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Book Identification and Characterization of the UL37 Protein of Herpes Simplex Virus Type 1 and Demonstration that it Interacts with ICP8  the Major DNA Binding Protein of Herpes Simplex Virus

Download or read book Identification and Characterization of the UL37 Protein of Herpes Simplex Virus Type 1 and Demonstration that it Interacts with ICP8 the Major DNA Binding Protein of Herpes Simplex Virus written by Lisa S. G. Shelton and published by . This book was released on 1992 with total page 218 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Further Characterization of the UL37 Protein of Herpes Simplex Virus Type 1 and Its Interaction with ICP8  the Major DNA binding Protein of Herpes Simplex Virus

Download or read book Further Characterization of the UL37 Protein of Herpes Simplex Virus Type 1 and Its Interaction with ICP8 the Major DNA binding Protein of Herpes Simplex Virus written by Allen G. Albright and published by . This book was released on 1994 with total page 222 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Characterization of the Herpes Simplex Virus 1 DNA Polymerase and Its Interaction with UL42 Protein and ICP8  and Mutational Analysis of a Viral Origin of Replication

Download or read book Characterization of the Herpes Simplex Virus 1 DNA Polymerase and Its Interaction with UL42 Protein and ICP8 and Mutational Analysis of a Viral Origin of Replication written by Thomas R. Hernandez and published by . This book was released on 1993 with total page 440 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Functional Significance of the Physical Interaction Between the Herpes Simplex Virus Type 1 Origin binding Protein  UL9  and the DNA Polymerase Processivity Factor  UL42

Download or read book Functional Significance of the Physical Interaction Between the Herpes Simplex Virus Type 1 Origin binding Protein UL9 and the DNA Polymerase Processivity Factor UL42 written by Kelly S. Trego and published by . This book was released on 2003 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: Abstract: The origin (ori)-binding protein of herpes simplex virus type 1 (HSV-1), encoded by the UL9 open-reading frame, has been shown to physically interact with a number of cellular and viral proteins, including three HSV-1 proteins (ICP8, UL42, and UL8) essential for ori-dependent DNA replication. In this report, it is demonstrated for the first time that the DNA polymerase processivity factor, UL42 protein, provides accessory function to the UL9 protein, by enhancing the 3' to 5' helicase activity of UL9 on partially duplex non-specific DNA substrates. UL42 fails to enhance the unwinding activity of a non-cognate helicase, suggesting enhancement of unwinding requires the physical interaction between UL42 and UL9. UL42 increases the steady-state rate for unwinding a 23/38-mer by UL9, but only at limiting UL9 concentrations, consistent with a role in increasing the affinity of UL9 for DNA. Optimum enhancement of unwinding was observed at UL42:UL9 molecular ratios of 4:1, although enhancement was reduced when high ratios of UL42:DNA were present. Under the assay conditions employed, UL42 did not alter the rate of dissociation of UL9 from the DNA substrate. UL42 also did not alter the requirement or time for an assembly/conformational change step, regardless of whether it was added to DNA prior to or at the same time as UL9, or after steady-state unwinding by UL9 alone had been achieved. Thus, the increased affinity of UL9 for DNA most likely is the result of an increase in the association rate constant for binding of UL9 to DNA, and explains why helicase enhancement is observed only at subsaturating concentrations of UL9 with respect to DNA. Consistent with this interpretation are results which demonstrate that UL42 also enhances the ATPase activity of UL9 on single-strand and partially duplex DNA substrates when UL9 is limiting. In contrast, ICP8 enhances unwinding at both saturating and subsaturating UL9 concentrations, and reduces or eliminates the lag period. The different means by which ICP8 and UL42 enhance activities of UL9 suggest that these two members of the presumed functional replisome may act synergistically on UL9 to effect initiation of HSV-1 DNA replication in vivo.

Book Herpes Simplex Virus 1 DNA Packaging

Download or read book Herpes Simplex Virus 1 DNA Packaging written by Ying Fan and published by . This book was released on 1997 with total page 192 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Dissertation Abstracts International

Download or read book Dissertation Abstracts International written by and published by . This book was released on 1994 with total page 700 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Identification and Charaterization of Protein Interaction Domains in the Herpes Simplex Virus Type 1 Transcription Factor ICP4

Download or read book Identification and Charaterization of Protein Interaction Domains in the Herpes Simplex Virus Type 1 Transcription Factor ICP4 written by James William Bruce and published by . This book was released on 2002 with total page 240 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Structure function Analysis of the Herpes Simplex Virus Type 1 Origin Binding Protein  UL9

