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Relevant bibliographies by topics / Foamy virus

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Academic literature on the topic 'Foamy virus'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Foamy virus"

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Juretzek, Thomas, Teresa Holm, Kathleen Gärtner, Sylvia Kanzler, Dirk Lindemann, Ottmar Herchenröder, Marcus Picard-Maureau, Matthias Rammling, Martin Heinkelein, and Axel Rethwilm. "Foamy Virus Integration." Journal of Virology 78, no. 5 (March 1, 2004): 2472–77. http://dx.doi.org/10.1128/jvi.78.5.2472-2477.2004.

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ABSTRACT It had been suggested that during integration of spumaretroviruses (foamy viruses) the right (U5) end of the cDNA is processed, while the left (U3) remains uncleaved. We confirmed this hypothesis by sequencing two-long terminal repeat (LTR) circle junctions of unintegrated DNA. Based on an infectious foamy virus molecular clone, a set of constructs harboring mutations at the 5′ end of the U3 region in the 3′ LTR was analyzed for particle export, reverse transcription, and replication. Following transient transfection some mutants were severely impaired in generating infectious virus, while others replicated almost like the wild type. The replication competence of the mutants was unrelated to the cleavability of the newly created U3 end. This became obvious with two mutants both belonging to the high-titer type. One mutant containing a dinucleotide artificially transferred from the right to the left end was trimmed upon integration, while another one with an unrelated dinucleotide in that place was not. The latter construct in particular showed that the canonical TG motif at the beginning of the provirus is not essential for foamy virus integration.

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Russell, D. W., and A. D. Miller. "Foamy virus vectors." Journal of virology 70, no. 1 (1996): 217–22. http://dx.doi.org/10.1128/jvi.70.1.217-222.1996.

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Kretzschmar, Benedikt, Ali Nowrouzi, Maximilian J. Hartl, Kathleen Gärtner, Tatiana Wiktorowicz, Ottmar Herchenröder, Sylvia Kanzler, et al. "AZT-resistant foamy virus." Virology 370, no. 1 (January 2008): 151–57. http://dx.doi.org/10.1016/j.virol.2007.08.025.

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Deyle, David R., Yi Li, Erik M. Olson, and David W. Russell. "Nonintegrating Foamy Virus Vectors." Journal of Virology 84, no. 18 (June 30, 2010): 9341–49. http://dx.doi.org/10.1128/jvi.00394-10.

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ABSTRACT Foamy viruses (FVs), or spumaviruses, are integrating retroviruses that have been developed as vectors. Here we generated nonintegrating foamy virus (NIFV) vectors by introducing point mutations into the highly conserved DD35E catalytic core motif of the foamy virus integrase sequence. NIFV vectors produced high-titer stocks, transduced dividing cells, and did not integrate. Cells infected with NIFV vectors contained episomal vector genomes that consisted of linear, 1-long-terminal-repeat (1-LTR), and 2-LTR circular DNAs. These episomes expressed transgenes, were stable, and became progressively diluted in the dividing cell population. 1-LTR circles but not 2-LTR circles were found in all vector stocks prior to infection. Residual integration of NIFV vectors occurred at a frequency 4 logs lower than that of integrase-proficient FV vectors. Cre recombinase expressed from a NIFV vector mediated excision of both an integrated, floxed FV vector and a gene-targeted neo expression cassette, demonstrating the utility of these episomal vectors. The broad host range and large packaging capacity of NIFV vectors should make them useful for a variety of applications requiring transient gene expression.

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Fischer, Nicole, Martin Heinkelein, Dirk Lindemann, Jörg Enssle, Christopher Baum, Evelyn Werder, Hanswalter Zentgraf, Justus G. Müller, and Axel Rethwilm. "Foamy Virus Particle Formation." Journal of Virology 72, no. 2 (February 1, 1998): 1610–15. http://dx.doi.org/10.1128/jvi.72.2.1610-1615.1998.

