Download or read book Identification and Characterization of the Protein Encoded by Gene UL49A of Herpes Simplex Virus Type 1 and Investigation of Its Role in the Virus Life Cycle written by Ralph Adams (Ph.D.) and published by . This book was released on 1999 with total page 221 pages. Available in PDF, EPUB and Kindle. Book excerpt:
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:
Download or read book Characterization of the Herpes Simplex Virus Type 1 Virion Host Shutoff Protein written by Bradley M. Karr and published by . This book was released on 1994 with total page 224 pages. Available in PDF, EPUB and Kindle. Book excerpt:
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:
Download or read book Identification and Characterization of Cis acting Elements Upstream of Herpes Simplex Virus Type 1 GC TATA Box written by Chin-Cheng Huang and published by . This book was released on 1998 with total page 336 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book The Role of Tegument Proteins and the Dynamic Interplay They Have with One Another Throughout the Course of Herpes Simplex Virus Type 1 Infections written by Ekaette Francis Mbong and published by . This book was released on 2012 with total page 169 pages. Available in PDF, EPUB and Kindle. Book excerpt: Herpes simplex virus type 1 (HSV-1) is a neurotropic virus affecting up to 98% of the adult population. Central to this report is the proteinaceous layer termed the tegument found within the HSV-1 virion. The tegument is composed of>20 different viral proteins of varying stoichiometries. Tegument proteins are delivered to the host cell upon infection, providing this virus an advantage early in its replication cycle. Tegument proteins also function at late times in infection when they are synthesized at high levels. One of the most abundant tegument proteins is VP22, encoded by the U_L 49 gene, with over 2000 copies per virion. The studies described herein provided much insight into how VP22 promotes the HSV-1 replication cycle. We found the absence of VP22 during infection resulted in decreased mRNA levels at early times and decreased protein synthesis at late times. These results were distinct and separable with respect to both the genes affected and the timing during infection. Because U_L 49^- infections often result in secondary, compensatory mutations in the gene encoding vhs, we examined the effects of one such mutation as well as the role of vhs's RNase activity on protein synthesis in the presence and absence of VP22. Our results indicated secondary mutations that decreased vhs's RNase activity compensated for the lack of VP22 during HSV-1 infections. Further analyses indicated the absence of VP22 resulted in decreased translation efficiency independent of mRNA abundance, the result of cleavage of the 5' UTRs of viral mRNAs. In separate studies we focused on the tegument protein encoded by the U_L21 gene. Although much is known about the role of this protein at late times in infection, very little was known about its role at early times in HSV-1 infections. We found the absence of pUL21 resulted in decreased levels of several immediate early mRNAs, and their corresponding proteins, at early times in infection. Although HSV-1 establishes a persistent infection, and is therefore incurable, we have made several novel findings that contribute important knowledge to the herpesvirus field and will hopefully aid in the development of new therapeutics.
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.
Download or read book Analysis of the Intranuclear Localization of Essential Herpes Simplex Virus Type 1 Replication Proteins written by Christopher Joseph Lukonis and published by . This book was released on 1998 with total page 462 pages. Available in PDF, EPUB and Kindle. Book excerpt:
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:
Download or read book Index to Theses with Abstracts Accepted for Higher Degrees by the Universities of Great Britain and Ireland and the Council for National Academic Awards written by and published by . This book was released on 2000 with total page 786 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book The Identification and Characterization of the Bovine Virus Type 1 E1 Protein written by Shaw Sun and published by . This book was released on 1990 with total page 122 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Interactions Between the Tegument Proteins UL11 and UL16 and the Glycoprotein E of Herpes Simplex Virus written by Pei-Chun Yeh and published by . This book was released on 2009 with total page 202 pages. Available in PDF, EPUB and Kindle. Book excerpt: The herpesvirus tegument region present between the virion envelope and the nucleocapsid contains more than 20 different virus-encoded proteins. The process of tegument assembly and final envelopment has been unfoldeding over the past few decades. It is thought that a few tegument proteins are added to the capsid in the nucleus, whereas most of them are acquired