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Advances in Virus Research.

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Advances in Virus Research, Volume 119, is a comprehensive scholarly work edited by Robin MacDiarmid, Benhur Lee, and Martin Beer. It explores the intricate mechanisms of viral entry and replication, focusing on how viruses manipulate host cells for efficient infection and propagation. The book delv...

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Bibliographic Details
Main Author: MacDiarmid, Robin
Corporate Author: ScienceDirect (Online service)
Other Authors: Lee, Benhur, Beer, Martin
Format: eBook
Language:English
Published: Chantilly : Elsevier Science & Technology, 2024.
Edition:1st ed.
Series:Issn Series.
Subjects:
Host-virus relationships.
Virology.
Electronic books.
Online Access:Connect to the full text of this electronic book
Table of Contents:
  • Intro
  • Advances in Virus Research
  • Copyright
  • Contents
  • Contributors
  • Chapter One: Ubiquitination in viral entry and replication: Mechanisms and implications
  • 1. Introduction
  • 2. Ubiquitination: An overview
  • 2.1. Type of polyubiquitin linkages
  • 2.2. E3 ligases-Conductors of ubiquitin attachment
  • 2.2.1. RING
  • 2.2.2. HECT
  • 2.2.3. RBR
  • 2.3. Deubiquitinating enzymes (DUBs)
  • 3. Ubiquitination in viral entry
  • 3.1. Proviral effects
  • 3.1.1. Enhanced attachment
  • 3.1.2. Facilitated endocytosis
  • 3.1.3. Ubiquitination promotes virus uncoating and release of viral genome
  • 3.1.4. Facilitated fusion
  • 4. Viral strategies to manipulate ubiquitination during viral replication
  • 4.1. Ubiquitination regulating virus replication
  • 4.1.1. Ubiquitination facilitating viral replication via autophagy
  • 4.2. Ubiquitination in packaging and egress
  • 5. Antiviral effects
  • 5.1. Interference with viral attachment
  • 5.2. Regulation of immune responses and viral antagonism of innate immunity
  • 6. Therapeutic interventions by targeting ubiquitination and viral entry
  • 7. Concluding remark
  • Acknowledgments
  • References
  • Chapter Two: Selection of nonstandard viral genomes during the evolution of RNA viruses: A virus survival strategy or a p ...
  • 1. Introduction
  • 2. What drives the selection of nsVG types and species?
  • 2.1. Types of nsVGs
  • 2.2. One virus, different nsVG species
  • 2.3. Hotspots for nsVG generation
  • 2.4. Impact of the host cell on nsVG species
  • 2.5. Impact of viral proteins on nsVG species
  • 3. Origin of nsVGs
  • 4. Are nsVGs a strategy for viruses to be maintained in the host population?
  • 4.1. A case for the evolutionary advantage of nsVGs
  • 4.2. nsVG-induced interference as an integral part of the virus life cycle
  • 4.3. nsVGs and viral persistence
  • 4.4. nsVGs and viral transmission.
  • 4.5. nsVGs and viral epidemiology
  • 5. Concluding remarks
  • References
  • Chapter Three: Uncloaking the viral glycocalyx: How do viruses exploit glycoimmune checkpoints?
  • 1. Introduction
  • 1.1. Why do pathogens mimic host glycans?
  • 1.2. Sialic acids play central roles in mammalian glycan recognition systems
  • 1.3. The challenges of studying glycans are matched by promising new tools
  • 2. Many viruses interact with sialic acids during entry
  • 3. The sialic acid binding immunoglobulin-like lectins (Siglecs)
  • 3.1. Roles for additional classes of sialic acid binding receptors
  • 4. Viruses that engage Siglecs to dampen immune responses
  • 4.1. Hepatitis B virus
  • 4.2. Other examples: Sendai virus, vesicular stomatitis virus, and human immunodeficiency virus-1
  • 5. Viruses that use Siglecs or Siglec-like proteins to facilitate cell entry
  • 5.1. Porcine reproductive and respiratory syndrome virus (PRRSV)
  • 5.2. Varicella zoster virus
  • 5.3. Herpes simplex virus 1
  • 5.4. Human immunodeficiency virus type 1 (HIV-1)
  • 6. The glycan structures associated with virions and their roles in infection remain largely unknown, even for medically ...
  • 6.1. Criteria to establish physiological relevance of virion and virus infected cell associated glycocalyxes
  • 6.2. Viruses that establish persistent or chronic infections are promising candidates for discovering viral glycoimmune m ...
  • 7. Do viruses harness the unfolded protein response to sculpt the glycocalyxes of infected cells and virions?
  • 7.1. A brief overview of the UPR and protein glycosylation
  • 7.2. The IRE1/XBP1s arm of the UPR links ER stress to N-glycan architecture
  • 7.3. Viral modulation of the UPR holds the potential to impact virion and infected cell glycocalyces
  • 7.4. A cytomegalovirus UPR activator prevents shedding of the infected cell glycocalyx
  • 8. Further reading.