Download or read book Structure function Analysis of the Herpes Simplex Virus Type 1 Origin Binding Protein UL9 written by Ajay Kumar Malik and published by . This book was released on 1996 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Cumulated Index Medicus

Download or read book Cumulated Index Medicus written by and published by . This book was released on 1993 with total page 1488 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Book Isolation of Host Proteins Involved in Herpes Simplex Virus Type 1 DNA Synthesis

Download or read book Isolation of Host Proteins Involved in Herpes Simplex Virus Type 1 DNA Synthesis written by Whitney Cogswell and published by . This book was released on 2008 with total page 49 pages. Available in PDF, EPUB and Kindle. Book excerpt: Abstract: Herpes simplex virus type 1 (HSV-1) is the prototypic member of a large family of viruses known as Herpesviridae. Herpesviruses possess a double-stranded DNA genome and infect a broad range of species. In addition to HSV-1, there are seven other herpesviruses that are known to infect humans. Although antiviral treatment is available for HSV infections, there are few or no options for treatment of infections by other herpesviruses. One of the best targets for development of new antivirals is the viral DNA replication apparatus. HSV-1 encodes for seven proteins directly involved in viral DNA replication. However, no HSV-1 origin-dependent DNA replication has been reconstituted in vitro using purified viral proteins. It is hypothesized that proteins (host and/or viral) in addition to the seven known viral DNA replication proteins are involved in viral DNA replication in vivo. Moreover, it is predicted that such proteins would interact with one or more of the viral DNA replication proteins. In an effort to identify interacting host proteins, co-immunoprecipitation analysis was performed using antibodies specific for an essential HSV DNA replication protein, UL42, the polymerase processivity factor. Extracts from infected and mock-infected cells were immunoprecipitated with the UL42 antibody. UL42, and all that is bound to it, bind to the antibody which binds to the Protein G agarose matrix. Those proteins that are specifically pulled down from infected cell extracts, but not from mock-infected extracts, were to be identified by mass-spectrometry. The immunoprecipitates were analyzed following separation on denaturing polyacrylamide gels. Gels were silver-stained or analyzed for the presence of UL42 using a Western blot. Conditions were adjusted to optimize the amount of UL42 immunoprecipitated, but UL42 could not be immunoprecipitated quantitatively. Following immunoprecipitation under optimum conditions, no differences were observed between the proteins pulled-down from mock- or infected-cell extracts. Due to the poor ability of the antibody to pull-down UL42, a second approach was employed. A histidine-tagged version of UL42 was purified using a nickel chelating column and then mixed with infected or mock-infected cell extracts. Those proteins that specifically interact with his-UL42 were expected to bind to a nickel column. However, nonspecific interactions with the matrix were observed and prevented identification of proteins by mass-spectrometry.