after entering the cytoplasm or traveling to the site of final envelopment at the trans-Golgi network. Overall, the research presented in this dissertation provides insights into the molecular mechanism of protein-protein interactions that may be involved in (or contribute to) assembly and maturation of herpes simplex virus type 1 (HSV-1). The UL11 (membrane-bound) and UL16 (capsid-associated) tegument proteins are conserved among all herpesviruses, and interaction between the two has been implicated in linking the viral capsid, tegument, and membrane during final envelopment process. Both in transfected and virus-infected cells, a subpopulation of the UL11 protein was found associated with detergent-resistant membranes via modifications with two fatty- acid chains (myristate and palmitate). UL11 can directly interact with UL16 in a manner dependent on the acidic cluster and leucine-isoleucine motifs of UL11. And, N-ethylmaleimide-modified UL16 was found to be incapable of binding UL11, suggesting that free cysteines in UL16 somehow play a role in the interaction. UL16 is stably associated with cytoplasmic capsids isolated from infected cells. In response to initial attachment of virus to the cell surface, an 'outside-in' signal is transmitted across the virion membrane, and as a result, UL16 is dissociated from the capsid. The mechanism by which the signal is sent to UL16 remains unclear but seems likely to be mediated by the glycoproteins on the virion envelope. A GST chimera bearing the cytoplasmic tail of glycoprotein E (gE. CT) was found to be capable of binding UL16 expressed in mammalian or insect cells. To better understand the molecular mechanism of this signaling process, the interaction network emanating from UL16 was investigated. In addition, previously using a GST pull-down assay, it was observed that UL16 interacts with virus-specific proteins from HSV- and PRV-infected cell lysates, providing evidence that UL16 is present in protein complexes. To characterize native complexes that contain UL16, a recombinant virus was constructed expressing a tagged derivative. Using the combination of tandem affinity purification and mass spectrometry analysis, we identified gE to be present in the complexes isolated from infected cells. The UL16-gE interaction was confirmed in co-immunoprecipitation assays with infected cell lysates. Moreover, mutational analyses of gE. CT have suggested that in infected cells UL16 may interact with gE. CT in both UL11-dependent and -independent manners. Based on all available data, we hypothesize that UL11, UL16, and gE may form a tripartite complex which plays a role in multiple aspects of the virus life cycle, including signaling events during virus attachment, virion maturation, or cell-to-cell spread. Collectively, our research focused on the protein-protein network has built a foundation for future studies, and also advanced our current knowledge of herpesvirus replication.
Download or read book Characterization and Packaging of the Herpes Simplex Type 1 Virion Host Shutoff Protein written by Mary Patterson and published by . This book was released on 1997 with total page 288 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book The Role of the Herpes Simplex Virus Type 1 Alkaline Nuclease in Processing DNA Replication Intermediates written by Joshua Norkin Goldstein and published by . This book was released on 2000 with total page 482 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Identification and Characterization of a Herpes Simplex Virus Type 1 HSV 1 specific Cytotoxic T Lymophocyte Epitope Within the HSV 1 Ribonucleotide Reductase Large Subunit written by Lisa Anne Salvucci and published by . This book was released on 1994 with total page 188 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Identification of Cellular Factors Involved in Herpes Simplex Virus Type 1 Nucelar Egress written by Martina Maric and published by . This book was released on 2012 with total page 134 pages. Available in PDF, EPUB and Kindle. Book excerpt: The herpesvirus life cycle involves a step where newly formed capsids leave the nucleus by translocating across the intact nuclear envelope (NE). Little is known about the role of cellular factors during nuclear egress. We sought to identify novel cellular proteins that interact with the conserved herpes simplex virus-1 (HSV-1) pUL34 by performing a yeast two-hybrid screen. pUL34 was chosen due to its crucial and multifunctional role during nuclear egress. From 42 cellular factors that interacted with pUL34 in yeast, twelve were further evaluated in mammalian cells by co-localization studies using immunofluorescence. No specific co-location between the tested cellular factors and pUL34 was observed in infected cells, thus the screen failed to convincingly identify novel pUL34 interactors.
Download or read book Cumulated Index Medicus written by and published by . This book was released on 1989 with total page 1272 pages. Available in PDF, EPUB and Kindle. Book excerpt:
