Virus assembly and exit pathways:
Gespeichert in:
| Weitere beteiligte Personen: | , , |
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| Format: | Elektronisch E-Book |
| Sprache: | Englisch |
| Veröffentlicht: |
Cambride, MA, United States ; San Diego, CA, United States ; Kidlington, Oxford, United Kingdom ; London, United Kingdom
Academic Press, an imprint of Elsevier
2020
|
| Ausgabe: | First edition |
| Schriftenreihe: | Advances in virus research
108 |
| Links: | https://ebookcentral.proquest.com/lib/munchentech/detail.action?docID=6377810 |
| Umfang: | 1 Online-Ressource (xi, 392 Seiten) Illustrationen, Diagramme |
| ISBN: | 9780128207628 |
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| 245 | 1 | 0 | |a Virus assembly and exit pathways |c edited by Margaret Kielian, Thomas C. Mettenleiter, Marilyn J. Roossinck |
| 250 | |a First edition | ||
| 264 | 1 | |a Cambride, MA, United States ; San Diego, CA, United States ; Kidlington, Oxford, United Kingdom ; London, United Kingdom |b Academic Press, an imprint of Elsevier |c 2020 | |
| 264 | 4 | |c © 2020 | |
| 300 | |a 1 Online-Ressource (xi, 392 Seiten) |b Illustrationen, Diagramme | ||
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| 490 | 1 | |a Advances in virus research |v 108 | |
| 505 | 8 | |a Intro -- Virus Assembly and Exit Pathways -- Copyright -- Contents -- Contributors -- Chapter One: Geminivirus structure and assembly -- 1. Introduction -- 1.1. Genome organization -- 1.2. Host range and insect vector -- 2. Geminivirus structures -- 2.1. The geminivirus capsid architecture is encoded within the CP amino acid sequence -- 2.2. CP:CP and symmetry related interactions -- 2.3. CP:genome interactions -- 2.4. Geminivirus capsid assembly -- 3. Host and vector organelles important for capsid transport and gene expression -- 4. Environmental pH and capsid assembly -- 5. Methods of geminivirus control -- 5.1. Symptoms and diagnosis of geminivirus infections -- 5.2. Current methods of geminivirus control -- 5.3. Promising new technologies -- 6. Summary -- References -- Chapter Two: Structure-guided paradigm shifts in flavivirus assembly and maturation mechanisms -- 1. Introduction -- 1.1. Flavivirus life cycle -- 2. Flavivirus polyprotein translation and processing -- 3. Flavivirus structural proteins: Structure and function -- 3.1. Capsid (C) protein -- 3.2. Pre-membrane/membrane protein (prM/M) -- 3.3. The envelope protein (E) -- 3.3.1. E domain I -- 3.3.2. E domain II -- 3.3.3. E domain III -- 3.3.4. E stem-anchor region -- 3.3.5. prM-E heterodimer TMDs -- 4. Flavivirus assembly and budding -- 5. Flavivirus maturation and egress -- 6. Conclusions -- Acknowledgments -- Funding -- References -- Chapter Three: Viral cell-to-cell spread: Conventional and non-conventional ways -- 1. Introduction -- 2. Modes of cell-to-cell spread -- 2.1. Cell-free viral particles -- 2.2. Formation of actin tails -- 2.3. Syncytia -- 2.4. Spread at cell junctions -- 2.5. Virological synapses -- 2.6. Viral biofilms -- 2.7. Tunneling nanotubes -- 2.8. Filopodia -- 2.9. Membrane pores -- 2.10. Extracellular vesicles -- 3. Advantages of direct cell-to-cell spread | |
| 505 | 8 | |a 3.1. Rapid spread -- 3.2. Multiple genome transfer -- 3.3. Evasion of anti-viral and immune barriers -- 3.4. Role in pathogenesis -- 4. Experimental approaches for studying cell-to-cell spread -- 4.1. Cell culture experiments -- 4.2. Imaging techniques -- 5. Concluding remarks -- Acknowledgments -- References -- Chapter Four: Structure and assembly of archaeal viruses -- 1. Introduction: Diversity of archaeal viruses -- 2. Assembly of head-tailed archaeal viruses -- 2.1. Procapsid assembly -- 2.2. Capsid maturation -- 2.3. Genome packaging -- 2.4. Tail assembly -- 3. Assembly of tailless icosahedral viruses -- 3.1. Turriviridae family -- 3.2. Sphaerolipoviridae family -- 3.3. Portogloboviridae family -- 4. Assembly of filamentous viruses -- 4.1. Clavaviridae family -- 4.2. Rudiviridae family -- 4.3. Lipothrixviridae family -- 4.4. Tristromaviridae family -- 5. Assembly of spindle-shaped viruses -- 5.1. Fuselloviridae family -- 5.2. Bicaudaviridae family -- 6. Conclusions -- Acknowledgments -- References -- Chapter Five: Potyviral coat protein and genomic RNA: A striking partnership leading virion assembly and more -- 1. Introduction -- 2. Unlocking the smart structure of potyviral capsids -- 2.1. Discernible domains give meaning to the potyviral CP structure -- 2.2. Disorder drives functionality -- 2.3. Structure of the potyviral virion: An increasingly defined image -- 3. To assemble, or to disassemble, that is the question -- 3.1. The promiscuous polymerization of potyviral CP -- 3.2. Faithful potyviral virion assembly is more than CP self-polymerization -- 3.2.1. Protein requirements for potyviral virion assembly -- 3.2.2. Are specific RNA features required for potyviral virion assembly? -- 3.2.3. How does the potyviral CP select its cognate RNA? -- 4. CP and RNA encapsidation, stuck in the middle of infection | |