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ABSTRACT Subgenomic expression plasmids for the so-called human foamy virus (HFV) structural gag, gag/pol, and env genes were constructed and used to analyze foamy virus particle formation by electron microscopy. Expression of an R-U5-gag-pol construct under control of the human cytomegalovirus immediate-early enhancer-promoter resulted in the formation of viral cores with a homogeneous size of approximately 50 nm located in the cytoplasm. Upon coexpression of an envelope construct, particles were observed budding into cytoplasmic vesicles and from the plasma membrane. Expression of the Gag protein precursor pr74 alone led to aberrantly formed viral particles of heterogeneous size and with open cores. Normal-shaped cores were seen after transfection of a construct expressing the p70 gag cleavage product, indicating that p70 gag is able to assemble into capsids. Coexpression of p70 gag and Env resulted in budding virions, ruling out a requirement of the reverse transcriptase for capsid or virion formation. In sharp contrast to other retroviruses, the HFV cores did not spontaneously bud from cellular membranes. Radiochemical labeling followed by protein gel electrophoresis also revealed the intracellular retention of Env-deprived HFV capsids.

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Lo, Yung-Tsun, Tao Tian, Peter E. Nadeau, Jeonghae Park, and Ayalew Mergia. "The Foamy Virus Genome Remains Unintegrated in the Nuclei of G1/S Phase-Arrested Cells, and Integrase Is Critical for Preintegration Complex Transport into the Nucleus." Journal of Virology 84, no. 6 (December 23, 2009): 2832–42. http://dx.doi.org/10.1128/jvi.02435-09.

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ABSTRACT Foamy viruses are a member of the spumavirus subfamily of retroviruses with unique mechanisms of virus replication. Foamy virus replication is cell cycle dependent; however, the genome is found in the nuclei of cells arrested in the G1/S phase. Despite the presence of genome in the nuclei of growth-arrested cells, there is no viral gene expression, thus explaining its dependency on cell cycle. This report shows that the foamy virus genome remains unintegrated in G1/S phase-arrested cells. The foamy virus genome is detected by confocal microscopy in the nuclei of both dividing and growth-arrested cells. Alu PCR revealed foamy virus-specific DNA amplification from genomic DNA isolated in cycling cells at 24 h postinfection. In arrested cells no foamy virus DNA band was detected in cells harvested at 1 or 7 days after infection, and a very faint band that is significantly less than DNA amplified from cycling cells was observed at day 15. After these cells were arrested at the G1/S phase for 1, 7, or 15 days they were allowed to cycle, at which time foamy virus-specific DNA amplification was readily observed. Taken together, these results suggest that the foamy virus genome persists in nondividing cells without integrating. We have also established evidence for the first time that the foamy virus genome and Gag translocation into the nucleus are dependent on integrase in cycling cells, implicating the role of integrase in transport of the preintegration complex into the nucleus. Furthermore, despite the presence of a nuclear localization signal sequence in Gag, we observed no foamy virus Gag importation into the nucleus in the absence of integrase.

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Verschoor, Ernst J., Susan Langenhuijzen, Saskia van den Engel, Henk Niphuis, Kristin S. Warren, and Jonathan L. Heeney. "Structural and Evolutionary Analysis of an Orangutan Foamy Virus." Journal of Virology 77, no. 15 (August 1, 2003): 8584–87. http://dx.doi.org/10.1128/jvi.77.15.8584-8587.2003.

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ABSTRACT The full-length proviral genome of a foamy virus infecting a Bornean orangutan was amplified, and its sequence was analyzed. Although the genome showed a clear resemblance to other published foamy virus genomes from apes and monkeys, phylogenetic analysis revealed that simian foamy virus SFVora was evolutionarily equidistant from foamy viruses from other hominoids and from those from Old World monkeys. This finding suggests an independent evolution within its host over a long period of time.

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Murray, Shannon M., and Maxine L. Linial. "Simian Foamy Virus Co-Infections." Viruses 11, no. 10 (September 27, 2019): 902. http://dx.doi.org/10.3390/v11100902.

