, whilst IAV replication was facilitated by coinfection. To further characterise IAV/RSV interactions, we determined the relative proportions of single virus infected or coinfected cells during early and late timepoints post-infection and observed differences in expression of viral proteins between single and coinfected states. Additionally, cell viability was measured determine differences in viral-induced cytopathic effect. Compared with RSV infection, cell death is induced at earlier timepoints post IAV infection and coinfection, indicating that different cellular processes are initiated in response to infection. These studies highlight that both competitive and facilitative ecological interactions occur between IAV and RSV during coinfection and shed light on sources of potential interactions at the cellular and molecular level.
    Electronic ISSN: 2504-3900
    Topics: Technology
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  • 3
    Publication Date: 2017-09-15
    Description: Rift Valley fever phlebovirus (RVFV) is a clinically and economically important pathogen increasingly likely to cause widespread epidemics. RVFV virulence depends on the interferon antagonist non-structural protein (NSs), which remains poorly characterized. We identified a stable core domain of RVFV NSs (residues 83–248), and solved its crystal structure, a novel all-helical fold organized into highly ordered fibrils. A hallmark of RVFV pathology is NSs filament formation in infected cell nuclei. Recombinant virus encoding the NSs core domain induced intranuclear filaments, suggesting it contains all essential determinants for nuclear translocation and filament formation. Mutations of key crystal fibril interface residues in viruses encoding full-length NSs completely abrogated intranuclear filament formation in infected cells. We propose the fibrillar arrangement of the NSs core domain in crystals reveals the molecular basis of assembly of this key virulence factor in cell nuclei. Our findings have important implications for fundamental understanding of RVFV virulence.
    Electronic ISSN: 2050-084X
    Topics: Biology , Medicine , Natural Sciences in General
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  • 4
    Publication Date: 2019-02-03
    Description: The primary envelopment/de-envelopment of Herpes viruses during nuclear exit is poorly understood. In Herpes simplex virus type-1 (HSV-1), proteins pUL31 and pUL34 are critical, while pUS3 and some others contribute; however, efficient membrane fusion may require additional host proteins. We postulated that vesicle fusion proteins present in the nuclear envelope might facilitate primary envelopment and/or de-envelopment fusion with the outer nuclear membrane. Indeed, a subpopulation of vesicle-associated membrane protein-associated protein B (VAPB), a known vesicle trafficking protein, was present in the nuclear membrane co-locating with pUL34. VAPB knockdown significantly reduced both cell-associated and supernatant virus titers. Moreover, VAPB depletion reduced cytoplasmic accumulation of virus particles and increased levels of nuclear encapsidated viral DNA. These results suggest that VAPB is an important player in the exit of primary enveloped HSV-1 virions from the nucleus. Importantly, VAPB knockdown did not alter pUL34, calnexin or GM-130 localization during infection, arguing against an indirect effect of VAPB on cellular vesicles and trafficking. Immunogold-labelling electron microscopy confirmed VAPB presence in nuclear membranes and moreover associated with primary enveloped HSV-1 particles. These data suggest that VAPB could be a cellular component of a complex that facilitates UL31/UL34/US3-mediated HSV-1 nuclear egress.
    Electronic ISSN: 2073-4409
    Topics: Biology
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  • 5
    Publication Date: 2018-06-20
    Print ISSN: 1544-9173
    Electronic ISSN: 1545-7885
    Topics: Biology
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  • 6
    Publication Date: 2020-10-19
    Description: Cryo electron microscopy (cryo-EM), a key method for structure determination involves imaging purified material embedded in vitreous ice. Images are then computationally processed to obtain three-dimensional structures approaching atomic resolution. There is increasing interest in extending structural studies by cryo-EM into the cell, where biological structures and processes may be imaged in context. The limited penetrating power of electrons prevents imaging of thick specimens (〉 500 nm) however. Cryo-sectioning methods employed to overcome this are technically challenging, subject to artefacts or involve specialised and costly equipment. Here we describe the first structure of herpesvirus capsids determined by sub-tomogram averaging from nuclei of eukaryotic cells, achieved by cryo-electron tomography (cryo-ET) of re-vitrified cell sections prepared using the Tokuyasu method. Our reconstructions confirm that the capsid associated tegument complex is present on capsids prior to nuclear egress. We demonstrate that this method is suited to both 3D structure determination and correlative light/electron microscopy, thus expanding the scope of cryogenic cellular imaging.
    Electronic ISSN: 2045-2322
    Topics: Natural Sciences in General
    Published by Springer Nature
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