| 505 | 8 | |a 4.1. First steps of potyviral infection -- 4.2. Virion assembly and cell-to-cell and long-distance movement -- 4.3. CP-host factors interplay and regulation of viral replication -- 4.4. CP in the potyvirus/plant defense interaction -- 5. Potyviral capsids as biotechnological tools, an increasingly promising future -- 6. And now what? -- Acknowledgments -- References -- Chapter Six: Structure and assembly of double-stranded RNA mycoviruses -- 1. Introduction -- 2. Lineage of dsRNA viruses -- 3. Structure of dsRNA mycovirus capsids -- 3.1. Totivirus capsid structure: Saccharomyces cerevisiae virus L-A -- 3.2. Partitivirus capsid structure: Penicillium stoloniferum virus F -- 3.3. Chrysovirus capsid structure: Penicillium chrysogenum virus -- 3.4. Quadrivirus capsid structure: Rosellinia necatrix quadrivirus 1 -- 3.5. Megabirnavirus capsid structure: Rosellinia necatrix megabirnavirus 1 -- 4. Assembly of dsRNA mycoviruses -- 5. Mycovirus capsids as nanomachines for RNA synthesis -- 6. Evolutionary relationships among dsRNA mycoviruses -- 7. Additional functions of mycovirus capsids -- 8. Conclusions and perspectives -- Acknowledgments -- References -- Chapter Seven: Bluetongue virus assembly and exit pathways -- 1. Introduction -- 1.1. Overview of the replication cycle -- 2. Assembly pathway of core components -- 2.1. Assembly of the Two major proteins, VP7 and VP3 -- 2.2. The minor proteins, the three catalytic proteins -- 2.3. Assembly of genomic RNA and packaging -- 2.4. Assembly pathway of core proteins in virus infected cells -- 3. Interactions between core and outer capsid proteins -- 4. Virion egress pathway -- 4.1. The glycoprotein NS3 -- 4.2. Virus egress by cell lysis -- 4.3. Nonlytic release of BTV -- 5. Conclusion -- References -- Chapter Eight: Current capsid assembly models of icosahedral nucleocytoviricota viruses | |
| 505 | 8 | |a 1. The nucleocytoplasmic large DNA viruses (NCLDVs) -- 2. The double jelly roll and the nucleocytoviricota viruses (NCVs) -- 3. The structure of icosahedral NCVs -- 4. The triangulation numbers of the icosahedral NCV capsids -- 5. Viral factory and NCV assembly -- 6. The current models in the capsid assembly of NCVs -- 6.1. The symmetron assembly model -- 6.2. The spiral assembly model -- 6.3. The mCP scaffold model -- 7. The tape measure proteins (TmPs) on icosahedral NCV capsid assembly -- 8. A refined assembly model for giant virus capsids -- 9. Conclusion -- Acknowledgments -- Funding -- References -- Chapter Nine: Quasi-enveloped hepatitis virus assembly and release -- 1. Introduction -- 2. Quasi-enveloped HAV assembly and release -- 2.1. HAV virion structure -- 2.2. HAV capsid assembly and genome packaging -- 2.3. HAV envelopment and exit -- 2.4. Release of HAV from polarized hepatocytes -- 3. Quasi-enveloped HEV assembly and release -- 3.1. HEV virion structure -- 3.2. HEV capsid assembly and genome packaging -- 3.3. HEV envelopment and exit -- 3.4. Release of HEV from polarized hepatocytes -- 4. Unanswered questions and future directions -- Acknowledgments -- References -- Chapter Ten: Betaherpesvirus assembly and egress: Recent advances illuminate the path -- 1. Introduction -- 2. Overview -- 2.1. Herpesviruses -- 2.1.1. Herpesvirus taxonomy -- 2.1.2. Betaherpesviruses: Cytomegaloviruses and roseoloviruses -- 2.2. Why we care -- 2.3. Host systems -- 2.4. Betaherpesvirus replication cycle -- 2.4.1. Overview of lytic replication -- 2.4.1.1. Entry -- 2.4.1.2. Lytic gene expression and genome replication -- 2.4.1.3. Primary envelopment and nuclear egress -- 2.4.1.4. Tegumentation -- 2.4.1.5. Secondary envelopment and release -- 3. Viral interactions with and modification of host systems -- 3.1. Metabolism -- 3.1.1. Mitochondria -- 3.1.2. Lipids | |
| 505 | 8 | |a 3.1.3. Glycolysis -- 3.2. Betaherpesviruses interact with host cytoplasmic structures and pathways -- 3.2.1. HCMV cVAC -- 3.2.2. Microtubules -- 3.2.3. Autophagy and virus replication -- 3.2.4. ESCRT system -- 3.2.5. Endocytic-recycling compartment -- 3.2.6. Infection-induced changes in organelle proteomes and structures -- 3.2.7. Antiviral defenses -- 3.2.7.1. Apoptosis -- 3.2.7.2. Inflammasome activity -- 3.2.7.3. Autophagy and antiviral defense -- 3.3. Virion components and structure -- 3.3.1. Genome -- 3.3.2. Nucleocapsid and capsid-associated tegument complexes -- 3.3.2.1. Alternative capsids formed during infection -- 3.3.3. Tegument -- 3.3.4. Envelope -- 4. Betaherpesvirus virion assembly and egress -- 4.1. Nuclear steps during betaherpesvirus virion assembly -- 4.1.1. Virus gene expression -- 4.1.2. Genome replication -- 4.1.3. Capsid assembly -- 4.1.4. Genome packaging -- 4.1.5. Nuclear egress -- 4.2. Cytoplasmic assembly -- 4.2.1. Virion trafficking/transport -- 4.2.2. Tegumentation -- 4.2.3. Secondary envelopment -- 4.2.4. Egress -- 5. Final perspective -- References | |
| 700 | 1 | |a Kielian, Margaret |0 (DE-588)1221770683 |4 edt | |
| 700 | 1 | |a Mettenleiter, Thomas C. |d 1957- |0 (DE-588)141505168 |4 edt | |
| 700 | 1 | |a Roossinck, Marilyn J. |d ca. 20./21. Jh. |0 (DE-588)1147011915 |4 edt | |