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Foamy viruses (FVs), also known as spumaretroviruses, are complex retroviruses that are seemingly nonpathogenic in natural hosts. In natural hosts, which include felines, bovines, and nonhuman primates (NHPs), a large percentage of adults are infected with FVs. For this reason, the effect of FVs on infections with other viruses (co-infections) cannot be easily studied in natural populations. Most of what is known about interactions between FVs and other viruses is based on studies of NHPs in artificial settings such as research facilities. In these settings, there is some indication that FVs can exacerbate infections with lentiviruses such as simian immunodeficiency virus (SIV). Nonhuman primate (NHP) simian FVs (SFVs) have been shown to infect people without any apparent pathogenicity. Humans zoonotically infected with simian foamy virus (SFV) are often co-infected with other viruses. Thus, it is important to know whether SFV co-infections affect human disease.

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Hütter, Sylvia, Irena Zurnic, and Dirk Lindemann. "Foamy Virus Budding and Release." Viruses 5, no. 4 (April 10, 2013): 1075–98. http://dx.doi.org/10.3390/v5041075.

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Murray, S. M., and M. L. Linial. "Foamy virus infection in primates." Journal of Medical Primatology 35, no. 4-5 (August 2006): 225–35. http://dx.doi.org/10.1111/j.1600-0684.2006.00171.x.

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Dissertations / Theses on the topic "Foamy virus"

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Murray, Shannon. "Foamy virus-host interactions /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/4987.

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Hütter, Sylvia, Irena Zurnic, and Dirk Lindemann. "Foamy Virus Budding and Release." Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-127060.

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Like all other viruses, a successful egress of functional particles from infected cells is a prerequisite for foamy virus (FV) spread within the host. The budding process of FVs involves steps, which are shared by other retroviruses, such as interaction of the capsid protein with components of cellular vacuolar protein sorting (Vps) machinery via late domains identified in some FV capsid proteins. Additionally, there are features of the FV budding strategy quite unique to the spumaretroviruses. This includes secretion of non-infectious subviral particles and a strict dependence on capsid-glycoprotein interaction for release of infectious virions from the cells. Virus-like particle release is not possible since FV capsid proteins lack a membrane-targeting signal. It is noteworthy that in experimental systems, the important capsid-glycoprotein interaction could be bypassed by fusing heterologous membrane-targeting signals to the capsid protein, thus enabling glycoprotein-independent egress. Aside from that, other systems have been developed to enable envelopment of FV capsids by heterologous Env proteins. In this review article, we will summarize the current knowledge on FV budding, the viral components and their domains involved as well as alternative and artificial ways to promote budding of FV particle structures, a feature important for alteration of target tissue tropism of FV-based gene transfer systems.

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Hartl, Maximilian Johannes. "Foamy virus enzymes : activity, regulation and resistance." kostenfrei, 2009. http://opus.ub.uni-bayreuth.de/volltexte/2010/676/.

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Eastman, Scott Walton. "The mechanisms of foamy virus capsid assembly /." Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/11516.

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Meiering, Christopher David. "The complexity of persistent foamy virus infection /." Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/11527.

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Stenbak, Carolyn Rinke. "Foamy virus polymerase : enzymatic activities and assembly /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/11510.

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Patton, Gillian Sarah. "Production and application of foamy virus-derived vectors." Thesis, Imperial College London, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.429910.

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Russell, Rebecca Alice. "Prototype foamy virus gene expression and hybrid vector development." Thesis, Imperial College London, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.408262.

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Sweeney, Nathan Paul. "Foamy virus vector integration and application in gene therapy." Thesis, Imperial College London, 2015. http://hdl.handle.net/10044/1/50704.

