DNA virus replication /

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Bibliographic Details
Imprint:Oxford ; New York : Oxford University Press, c2000.
Description:xvi, 232 p. : ill. ; 25 cm.
Language:English
Series:Frontiers in molecular biology ; 26
Subject:
Format: E-Resource Print Book
URL for this record:http://pi.lib.uchicago.edu/1001/cat/bib/4562750
Hidden Bibliographic Details
Other authors / contributors:Cann, Alan.
ISBN:019963713X (hbk.)
0199637121 (pbk.)
Notes:Includes bibliographical references and index.
Table of Contents:
  • List of contributors
  • Abbreviations
  • 1. Macromolecular interactions in hepatitis B virus replication and particle assembly
  • 1.. Introduction
  • 2.. The HBV infectious cycle
  • 3.. Experimental systems to study HBV replication
  • 3.1. Animal models
  • 3.2. Transfection of cloned hepadnavirus DNA
  • 3.3. Reconstituting hepadnavirus reverse transcription in vitro
  • 4.. Assembly of virus particles
  • 4.1. Envelope containing particles
  • 4.2. The nucleocapsid
  • 5.. The enigma of HBx
  • 6.. Conclusions and perspectives
  • Acknowledgements
  • References
  • 2. Protein-protein interactions in papillomavirus replication
  • 1.. Introduction
  • 2.. Early HPV proteins
  • 2.1. HPV-16 E6
  • 2.2. HPV-16 E7
  • 2.3. HPV-16 E5
  • 2.4. Summary of the roles of E6, E7, and E5 in keratinocyte differentiation and cell cycle control
  • 3.. Viral proteins involved in viral DNA replication
  • 3.1. E1 and E2 proteins
  • 3.2. Maintenance and amplification of HPV genomes
  • 4.. Summary
  • Acknowledgments
  • References
  • 3. Molecular interactions in herpes simplex virus DNA replication
  • 1.. Introduction
  • 2.. Identification of the cis-acting signals and trans-acting proteins involved in HSV-1 DNA synthesis
  • 3.. Models for HSV-1 DNA replication
  • 4.. Molecular interactions involved in HSV-1 DNA synthesis
  • 5.. Interactions involved in unwinding the replication origins
  • 5.1. ICP8
  • 5.2. HSV-1 DNA replication origins
  • 5.3. Interaction of UL9 with the viral origins
  • 5.4. DNA helicase activity of UL9 and interaction with ICP8
  • 5.5. Unwinding of the replication origins
  • 5.6. Regulation of origin activity
  • 6.. Interactions involved in the initiation of DNA synthesis
  • 6.1. The helicase--primase complex
  • 6.2. Effect of ICP8 on the helicase--primase complex
  • 6.3. The HSV-1 DNA polymerase holoenzyme
  • 6.4. Interaction between UL8 and UL9
  • 6.5. Interactions of the HSV-1 DNA polymerase with UL8 and UL9
  • 6.6. Interaction of host DNA polymerase [alpha] with UL9
  • 7. A model for the establishment of the HSV-1 replication fork
  • 8. Other interactions involving HSV-1 ICP8
  • 9.. Intranuclear localization of HSV-1 DNA synthesis
  • 10.. Concluding remarks
  • References
  • 4. Epstein--Barr virus proteins involved in cell immortalization
  • 1.. Introduction
  • 2.. The nuclear proteins expressed in EBV-transformed B cells
  • 2.1. The EBV nuclear antigen-1, EBNA1
  • 2.2. The EBV nuclear antigen-2, EBNA2
  • 2.3. The EBV leader protein, EBNA-LP
  • 2.4. The EBV nuclear antigen-3 family, EBNA3A, EBNA3B, and EBNA3C
  • 3.. Latent membrane proteins expressed in EBV-transformed B cells
  • 3.1. The latent membrane protein-1, LMP1
  • 3.2. The latent membrane protein-2, LMP2
  • 4.. Conclusions
  • References
  • 5. Molecular piracy by KSHV: a strategy of live and let live
  • 1.. Introduction
  • 2.. KSHV as a model for molecular piracy
  • 3.. Immunomodulatory proteins encoded by KSHV
  • 3.1. Viral interleukin-6 (vIL-6)
  • 3.2. Viral macrophage inflammatory proteins (vMIPs)
  • 3.3. Viral G protein-coupled receptor (vGCR)
  • 3.4. Viral interferon regulatory factor (vIRF)
  • 4.. KSHV proteins affecting the cell cycle and apoptosis
  • 4.1. Viral cyclin (v-Cyc)
  • 4.2. Viral Bcl-2 (vBcl-2)
  • 4.3. Viral FLIP (vFLIP)
  • 5.. Novel ORFs encoded by KSHV
  • 5.1. ORF K1
  • 5.2. Kaposin
  • 6.. Conclusions
  • Acknowledgements
  • References
  • 6. Cellular sites and mechanisms of human cytomegalovirus latency
  • 1.. Introduction
  • 2.. Cells of the myeloid lineage are an important site of carriage of HCMV
  • 3.. Viral gene expression associated with latency
  • 4.. Permissiveness of peripheral blood cells for HCMV infection requires differentiation
  • 5.. Bone marrow--a reservoir of virus in the healthy carrier
  • 6.. Conditionally permissive cell lines as models for factors controlling latency and reactivation
  • 7.. Many cell types are infected during viraemia--does this reflect other sites of latency?
  • 8.. Conclusions
  • Acknowledgements
  • References
  • 7.. Control of transcription by adenovirus-E1A proteins
  • 1.. Introduction
  • 2.. The adenovirus E1A proteins
  • 3.. Transcriptional regulation
  • 3.1. Regulation of transcription initiation
  • 4.. Binding of E1A to the retinoblastoma and related proteins
  • 4.1. Effect of pocket proteins on E2F
  • 4.2. Binding of pRb to other cellular proteins
  • 5.. Binding of E1A to p300 and related proteins
  • 5.1. Role of p300/CBP in transcription regulation
  • 5.2. The intrinsic and associated acetyltransferase activity of p300/CBP
  • 5.3. Role of p300/CBP in cell growth and differentiation
  • 5.4. Role of the individual p300/CBP members
  • 6.. Other proteins associating with E1A
  • Acknowledgements
  • References
  • 8.. Adenovirus proteins that regulate apoptosis
  • 1.. Introduction
  • 2.. Course of adenovirus infection
  • 3.. E3-coded proteins that inhibit immune-mediated apoptosis
  • 4.. Induction of apoptosis by E1A
  • 5.. Inhibition of apoptosis by the E1B-19K protein
  • 6.. Inhibition of apoptosis by the E1B-55K protein
  • 7.. Apoptosis regulation by E4 proteins
  • 8.. Inhibition of the antiviral effects of interferons
  • 9.. Induction of cell lysis and virus release by the adenovirus death protein (ADP)
  • 10.. Concluding remarks
  • Acknowledgements
  • References
  • Index