| 776 | 0 | 8 | |i Erscheint auch als |a Kielian, Margaret |t Virus Assembly and Exit Pathways |d San Diego : Elsevier Science & Technology,c2020 |n Druck-Ausgabe |z 978-0-12-820761-1 |
| 830 | 0 | |a Advances in virus research |v 108 |w (DE-604)BV021797746 |9 108 | |
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Datensatz im Suchindex
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| _version_ | 1821935654502662144 |
| any_adam_object | |
| author2 | Kielian, Margaret Mettenleiter, Thomas C. 1957- Roossinck, Marilyn J. ca. 20./21. Jh |
| author2_role | edt edt edt |
| author2_variant | m k mk t c m tc tcm m j r mj mjr |
| author_GND | (DE-588)1221770683 (DE-588)141505168 (DE-588)1147011915 |
| author_facet | Kielian, Margaret Mettenleiter, Thomas C. 1957- Roossinck, Marilyn J. ca. 20./21. Jh |
| building | Verbundindex |
| bvnumber | BV047442148 |
| classification_tum | MED 403 BIO 300 |
| collection | ZDB-30-PQE |
| contents | Intro -- Virus Assembly and Exit Pathways -- Copyright -- Contents -- Contributors -- Chapter One: Geminivirus structure and assembly -- 1. Introduction -- 1.1. Genome organization -- 1.2. Host range and insect vector -- 2. Geminivirus structures -- 2.1. The geminivirus capsid architecture is encoded within the CP amino acid sequence -- 2.2. CP:CP and symmetry related interactions -- 2.3. CP:genome interactions -- 2.4. Geminivirus capsid assembly -- 3. Host and vector organelles important for capsid transport and gene expression -- 4. Environmental pH and capsid assembly -- 5. Methods of geminivirus control -- 5.1. Symptoms and diagnosis of geminivirus infections -- 5.2. Current methods of geminivirus control -- 5.3. Promising new technologies -- 6. Summary -- References -- Chapter Two: Structure-guided paradigm shifts in flavivirus assembly and maturation mechanisms -- 1. Introduction -- 1.1. Flavivirus life cycle -- 2. Flavivirus polyprotein translation and processing -- 3. Flavivirus structural proteins: Structure and function -- 3.1. Capsid (C) protein -- 3.2. Pre-membrane/membrane protein (prM/M) -- 3.3. The envelope protein (E) -- 3.3.1. E domain I -- 3.3.2. E domain II -- 3.3.3. E domain III -- 3.3.4. E stem-anchor region -- 3.3.5. prM-E heterodimer TMDs -- 4. Flavivirus assembly and budding -- 5. Flavivirus maturation and egress -- 6. Conclusions -- Acknowledgments -- Funding -- References -- Chapter Three: Viral cell-to-cell spread: Conventional and non-conventional ways -- 1. Introduction -- 2. Modes of cell-to-cell spread -- 2.1. Cell-free viral particles -- 2.2. Formation of actin tails -- 2.3. Syncytia -- 2.4. Spread at cell junctions -- 2.5. Virological synapses -- 2.6. Viral biofilms -- 2.7. Tunneling nanotubes -- 2.8. Filopodia -- 2.9. Membrane pores -- 2.10. Extracellular vesicles -- 3. Advantages of direct cell-to-cell spread 3.1. Rapid spread -- 3.2. Multiple genome transfer -- 3.3. Evasion of anti-viral and immune barriers -- 3.4. Role in pathogenesis -- 4. Experimental approaches for studying cell-to-cell spread -- 4.1. Cell culture experiments -- 4.2. Imaging techniques -- 5. Concluding remarks -- Acknowledgments -- References -- Chapter Four: Structure and assembly of archaeal viruses -- 1. Introduction: Diversity of archaeal viruses -- 2. Assembly of head-tailed archaeal viruses -- 2.1. Procapsid assembly -- 2.2. Capsid maturation -- 2.3. Genome packaging -- 2.4. Tail assembly -- 3. Assembly of tailless icosahedral viruses -- 3.1. Turriviridae family -- 3.2. Sphaerolipoviridae family -- 3.3. Portogloboviridae family -- 4. Assembly of filamentous viruses -- 4.1. Clavaviridae family -- 4.2. Rudiviridae family -- 4.3. Lipothrixviridae family -- 4.4. Tristromaviridae family -- 5. Assembly of spindle-shaped viruses -- 5.1. Fuselloviridae family -- 5.2. Bicaudaviridae family -- 6. Conclusions -- Acknowledgments -- References -- Chapter Five: Potyviral coat protein and genomic RNA: A striking partnership leading virion assembly and more -- 1. Introduction -- 2. Unlocking the smart structure of potyviral capsids -- 2.1. Discernible domains give meaning to the potyviral CP structure -- 2.2. Disorder drives functionality -- 2.3. Structure of the potyviral virion: An increasingly defined image -- 3. To assemble, or to disassemble, that is the question -- 3.1. The promiscuous polymerization of potyviral CP -- 3.2. Faithful potyviral virion assembly is more than CP self-polymerization -- 3.2.1. Protein requirements for potyviral virion assembly -- 3.2.2. Are specific RNA features required for potyviral virion assembly? -- 3.2.3. How does the potyviral CP select its cognate RNA? -- 4. CP and RNA encapsidation, stuck in the middle of infection 4.1. First steps of potyviral infection -- 4.2. Virion assembly and cell-to-cell and long-distance movement -- 4.3. CP-host factors interplay and regulation of viral replication -- 4.4. CP in the potyvirus/plant defense interaction -- 5. Potyviral capsids as biotechnological tools, an increasingly promising future -- 6. And now what? -- Acknowledgments -- References -- Chapter Six: Structure and assembly of double-stranded RNA mycoviruses -- 1. Introduction -- 2. Lineage of dsRNA viruses -- 3. Structure of dsRNA mycovirus capsids -- 3.1. Totivirus capsid structure: Saccharomyces cerevisiae virus L-A -- 3.2. Partitivirus capsid structure: Penicillium stoloniferum virus F -- 3.3. Chrysovirus capsid structure: Penicillium chrysogenum virus -- 3.4. Quadrivirus capsid structure: Rosellinia necatrix quadrivirus 1 -- 3.5. Megabirnavirus capsid structure: Rosellinia necatrix megabirnavirus 1 -- 4. Assembly of dsRNA mycoviruses -- 5. Mycovirus capsids as nanomachines for RNA synthesis -- 6. Evolutionary relationships among dsRNA mycoviruses -- 7. Additional functions of mycovirus capsids -- 8. Conclusions and perspectives -- Acknowledgments -- References -- Chapter Seven: Bluetongue virus assembly and exit pathways -- 1. Introduction -- 1.1. Overview of the replication cycle -- 2. Assembly pathway of core components -- 2.1. Assembly of the Two major proteins, VP7 and VP3 -- 2.2. The minor proteins, the three catalytic proteins -- 2.3. Assembly of genomic RNA and packaging -- 2.4. Assembly pathway of core proteins in virus infected cells -- 3. Interactions between core and outer capsid proteins -- 4. Virion egress pathway -- 4.1. The glycoprotein NS3 -- 4.2. Virus egress by cell lysis -- 4.3. Nonlytic release of BTV -- 5. Conclusion -- References -- Chapter Eight: Current capsid assembly models of icosahedral nucleocytoviricota viruses 1. The nucleocytoplasmic large DNA viruses (NCLDVs) -- 2. The double jelly roll and the nucleocytoviricota viruses (NCVs) -- 3. The structure of icosahedral NCVs -- 4. The triangulation numbers of the icosahedral NCV capsids -- 5. Viral factory and NCV assembly -- 6. The current models in the capsid assembly of NCVs -- 6.1. The symmetron assembly model -- 6.2. The spiral assembly model -- 6.3. The mCP scaffold model -- 7. The tape measure proteins (TmPs) on icosahedral NCV capsid assembly -- 8. A refined assembly model for giant virus capsids -- 9. Conclusion -- Acknowledgments -- Funding -- References -- Chapter Nine: Quasi-enveloped hepatitis virus assembly and release -- 1. Introduction -- 2. Quasi-enveloped HAV assembly and release -- 2.1. HAV virion structure -- 2.2. HAV capsid assembly and genome packaging -- 2.3. HAV envelopment and exit -- 2.4. Release of HAV from polarized hepatocytes -- 3. Quasi-enveloped HEV assembly and release -- 3.1. HEV virion structure -- 3.2. HEV capsid assembly and genome packaging -- 3.3. HEV envelopment and exit -- 3.4. Release of HEV from polarized hepatocytes -- 4. Unanswered questions and future directions -- Acknowledgments -- References -- Chapter Ten: Betaherpesvirus assembly and egress: Recent advances illuminate the path -- 1. Introduction -- 2. Overview -- 2.1. Herpesviruses -- 2.1.1. Herpesvirus taxonomy -- 2.1.2. Betaherpesviruses: Cytomegaloviruses and roseoloviruses -- 2.2. Why we care -- 2.3. Host systems -- 2.4. Betaherpesvirus replication cycle -- 2.4.1. Overview of lytic replication -- 2.4.1.1. Entry -- 2.4.1.2. Lytic gene expression and genome replication -- 2.4.1.3. Primary envelopment and nuclear egress -- 2.4.1.4. Tegumentation -- 2.4.1.5. Secondary envelopment and release -- 3. Viral interactions with and modification of host systems -- 3.1. Metabolism -- 3.1.1. Mitochondria -- 3.1.2. Lipids 3.1.3. Glycolysis -- 3.2. Betaherpesviruses interact with host cytoplasmic structures and pathways -- 3.2.1. HCMV cVAC -- 3.2.2. Microtubules -- 3.2.3. Autophagy and virus replication -- 3.2.4. ESCRT system -- 3.2.5. Endocytic-recycling compartment -- 3.2.6. Infection-induced changes in organelle proteomes and structures -- 3.2.7. Antiviral defenses -- 3.2.7.1. Apoptosis -- 3.2.7.2. Inflammasome activity -- 3.2.7.3. Autophagy and antiviral defense -- 3.3. Virion components and structure -- 3.3.1. Genome -- 3.3.2. Nucleocapsid and capsid-associated tegument complexes -- 3.3.2.1. Alternative capsids formed during infection -- 3.3.3. Tegument -- 3.3.4. Envelope -- 4. Betaherpesvirus virion assembly and egress -- 4.1. Nuclear steps during betaherpesvirus virion assembly -- 4.1.1. Virus gene expression -- 4.1.2. Genome replication -- 4.1.3. Capsid assembly -- 4.1.4. Genome packaging -- 4.1.5. Nuclear egress -- 4.2. Cytoplasmic assembly -- 4.2.1. Virion trafficking/transport -- 4.2.2. Tegumentation -- 4.2.3. Secondary envelopment -- 4.2.4. Egress -- 5. Final perspective -- References |
| ctrlnum | (ZDB-30-PQE)EBC6377810 (ZDB-30-PAD)EBC6377810 (ZDB-89-EBL)EBL6377810 (OCoLC)1268182781 (DE-599)BVBBV047442148 |
| dewey-full | 579.2 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 579 - Microorganisms, fungi & algae |
| dewey-raw | 579.2 |
| dewey-search | 579.2 |
| dewey-sort | 3579.2 |
| dewey-tens | 570 - Biology |
| discipline | Biologie Medizin |
| edition | First edition |
| format | Electronic eBook |