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Foamy viruses (FVs) are unique ancient retroviruses that infect all non-human primates, but do not cause disease. We aimed to understand the FV pre-integration complex by isolating it from infected cells and characterising its protein constituents. Using a PCR to quantify integration in infected cells, we determined that integration occurs from 10 hours post-transduction. In synchronised cells, the peak of integration correlated well with cells passing through mitosis. However, we were unable to detect in vitro strand-transfer activity to indicate that active pre-integration complexes had been isolated. We conclude that FV pre-integration complexes are likely to be inactive in the conditions tested. A further aim was to optimise FV vectors for use in mesenchymal stem cells and test this vector in mouse models of sphingolipidoses, namely metachromatic leukodystrophy and Krabbe disease. We permitted transduction of cells at a high multiplicity of infection by exchanging the envelope from the prototype FV to that of the macaque. We tested various FV vectors in mesenchymal stem cells and determined that the non-toxic macaque envelope increased transduction efficiency from under 65% to over 95% in a single round of transduction. We achieved high and sustained transgene expression using the phosphoglycerate kinase promoter. Transduced MSCs delivered to the brains of the mouse model for metachromatic leukodystrophy caused only a modest improvement in sulphatide storage, the primary biochemical output for efficacy, although results are inconclusive. In the mouse model for Krabbe disease, transduced MSCs delivered to the brain or the peritoneum had no effect on disease progression. In conclusion, FV vectors are suited to gene therapy of MSCs since they offer the highest transduction efficiency from a single round of transduction, while MSC based gene therapy strategies for Krabbe disease or metachromatic leukodystrophy are unlikely to offer clinical benefit.

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Renault, Noémie. "Trafic intracellulaire de la protéine Gag du virus Foamy." Paris 7, 2009. http://www.theses.fr/2009PA077154.

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Les virus foamy sont des rétrovirus complexes qui appartiennent à la famille des spumaviridae. Ces rétrovirus présentent de nombreuses particularités qui les différencient des orthorétrovirus comme l'existence d'ADN viral infectieux dans la particule virale ou celle d'un ARNm codant pour la polyprotéine Pol, ou encore l'absence d'un facteur de régulation post-transcriptionnelle de type Rev ou Rex. De la même manière, les protéines Gag ne présentent pas les caractéristiques fondamentales retrouvées chez les autres rétrovirus comme le clivage en matrice, capside et nucléocapside. Nous avons focalisé notre travail sur ces protéines structurales et sur leurs rôles tant lors des étapes précoces que tardives. Lors des étapes précoces, la polyprotéine Gag protège le génome viral et le guide sur le réseau microtubulaire jusqu'à la membrane nucléaire. Dans les cellules qui cyclent, les particules,virales enfantes du virus foamy sont retrouvées intactes au centrosome à partir de 4 h post-infection. La capside subit alors un désassemblage en partie dépendant de la protéase virale. A l'inverse, dans les cellules quiescentes, nous montrons que les capsides restent structurées autour centrosome. A la reprise du cycle cellulaire, le cycle réplicatif viral reprend avec le déshabillage de la capside et l'intégration du provirus. Les protéases cellulaires et virales, qui interviennent lors de la décapsidation, semblent ainsi inactives lorsque les cellules sont en phase GO. De manière non exclusive, les sites de clivage de ces protéases sur les protéines structurales du virus pourraient être inaccessibles dans ces conditions. Les protéines Gag jouent également un rôle clé lors des étapes tardives de l'infection, en étant responsables de l'assemblage des capsides qui a lieu dans le cytoplasme, autour du centrosome. De manière intéressante, avant l'assemblage, ces protéines transitent dans le noyau. Nous nous sommes intéressés à cette étape nucléaire et montrons que la protéine Gag est exportée du noyau grâce à un signal d'export nucléaire riche en leucine et sensible à la leptomycine B, présent dans la partie N-terminale de la protéine. Une protéine Gag mutée dans ce domaine est non seulement incapable de quitter le noyau mais interfère négativement avec la réplication d'un virus sauvage. Nous suggérons que les protéines Gag des virus foamy pourraient intervenir dans l’export nucléaire de l’ARN viral lors des étapes tardives de l'infection
Foamy viruses (FVs) are complex exogenous animal retroviruses that differ in many aspects of their life cycle from the orthoretroviruses such as human immunodefîciency virus (HIV). In particular, in FVvs, Gag and Pol proteins are expressed independently of one another, and both proteins undergo single clivage events. None of the conventional Gag landmarks of exogenous retroviruses, such as the major homology region or Cys-His motifs, are found in this protein. Instead, FV Gag harbors conserved C-terminal basic motifs, referred to as Gly-Arg (GR) boxes. Although the first GR (GRI) box binds viral nucleic acids and is required for viral genome packaging, the second (GRII) harbors a nuclear localization sequence (NLS) at its C-terminus, targeting Gag to the nucleus early after infection. GRII also contains a chromatin binding sequence (CBS) in its N-terminus, tethering the FV incoming pre-integration complex onto host chromosomes. The present work focuses on the structural Gag proteins, in early and late stages of infection. Troviral Gag proteins are involved in early stages of infection such as trafficking of incoming viruses nd nuclear import. FV Gag protein uses the microtubule network to reach the nucleus. In cycling cells,FV articles are structured at the centrosome 4 h post-infection. Then, the viral protease helps capsid for ncoating. In quiescent cells, we have shown that viral particles remain structured at the centrosome during everal weeks and that uncoating does not occur : this step is a limiting factor for infection although viral articles are still infectious. Upon cells reactivation, viral capsids undergo proteolysis and disassembly, llowing infection to proceed. During the late stages of infection, Gag undergoes transient nuclear trafficking after it synthesis, before returning back to the cytoplasm for capsid assembly and virus egress. The functional role of this nuclear stage, as well as the molecular mechanisms responsible for Gag nuclear export, are not understood. Here, we identify a leptomycin-sensitive nuclear export sequence (NES) within the N-terminus of the primate foamy virus Gag protein that is absolutely required for the completion of late stages of virus replication. Point mutation of conserved residues within this motif leads to nuclear retention of Gag and dramatically affects viral replication. Moreover, complementation experiments demonstrate that nuclear export-defective Gag mutants negatively interfere with virus release by sequestering wild-type Gag in the nucleus

