Johnson | Cell Entry by Non-Enveloped Viruses | E-Book | www.sack.de
E-Book

E-Book, Englisch, Band 343, 230 Seiten

Reihe: Current Topics in Microbiology and Immunology

Johnson Cell Entry by Non-Enveloped Viruses


1. Auflage 2010
ISBN: 978-3-642-13332-9
Verlag: Springer
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band 343, 230 Seiten

Reihe: Current Topics in Microbiology and Immunology

ISBN: 978-3-642-13332-9
Verlag: Springer
Format: PDF
Kopierschutz: 1 - PDF Watermark



The means by which non-enveloped viruses penetrate cellular membranes during cell entry remain poorly defined. Recent findings indicate several members of this group share a common mechanism of membrane penetration in which the virus particle undergoes programmed conformational changes, leading to capsid disassembly and release of small membrane-interacting peptides. A complete understanding of host cell entry by this minimal system will help elucidate the mechanisms of non-enveloped virus membrane penetration in general

Johnson Cell Entry by Non-Enveloped Viruses jetzt bestellen!

Autoren/Hrsg.


Weitere Infos & Material


1;Preface;6
2;References;8
3;Contents;10
4;Contributors;12
5;Flock House Virus: A Model System for Understanding Non-Enveloped Virus Entry and Membrane Penetration;16
5.1;1 Introduction;17
5.2;2 Capsid Architecture and Autocatalytic Cleavage of Subunits;18
5.2.1;2.1 FHV Expression Systems;18
5.2.2;2.2 Capsid Structure;19
5.2.3;2.3 Capsid-RNA Interactions;20
5.2.4;2.4 Autocatalytic Cleavage and Production of the Gamma Peptide;21
5.2.5;2.5 Structure and Organization of the gamma Peptides;23
5.2.6;2.6 Metal Ion Binding Sites;24
5.3;3 Early Events During FHV Cell Entry;26
5.3.1;3.1 FHV Cell Surface Receptor;27
5.3.2;3.2 Route of FHV Entry;27
5.4;4 FHV Membrane Penetration;27
5.4.1;4.1 Structure-Based Model of FHV Membrane Penetration;27
5.4.2;4.2 In Vitro Studies of FHV Membrane Penetration;28
5.4.3;4.3 FHV Membrane Lytic Activity Is Triggered by Low Endocytic pH;29
5.4.4;4.4 FHV Autoproteolytic Cleavage Is Required for Membrane Disruption;29
5.4.5;4.5 Working Model of FHV Entry and Membrane Penetration;30
5.4.6;4.6 Do Particle-Associated or Released gamma Peptides Mediate Membrane Interactions?;30
5.5;5 Entry-Intermediate Particle Types;31
5.5.1;5.1 The Eluted Particle: A Putative Entry Intermediate;31
5.5.2;5.2 Additional Entry Intermediate Particle Types?;32
5.6;6 Functional Domains of gamma Involved in Entry;32
5.6.1;6.1 gamma Trans-Complementation;33
5.6.2;6.2 Entry Related Function of gamma C-Terminus;33
5.6.3;6.3 Calcium Site Mutations Affect Membrane Penetration;34
5.6.4;6.4 Structure: Function Correlation of FHV Mutants;34
5.6.5;6.5 Does Quasi-Symmetry Dictate Separate Roles for gamma from Different Subunits?;35
5.7;7 Concluding Remarks;36
5.8;References;36
6;The Caliciviruses;38
6.1;1 Immunity Against Human Calicivirus Infection and Prospects for a Vaccine;38
6.2;2 Calicivirus Structure;41
6.3;3 Feline Calicivirus Interactions with Its Receptor;43
6.4;4 Interaction Between Noroviruses and Polysaccharides;45
6.5;5 Attenuation of NMV-1 Pathogenesis;47
6.6;6 The Cryo-TEM Structure of the T=3 MNV-1 Capsid;48
6.7;7 The Cryo-TEM Structure of MNV-1 Complexed with Fab´s;50
6.8;References;52
7;Picornaviruses;57
7.1;1 Introduction to Picornaviruses;58
7.2;2 Structure of Picornavirus Particles;60
7.3;3 Picornavirus Receptors;62
7.3.1;3.1 Immunoglobulin Superfamily Receptors: VCAM-1, ICAM-1, PVR, CAR;63
7.3.2;3.2 Decay Accelerating Factor;64
7.3.3;3.3 LDLR Family;64
7.3.4;3.4 Integrins;65
7.3.5;3.5 HAV Cellular Receptor (TIM-1);65
7.3.6;3.6 EV71 Receptors;66
7.3.7;3.7 Sialic Acid;66
7.3.8;3.8 Co-Receptors;66
7.3.9;3.9 Adaptation, Alternative Receptors, Tropism, and Pathogenicity;67
7.3.9.1;3.9.1 FMDV and Other Integrin-Binding Viruses;67
7.3.9.2;3.9.2 Major Group Human Rhinoviruses and Ig-Like Receptor-Binding Viruses;68
7.3.9.3;3.9.3 TMEV Pathogenesis;68
7.3.9.4;3.9.4 CD155/PVR as a Factor in Poliovirus Pathogenesis;68
7.4;4 Endocytosis and Sites of Uncoating;69
7.4.1;4.1 Clathrin-Mediated Endocytosis;70
7.4.1.1;4.1.1 Aphthoviruses;70
7.4.1.2;4.1.2 Minor Group Human Rhinoviruses;71
7.4.1.3;4.1.3 Major Group Human Rhinoviruses;72
7.4.1.4;4.1.4 Other Picornaviruses;73
7.4.1.5;4.1.5 Role of Endosomal pH;73
7.4.2;4.2 Caveolin-Mediated Endocytosis: Coxsackie and Echoviruses;75
7.4.2.1;4.2.1 Echovirus 1;75
7.4.2.2;4.2.2 Coxsackie B3: Role of Co-Receptors;76
7.4.3;4.3 Noncaveolin Nonclathrin Mediated Endocytosis: Poliovirus;77
7.4.4;4.4 Concluding Remarks on Picornavirus Endocytosis;78
7.5;5 Capsid Alterations During Uncoating;79
7.5.1;5.1 Enteroviruses;79
7.5.2;5.2 Aphthoviruses;85
7.6;6 Membrane Penetration;86
7.6.1;6.1 Review of Experimental Data;86
7.6.1.1;6.1.1 Interaction of Altered Particles with Membranes;86
7.6.1.2;6.1.2 Virus-Induced Membrane Permeability;86
7.6.1.3;6.1.3 Role of Externalized N-Terminus of VP1;87
7.6.1.4;6.1.4 Role for Released VP4;87
7.6.1.5;6.1.5 How Much VP4 Is Released During Picornavirus Entry?;88
7.6.2;6.2 Models for Entero/Rhinovirus Membrane Penetration;88
7.6.3;6.3 Membrane Penetration by Other Picornaviruses;89
7.6.4;6.4 Questions Remaining on Membrane Penetration;90
7.7;7 Overall Conclusions;90
7.8;References;91
8;From Touchdown to Transcription: The Reovirus Cell Entry Pathway;104
8.1;1 Introduction;105
8.2;2 Structural Analysis of Reovirus Virions and Attachment Protein sigma1;106
8.3;3 Reovirus Attachment Is Mediated by Cell-Surface Sialic Acid and Junctional Adhesion Molecule-A;109
8.4;4 Internalization of Reovirus Virions into the Endocytic Pathway Is Mediated by beta1 Integrins;111
8.5;5 Removal of Outer-Capsid Protein sigma3 by Cathepsin Proteases Initiates the Reovirus Disassembly Cascade;114
8.6;6 Penetration of Endosomal Membranes by Reovirus Is Mediated by Outer-Capsid Protein mu1;116
8.7;7 Reovirus Entry Evokes Innate Immune Responses that Trigger Cell Death;120
8.8;8 Conclusions and Future Directions;122
8.9;References;125
9;Rotavirus Cell Entry;133
9.1;1 Introduction;134
9.2;2 Rotavirus Structure;136
9.2.1;2.1 VP4 Spikes;138
9.2.2;2.2 Proteolytic Fragments of VP4;138
9.2.3;2.3 VP8* Structure;138
9.2.4;2.4 VP5* Structure;139
9.2.5;2.5 Oligomeric State of VP4;140
9.2.6;2.6 VP7 Capsid Layer;140
9.2.7;2.7 VP6 Layer;142
9.2.8;2.8 VP2 Layer and the Transcription Enzyme Complex;143
9.3;3 Cell Entry;143
9.3.1;3.1 Proteolytic Priming;143
9.3.2;3.2 Endocytosis or Direct Penetration;144
9.3.3;3.3 Membrane Permeabilization;145
9.3.4;3.4 Uncoating;146
9.3.5;3.5 Rotavirus Receptors;147
9.4;4 Structural Insights into Cell Entry;149
9.4.1;4.1 Trypsin-Induced Order-to-Disorder Transformation in VP4;150
9.4.2;4.2 Initial Cell Attachment: VP8*-SA Interactions;151
9.4.3;4.3 Entry-Related Structural Gymnastics of the VP4 Spike;152
9.5;5 Conclusions;153
9.6;References;154
10;Structures and Functions of Parvovirus Capsids and the Process of Cell Infection;161
10.1;1 Parvoviruses: Capsid Structures, Assembly and DNA Packaging;162
10.2;2 Dynamic Properties of the Parvovirus Capsid Structure and Cell Infection;167
10.3;3 Receptor Binding, Structural Effects, and Internalization from the Cell Surface;170
10.3.1;3.1 Binding Site Insertion and Retargeting;171
10.3.2;3.2 Receptor Binding and Effects on Capsid Structure;173
10.4;4 Antibody Binding and Capsid Structures and Functions;173
10.5;5 Endosomal Uptake, Signaling, and Infection;175
10.5.1;5.1 Trafficking Within the Endosomal System;176
10.5.2;5.2 Low pH and Virus Infection;177
10.5.3;5.3 Capsid Structural Changes and Endosomal Escape;177
10.6;6 Viral Trafficking in the Cytoplasm;178
10.7;7 Nuclear Trafficking and DNA Release;179
10.8;8 Summary and Future Challenges;181
10.9;References;182
11;Cellular Entry of Polyomaviruses;189
11.1;1 Introduction;190
11.2;2 Engaging the Host Cell Receptor;192
11.3;3 Trafficking to the ER;194
11.4;4 Penetration Across the ER Membrane;198
11.5;5 Nuclear Entry and Genome Release;201
11.6;6 Perspectives;202
11.7;References;202
12;Adenovirus;207
12.1;1 Structural Features of Adenovirus;208
12.2;2 Adenovirus Receptor Interactions;210
12.2.1;2.1 Interactions with the Coxsackie and Adenovirus Receptor;211
12.2.2;2.2 Interactions with CD46;212
12.2.3;2.3 Interactions with Sialic Acid;213
12.2.4;2.4 Alternative Routes of Adenovirus Attachment to Cells;213
12.3;3 Adenovirus Internalization;214
12.4;4 Uncoating of Adenovirus Particles;216
12.4.1;4.1 Vertex Dissociation from the Adenovirus Capsid;217
12.4.2;4.2 Adenovirus Uncoating in the Endosome;219
12.4.3;4.3 Identification of Membrane Lytic Factors of Adenovirus;220
12.4.4;4.4 Role of Acidic pH in Adenovirus Entry;223
12.4.5;4.5 Role of the Encapsidated Adenovirus Protease in Entry;226
12.4.6;4.6 Uncoating at the Nuclear Pore Complex;226
12.4.7;4.7 The Impact of the Immune System on Uncoating;227
12.5;5 Conclusions;227
12.6;References;228
13;Index;237



Ihre Fragen, Wünsche oder Anmerkungen
Vorname*
Nachname*
Ihre E-Mail-Adresse*
Kundennr.
Ihre Nachricht*
Lediglich mit * gekennzeichnete Felder sind Pflichtfelder.
Wenn Sie die im Kontaktformular eingegebenen Daten durch Klick auf den nachfolgenden Button übersenden, erklären Sie sich damit einverstanden, dass wir Ihr Angaben für die Beantwortung Ihrer Anfrage verwenden. Selbstverständlich werden Ihre Daten vertraulich behandelt und nicht an Dritte weitergegeben. Sie können der Verwendung Ihrer Daten jederzeit widersprechen. Das Datenhandling bei Sack Fachmedien erklären wir Ihnen in unserer Datenschutzerklärung.