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Introduction -- 1.1. Genome organization -- 1.2. Host range and insect vector -- 2. Geminivirus structures -- 2.1. The geminivirus capsid architecture is encoded within the CP amino acid sequence -- 2.2. CP:CP and symmetry related interactions -- 2.3. CP:genome interactions -- 2.4. Geminivirus capsid assembly -- 3. Host and vector organelles important for capsid transport and gene expression -- 4. Environmental pH and capsid assembly -- 5. Methods of geminivirus control -- 5.1. Symptoms and diagnosis of geminivirus infections -- 5.2. Current methods of geminivirus control -- 5.3. Promising new technologies -- 6. Summary -- References -- Chapter Two: Structure-guided paradigm shifts in flavivirus assembly and maturation mechanisms -- 1. Introduction -- 1.1. Flavivirus life cycle -- 2. Flavivirus polyprotein translation and processing -- 3. Flavivirus structural proteins: Structure and function -- 3.1. Capsid (C) protein -- 3.2. Pre-membrane/membrane protein (prM/M) -- 3.3. The envelope protein (E) -- 3.3.1. E domain I -- 3.3.2. E domain II -- 3.3.3. E domain III -- 3.3.4. E stem-anchor region -- 3.3.5. prM-E heterodimer TMDs -- 4. Flavivirus assembly and budding -- 5. Flavivirus maturation and egress -- 6. Conclusions -- Acknowledgments -- Funding -- References -- Chapter Three: Viral cell-to-cell spread: Conventional and non-conventional ways -- 1. Introduction -- 2. Modes of cell-to-cell spread -- 2.1. Cell-free viral particles -- 2.2. Formation of actin tails -- 2.3. Syncytia -- 2.4. Spread at cell junctions -- 2.5. Virological synapses -- 2.6. Viral biofilms -- 2.7. Tunneling nanotubes -- 2.8. Filopodia -- 2.9. Membrane pores -- 2.10. Extracellular vesicles -- 3. Advantages of direct cell-to-cell spread</subfield></datafield><datafield tag="505" ind1="8" ind2=" "><subfield code="a">3.1. Rapid spread -- 3.2. Multiple genome transfer -- 3.3. Evasion of anti-viral and immune barriers -- 3.4. Role in pathogenesis -- 4. Experimental approaches for studying cell-to-cell spread -- 4.1. Cell culture experiments -- 4.2. Imaging techniques -- 5. Concluding remarks -- Acknowledgments -- References -- Chapter Four: Structure and assembly of archaeal viruses -- 1. Introduction: Diversity of archaeal viruses -- 2. Assembly of head-tailed archaeal viruses -- 2.1. Procapsid assembly -- 2.2. Capsid maturation -- 2.3. Genome packaging -- 2.4. Tail assembly -- 3. Assembly of tailless icosahedral viruses -- 3.1. Turriviridae family -- 3.2. Sphaerolipoviridae family -- 3.3. Portogloboviridae family -- 4. Assembly of filamentous viruses -- 4.1. Clavaviridae family -- 4.2. Rudiviridae family -- 4.3. Lipothrixviridae family -- 4.4. Tristromaviridae family -- 5. Assembly of spindle-shaped viruses -- 5.1. Fuselloviridae family -- 5.2. Bicaudaviridae family -- 6. Conclusions -- Acknowledgments -- References -- Chapter Five: Potyviral coat protein and genomic RNA: A striking partnership leading virion assembly and more -- 1. Introduction -- 2. Unlocking the smart structure of potyviral capsids -- 2.1. Discernible domains give meaning to the potyviral CP structure -- 2.2. Disorder drives functionality -- 2.3. Structure of the potyviral virion: An increasingly defined image -- 3. To assemble, or to disassemble, that is the question -- 3.1. The promiscuous polymerization of potyviral CP -- 3.2. Faithful potyviral virion assembly is more than CP self-polymerization -- 3.2.1. Protein requirements for potyviral virion assembly -- 3.2.2. Are specific RNA features required for potyviral virion assembly? -- 3.2.3. How does the potyviral CP select its cognate RNA? -- 4. CP and RNA encapsidation, stuck in the middle of infection</subfield></datafield><datafield tag="505" ind1="8" ind2=" "><subfield code="a">4.1. First steps of potyviral infection -- 4.2. Virion assembly and cell-to-cell and long-distance movement -- 4.3. CP-host factors interplay and regulation of viral replication -- 4.4. CP in the potyvirus/plant defense interaction -- 5. Potyviral capsids as biotechnological tools, an increasingly promising future -- 6. And now what? -- Acknowledgments -- References -- Chapter Six: Structure and assembly of double-stranded RNA mycoviruses -- 1. Introduction -- 2. Lineage of dsRNA viruses -- 3. Structure of dsRNA mycovirus capsids -- 3.1. Totivirus capsid structure: Saccharomyces cerevisiae virus L-A -- 3.2. Partitivirus capsid structure: Penicillium stoloniferum virus F -- 3.3. Chrysovirus capsid structure: Penicillium chrysogenum virus -- 3.4. Quadrivirus capsid structure: Rosellinia necatrix quadrivirus 1 -- 3.5. Megabirnavirus capsid structure: Rosellinia necatrix megabirnavirus 1 -- 4. Assembly of dsRNA mycoviruses -- 5. Mycovirus capsids as nanomachines for RNA synthesis -- 6. Evolutionary relationships among dsRNA mycoviruses -- 7. Additional functions of mycovirus capsids -- 8. Conclusions and perspectives -- Acknowledgments -- References -- Chapter Seven: Bluetongue virus assembly and exit pathways -- 1. Introduction -- 1.1. Overview of the replication cycle -- 2. Assembly pathway of core components -- 2.1. Assembly of the Two major proteins, VP7 and VP3 -- 2.2. The minor proteins, the three catalytic proteins -- 2.3. Assembly of genomic RNA and packaging -- 2.4. Assembly pathway of core proteins in virus infected cells -- 3. Interactions between core and outer