Book Glycoprotein M and ESCRT in Herpes Simplex Virus Type 1 Assembly

Download or read book Glycoprotein M and ESCRT in Herpes Simplex Virus Type 1 Assembly written by Yudan Ren and published by . This book was released on 2012 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: Herpes simplex virus type 1 (HSV-1) has a large linear double-stranded DNA genome in an icosahedral capsid shell, a cell-derived lipid envelope and a proteinaceous tegument layer. There are over fifty viral proteins and many host proteins identified in HSV-1 virions. The final formation of mature virus particles requires the membrane wrapping of tegumented capsids in the cytoplasm, a process termed secondary envelopment. This process involves the coordination of numerous viral and cellular proteins and results in double-membrane structures with enveloped virions contained within cellular vesicles. Mature viruses are then released through the fusion of these virion-containing vesicles and plasma membranes. This thesis describes investigation into the functions of viral glycoprotein M (gM) and the cellular Endosomal Sorting Complexes Required for Transport (ESCRT) in secondary envelopment. Firstly, it has been reported that gH/L can be efficiently internalised and targeted to the TGN by the co-expression of gM in transfection assays. In order to examine the role of gM in guiding the localisation of viral proteins in infected cells, a HSV-1 gM deletion virus (∆gM), and its revertant virus were constructed. The major phenotype demonstrated was that the absence of gM caused the internalisation of cell surface gH/L to be inhibited and higher levels of gH/L to be observed on the cell surface. Further, lower levels of gH/L were detected in purified ∆gM virions, which was in agreement with the delayed entry kinetics, smaller plaque sizes and greater replication deficits at low multiplicity of infection observed in ∆gM infected cells. Over all the results presented in this thesis demonstrate that in infected cells the efficient incorporation of gH/L into virions relies on the function of gM in HSV-1. Secondly, during HSV-1 secondary envelopment the budding and scission of the viral envelope from the host membrane share topological similarities with the formation of intraluminal vesicle in multivesicular bodies, retrovirus budding, and abscission at the end of cytokinesis, processes that require the cellular ESCRT machinery. There are four multiprotein ESCRT complexes and many associated proteins involved in their regulation. It has been previously shown that the ESCRT-III complex and a functional ATPase VPS4 are required for HSV-1 secondary envelopment, but different from the strategy utilised by HIV-1, the recruitment of ESCRT during HSV-1 infection is independent of TSG101 and/or ALIX. Data presented in this thesis demonstrate that CHMP4A/B/C proteins of the ESCRT-III complex are specifically crucial for HSV-1 secondary envelopment. Simultaneous depletion of CHMP4A/B/C proteins significantly inhibited HSV-1 replication. Ultrastructure analysis revealed that there were virtually no extracellular virions in CHMP4A/B/C depleted samples while more free capsids were observed in the cytoplasm, although the nuclear capsids and primary envelopment events appeared to be normal. In order to identify interactions between HSV-1 and ESCRT proteins, 22 HSV-1 tegument proteins were cloned and tested against a panel of ESCRT and ESCRT-associated proteins in yeast two-hydrid assays. Analysis of positive hits from yeast two-hybrid interaction screens using GST pull-down, co-immunoprecipitation and protein co-localisation assays have validated interactions of pUL47 with CC2D1A/1B, CIN85, CHMP6 and ALIX, pUL46 and pUL49 with CC2D1A/1B and CIN85, and pUL16 with CC2D1A/1B. Furthermore, the newly identified ESCRT associated proteins CC2D1A and CC2D1B have been detected in purified virions. The role of the identified ESCRT proteins in HSV-1 replication has been investigated using siRNA depletion. Unfortunately siRNA depletions of the various ESCRT candidates individually or in combinations did not show any significant effect on HSV-1 replication. Overall these data suggest that unlike HIV and other retroviruses, HSV-1 has evolved multiple parallel pathways to hijack the ESCRT machinery to facilitate its replication, particularly, through the interactions that lead directly to the recruitment of CHMP4A/B/C proteins. Disruption of some of these pathways did not prevent HSV-1 replication in tissue culture, suggesting any one potential pathway is sufficient for ESCRT recruitment to sites of HSV-1 assembly.

Book Human Herpesviruses

    Book Details:
  • Author : Ann Arvin
  • Publisher : Cambridge University Press
  • Release : 2007-08-16
  • ISBN : 1139461648
  • Pages : 1325 pages

Download or read book Human Herpesviruses written by Ann Arvin and published by Cambridge University Press. This book was released on 2007-08-16 with total page 1325 pages. Available in PDF, EPUB and Kindle. Book excerpt: This comprehensive account of the human herpesviruses provides an encyclopedic overview of their basic virology and clinical manifestations. This group of viruses includes human simplex type 1 and 2, Epstein–Barr virus, Kaposi's Sarcoma-associated herpesvirus, cytomegalovirus, HHV6A, 6B and 7, and varicella-zoster virus. The viral diseases and cancers they cause are significant and often recurrent. Their prevalence in the developed world accounts for a major burden of disease, and as a result there is a great deal of research into the pathophysiology of infection and immunobiology. Another important area covered within this volume concerns antiviral therapy and the development of vaccines. All these aspects are covered in depth, both scientifically and in terms of clinical guidelines for patient care. The text is illustrated generously throughout and is fully referenced to the latest research and developments.

Book Recombinant Virus Vaccines

Download or read book Recombinant Virus Vaccines written by Maureen C. Ferran and published by Humana. This book was released on 2018-06-09 with total page 273 pages. Available in PDF, EPUB and Kindle. Book excerpt: This volume provides readers with methods and protocols for understanding the development of recombinant viruses and their use as vaccines platforms. Recombinant Virus Vaccines: Methods and Protocols details the use of recombinant vaccines that are employed to either produce immunogens in vitro or elicit antibody production in vivo. The chapters in this book are divided into four parts: Part I explores double-stranded DNA viruses; Part II discusses negative sense single-stranded RNA viruses; Part III talks about positive sense single-stranded RNA viruses; and Part IV describes bacteriophages. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Thorough and cutting-edge, Recombinant Virus Vaccines: Methods and Protocols is a valuable resource for scientists and clinicians who are interested in learning about and adopting methods for use in basic and biomedical research directed toward generating and developing recombinant viral vaccines.