E-Book, Englisch, Band 343, 230 Seiten
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
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