capsid proteins -- 4. Virion egress pathway -- 4.1. The glycoprotein NS3 -- 4.2. Virus egress by cell lysis -- 4.3. Nonlytic release of BTV -- 5. Conclusion -- References -- Chapter Eight: Current capsid assembly models of icosahedral nucleocytoviricota viruses</subfield></datafield><datafield tag="505" ind1="8" ind2=" "><subfield code="a">1. The nucleocytoplasmic large DNA viruses (NCLDVs) -- 2. The double jelly roll and the nucleocytoviricota viruses (NCVs) -- 3. The structure of icosahedral NCVs -- 4. The triangulation numbers of the icosahedral NCV capsids -- 5. Viral factory and NCV assembly -- 6. The current models in the capsid assembly of NCVs -- 6.1. The symmetron assembly model -- 6.2. The spiral assembly model -- 6.3. The mCP scaffold model -- 7. The tape measure proteins (TmPs) on icosahedral NCV capsid assembly -- 8. A refined assembly model for giant virus capsids -- 9. Conclusion -- Acknowledgments -- Funding -- References -- Chapter Nine: Quasi-enveloped hepatitis virus assembly and release -- 1. Introduction -- 2. Quasi-enveloped HAV assembly and release -- 2.1. HAV virion structure -- 2.2. HAV capsid assembly and genome packaging -- 2.3. HAV envelopment and exit -- 2.4. Release of HAV from polarized hepatocytes -- 3. Quasi-enveloped HEV assembly and release -- 3.1. HEV virion structure -- 3.2. HEV capsid assembly and genome packaging -- 3.3. HEV envelopment and exit -- 3.4. Release of HEV from polarized hepatocytes -- 4. Unanswered questions and future directions -- Acknowledgments -- References -- Chapter Ten: Betaherpesvirus assembly and egress: Recent advances illuminate the path -- 1. Introduction -- 2. Overview -- 2.1. Herpesviruses -- 2.1.1. Herpesvirus taxonomy -- 2.1.2. Betaherpesviruses: Cytomegaloviruses and roseoloviruses -- 2.2. Why we care -- 2.3. Host systems -- 2.4. Betaherpesvirus replication cycle -- 2.4.1. Overview of lytic replication -- 2.4.1.1. Entry -- 2.4.1.2. Lytic gene expression and genome replication -- 2.4.1.3. Primary envelopment and nuclear egress -- 2.4.1.4. Tegumentation -- 2.4.1.5. Secondary envelopment and release -- 3. Viral interactions with and modification of host systems -- 3.1. Metabolism -- 3.1.1. Mitochondria -- 3.1.2. Lipids</subfield></datafield><datafield tag="505" ind1="8" ind2=" "><subfield code="a">3.1.3. Glycolysis -- 3.2. Betaherpesviruses interact with host cytoplasmic structures and pathways -- 3.2.1. HCMV cVAC -- 3.2.2. Microtubules -- 3.2.3. Autophagy and virus replication -- 3.2.4. ESCRT system -- 3.2.5. Endocytic-recycling compartment -- 3.2.6. Infection-induced changes in organelle proteomes and structures -- 3.2.7. Antiviral defenses -- 3.2.7.1. Apoptosis -- 3.2.7.2. Inflammasome activity -- 3.2.7.3. Autophagy and antiviral defense -- 3.3. Virion components and structure -- 3.3.1. Genome -- 3.3.2. Nucleocapsid and capsid-associated tegument complexes -- 3.3.2.1. Alternative capsids formed during infection -- 3.3.3. Tegument -- 3.3.4. Envelope -- 4. Betaherpesvirus virion assembly and egress -- 4.1. Nuclear steps during betaherpesvirus virion assembly -- 4.1.1. Virus gene expression -- 4.1.2. Genome replication -- 4.1.3. Capsid assembly -- 4.1.4. Genome packaging -- 4.1.5. Nuclear egress -- 4.2. Cytoplasmic assembly -- 4.2.1. Virion trafficking/transport -- 4.2.2. Tegumentation -- 4.2.3. Secondary envelopment -- 4.2.4. Egress -- 5. Final perspective -- References</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kielian, Margaret</subfield><subfield code="0">(DE-588)1221770683</subfield><subfield code="4">edt</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Mettenleiter, Thomas C.</subfield><subfield code="d">1957-</subfield><subfield code="0">(DE-588)141505168</subfield><subfield code="4">edt</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Roossinck, Marilyn J.</subfield><subfield code="d">ca. 20./21. Jh.</subfield><subfield code="0">(DE-588)1147011915</subfield><subfield code="4">edt</subfield></datafield><datafield tag="776" ind1="0" ind2="8"><subfield code="i">Erscheint auch als</subfield><subfield code="a">Kielian, Margaret</subfield><subfield code="t">Virus Assembly and Exit Pathways</subfield><subfield code="d">San Diego : Elsevier Science & Technology,c2020</subfield><subfield code="n">Druck-Ausgabe</subfield><subfield code="z">978-0-12-820761-1</subfield></datafield><datafield tag="830" ind1=" " ind2="0"><subfield code="a">Advances in virus research</subfield><subfield code="v">108</subfield><subfield code="w">(DE-604)BV021797746</subfield><subfield code="9">108</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-30-PQE</subfield></datafield><datafield tag="943" ind1="1" ind2=" "><subfield code="a">oai:aleph.bib-bvb.de:BVB01-032844300</subfield></datafield><datafield tag="966" ind1="e" ind2=" "><subfield code="u">https://ebookcentral.proquest.com/lib/munchentech/detail.action?docID=6377810</subfield><subfield code="l">DE-91</subfield><subfield code="p">ZDB-30-PQE</subfield><subfield code="q">TUM_PDA_PQE_Kauf</subfield><subfield code="x">Aggregator</subfield><subfield code="3">Volltext</subfield></datafield></record></collection> |
| id | DE-604.BV047442148 |
| illustrated | Illustrated |
| indexdate | 2024-12-20T19:19:41Z |
| institution | BVB |
| isbn | 9780128207628 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-032844300 |
| oclc_num | 1268182781 |
| open_access_boolean | |
| owner | DE-91 DE-BY-TUM |
| owner_facet | DE-91 DE-BY-TUM |
| physical | 1 Online-Ressource (xi, 392 Seiten) Illustrationen, Diagramme |
| psigel | ZDB-30-PQE ZDB-30-PQE TUM_PDA_PQE_Kauf |
| publishDate | 2020 |
| publishDateSearch | 2020 |
| publishDateSort | 2020 |
| publisher | Academic Press, an imprint of Elsevier |
| record_format | marc |
| series | Advances in virus research |
| series2 | Advances in virus research |
| spellingShingle | Virus assembly and exit pathways Advances in virus research Intro -- Virus Assembly and Exit Pathways -- Copyright -- Contents -- Contributors -- Chapter One: Geminivirus structure and assembly -- 1. Introduction -- 1.1. Genome organization -- 1.2. Host range and insect vector -- 2. Geminivirus structures -- 2.1. The geminivirus capsid architecture is encoded within the CP amino acid sequence -- 2.2. CP:CP and symmetry related interactions -- 2.3. CP:genome interactions -- 2.4. Geminivirus capsid assembly -- 3. Host and vector organelles important for capsid transport and gene expression -- 4. Environmental pH and capsid assembly -- 5. Methods of geminivirus control -- 5.1. Symptoms and diagnosis of geminivirus infections -- 5.2. Current methods of geminivirus control -- 5.3. Promising new technologies -- 6. Summary -- References -- Chapter Two: Structure-guided paradigm shifts in flavivirus assembly and maturation mechanisms -- 1. Introduction -- 1.1. Flavivirus life cycle -- 2. Flavivirus polyprotein translation and processing -- 3. Flavivirus structural proteins: Structure and function -- 3.1. Capsid (C) protein -- 3.2. Pre-membrane/membrane protein (prM/M) -- 3.3. The envelope protein (E) -- 3.3.1. E domain I -- 3.3.2. E domain II -- 3.3.3. E domain III -- 3.3.4. E stem-anchor region -- 3.3.5. prM-E heterodimer TMDs -- 4. Flavivirus assembly and budding -- 5. Flavivirus maturation and egress -- 6. Conclusions -- Acknowledgments -- Funding -- References -- Chapter Three: Viral cell-to-cell spread: Conventional and non-conventional ways -- 1. Introduction -- 2. Modes of cell-to-cell spread -- 2.1. Cell-free viral particles -- 2.2. Formation of actin tails -- 2.3. Syncytia -- 2.4. Spread at cell junctions -- 2.5. Virological synapses -- 2.6. Viral biofilms -- 2.7. Tunneling nanotubes -- 2.8. Filopodia -- 2.9. Membrane pores -- 2.10. Extracellular vesicles -- 3. Advantages of direct cell-to-cell spread 3.1. Rapid spread -- 3.2. Multiple genome transfer -- 3.3. Evasion of anti-viral and immune barriers -- 3.4. Role in pathogenesis -- 4. Experimental approaches for studying cell-to-cell spread -- 4.1. Cell culture experiments -- 4.2. Imaging techniques -- 5. Concluding remarks -- Acknowledgments -- References -- Chapter Four: Structure and assembly of archaeal viruses -- 1. Introduction: Diversity of archaeal viruses -- 2. Assembly of head-tailed archaeal viruses -- 2.1. Procapsid assembly -- 2.2. Capsid maturation -- 2.3. Genome packaging -- 2.4. Tail assembly -- 3. Assembly of tailless icosahedral viruses -- 3.1. Turriviridae family -- 3.2. Sphaerolipoviridae family -- 3.3. Portogloboviridae family -- 4. Assembly of filamentous viruses -- 4.1. Clavaviridae family -- 4.2. Rudiviridae family -- 4.3. Lipothrixviridae family -- 4.4. Tristromaviridae family -- 5. Assembly of spindle-shaped viruses -- 5.1. Fuselloviridae family -- 5.2. Bicaudaviridae family -- 6. Conclusions -- Acknowledgments -- References -- Chapter Five: Potyviral coat protein and genomic RNA: A striking partnership leading virion assembly and more -- 1. Introduction -- 2. Unlocking the smart structure of potyviral capsids -- 2.1. Discernible domains give meaning to the potyviral CP structure -- 2.2. Disorder drives functionality -- 2.3. Structure of the potyviral virion: An increasingly defined image -- 3. To assemble, or to disassemble, that is the question -- 3.1. The promiscuous polymerization of potyviral CP -- 3.2. Faithful potyviral virion assembly is more than CP self-polymerization -- 3.2.1. Protein requirements for potyviral virion assembly -- 3.2.2. Are specific RNA features required for potyviral virion assembly? -- 3.2.3. How does the potyviral CP select its cognate RNA? -- 4. CP and RNA encapsidation, stuck in the middle of infection 4.1. First steps of potyviral infection -- 4.2. Virion assembly and cell-to-cell and long-distance movement -- 4.3. CP-host factors interplay and regulation of viral replication -- 4.4. CP in the potyvirus/plant defense interaction -- 5. Potyviral capsids as biotechnological tools, an increasingly promising future -- 6. And now what? -- Acknowledgments -- References -- Chapter Six: Structure and assembly of double-stranded RNA mycoviruses -- 1. Introduction -- 2. Lineage of dsRNA viruses -- 3. Structure of dsRNA mycovirus capsids -- 3.1. Totivirus capsid structure: Saccharomyces cerevisiae virus L-A -- 3.2. Partitivirus capsid structure: Penicillium stoloniferum virus F -- 3.3. Chrysovirus capsid structure: Penicillium chrysogenum virus -- 3.4. Quadrivirus capsid structure: Rosellinia necatrix quadrivirus 1 -- 3.5. Megabirnavirus capsid structure: Rosellinia necatrix megabirnavirus 1 -- 4. Assembly of dsRNA mycoviruses -- 5. Mycovirus capsids as nanomachines for RNA synthesis -- 6. Evolutionary relationships among dsRNA mycoviruses -- 7. Additional functions of mycovirus capsids -- 8. Conclusions and perspectives -- Acknowledgments -- References -- Chapter Seven: Bluetongue virus assembly and exit pathways -- 1. Introduction -- 1.1. Overview of the replication cycle -- 2. Assembly pathway of core components -- 2.1. Assembly of the Two major proteins, VP7 and VP3 -- 2.2. The minor proteins, the three catalytic proteins -- 2.3. Assembly of genomic RNA and packaging -- 2.4. Assembly pathway of core proteins in virus infected cells -- 3. Interactions between core and outer capsid proteins -- 4. Virion egress pathway -- 4.1. The glycoprotein NS3 -- 4.2. Virus egress by cell lysis -- 4.3. Nonlytic release of BTV -- 5. Conclusion -- References -- Chapter Eight: Current capsid assembly models of icosahedral nucleocytoviricota viruses 1. The nucleocytoplasmic large DNA viruses (NCLDVs) -- 2. The double jelly roll and the nucleocytoviricota viruses (NCVs) -- 3. The structure of icosahedral NCVs -- 4. The triangulation numbers of the icosahedral NCV capsids -- 5. Viral factory and NCV assembly -- 6. The current models in the capsid assembly of NCVs -- 6.1. The symmetron assembly model -- 6.2. The spiral assembly model -- 6.3. The mCP scaffold model -- 7. The tape measure proteins (TmPs) on icosahedral NCV capsid assembly -- 8. A refined assembly model for giant virus capsids -- 9. Conclusion -- Acknowledgments -- Funding -- References -- Chapter Nine: Quasi-enveloped hepatitis virus assembly and release -- 1. Introduction -- 2. Quasi-enveloped HAV assembly and release -- 2.1. HAV virion structure -- 2.2. HAV capsid assembly and genome packaging -- 2.3. HAV envelopment and exit -- 2.4. Release of HAV from polarized hepatocytes -- 3. Quasi-enveloped HEV assembly and release -- 3.1. HEV virion structure -- 3.2. HEV capsid assembly and genome packaging -- 3.3. HEV envelopment and exit -- 3.4. Release of HEV from polarized hepatocytes -- 4. Unanswered questions and future directions -- Acknowledgments -- References -- Chapter Ten: Betaherpesvirus assembly and egress: Recent advances illuminate the path -- 1. Introduction -- 2. Overview -- 2.1. Herpesviruses -- 2.1.1. Herpesvirus taxonomy -- 2.1.2. Betaherpesviruses: Cytomegaloviruses and roseoloviruses -- 2.2. Why we care -- 2.3. Host systems -- 2.4. Betaherpesvirus replication cycle -- 2.4.1. Overview of lytic replication -- 2.4.1.1. Entry -- 2.4.1.2. Lytic gene expression and genome replication -- 2.4.1.3. Primary envelopment and nuclear egress -- 2.4.1.4. Tegumentation -- 2.4.1.5. Secondary envelopment and release -- 3. Viral interactions with and modification of host systems -- 3.1. Metabolism -- 3.1.1. Mitochondria -- 3.1.2. Lipids 3.1.3. Glycolysis -- 3.2. Betaherpesviruses interact with host cytoplasmic structures and pathways -- 3.2.1. HCMV cVAC -- 3.2.2. Microtubules -- 3.2.3. Autophagy and virus replication -- 3.2.4. ESCRT system -- 3.2.5. Endocytic-recycling compartment -- 3.2.6. Infection-induced changes in organelle proteomes and structures -- 3.2.7. Antiviral defenses -- 3.2.7.1. Apoptosis -- 3.2.7.2. Inflammasome activity -- 3.2.7.3. Autophagy and antiviral defense -- 3.3. Virion components and structure -- 3.3.1. Genome -- 3.3.2. Nucleocapsid and capsid-associated tegument complexes -- 3.3.2.1. Alternative capsids formed during infection -- 3.3.3. Tegument -- 3.3.4. Envelope -- 4. Betaherpesvirus virion assembly and egress -- 4.1. Nuclear steps during betaherpesvirus virion assembly -- 4.1.1. Virus gene expression -- 4.1.2. Genome replication -- 4.1.3. Capsid assembly -- 4.1.4. Genome packaging -- 4.1.5. Nuclear egress -- 4.2. Cytoplasmic assembly -- 4.2.1. Virion trafficking/transport -- 4.2.2. Tegumentation -- 4.2.3. Secondary envelopment -- 4.2.4. Egress -- 5. Final perspective -- References |
| title | Virus assembly and exit pathways |
| title_auth | Virus assembly and exit pathways |
| title_exact_search | Virus assembly and exit pathways |
| title_full | Virus assembly and exit pathways edited by Margaret Kielian, Thomas C. Mettenleiter, Marilyn J. Roossinck |
| title_fullStr | Virus assembly and exit pathways edited by Margaret Kielian, Thomas C. Mettenleiter, Marilyn J. Roossinck |
| title_full_unstemmed | Virus assembly and exit pathways edited by Margaret Kielian, Thomas C. Mettenleiter, Marilyn J. Roossinck |
| title_short | Virus assembly and exit pathways |
| title_sort | virus assembly and exit pathways |
| volume_link | (DE-604)BV021797746 |
| work_keys_str_mv | AT kielianmargaret virusassemblyandexitpathways AT mettenleiterthomasc virusassemblyandexitpathways AT roossinckmarilynj virusassemblyandexitpathways |