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Books on the topic "Foamy virus"

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A, Rethwilm, ed. Foamy viruses. Berlin: Springer, 2003.

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Book chapters on the topic "Foamy virus"

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Mergia, A., and M. Heinkelein. "Foamy Virus Vectors." In Foamy Viruses, 131–59. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-55701-9_6.

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Lindemann, D., and P. A. Goepfert. "The Foamy Virus Envelope Glycoproteins." In Foamy Viruses, 111–29. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-55701-9_5.

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Löchelt, M. "Foamy Virus Transactivation and Gene Expression." In Foamy Viruses, 27–61. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-55701-9_2.

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Flügel, R. M., and K. I. Pfrepper. "Proteolytic Processing of Foamy Virus Gag and Pol Proteins." In Foamy Viruses, 63–88. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-55701-9_3.

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Rethwilm, A. "Regulation of Foamy Virus Gene Expression." In Transacting Functions of Human Retroviruses, 1–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-78929-8_1.

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Aguzzi, A., S. Marino, R. Tschopp, and A. Rethwilm. "Regulation of Expression and Pathogenic Potential of Human Foamy Virus In Vitro and in Transgenic Mice." In Current Topics in Microbiology and Immunology, 243–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-85208-4_13.

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Dias, Holger Warnat, Mordechai Aboud, and Rolf M. Flügel. "Analysis of the Phylogenetic Placement of Different Spumaretroviral Genes Reveals Complex Pattern of Foamy Virus Evolution." In Molecular Evolution of Viruses — Past and Present, 111–18. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-1407-3_9.

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Wagner, Erwin F., and Adriano Aguzzi. "Exploring the Pathogenic Potential of c-fos, Polyoma Middle T and Human Foamy Virus in Transgenic Mice." In Transgenic Animals as Model Systems for Human Diseases, 109–28. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02925-1_7.

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"Foamy Virus." In Molecular Detection of Human Viral Pathogens, 159–74. CRC Press, 2016. http://dx.doi.org/10.1201/b13590-17.

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"Primaten Foamy Virus (PFV)." In Lexikon der Infektionskrankheiten des Menschen, 668. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-39026-8_887.

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Conference papers on the topic "Foamy virus"

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Hu, Bin, and Sarah L. Kieweg. "The Effect of Surface Tension on the Epithelial Spreading of Non-Newtonian Drug Delivery Vehicles: Numerical Simulations." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206565.

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This paper is one of the components of our research on how to optimize polymeric drug delivery vehicles. One of the applications is in the topical delivery of anti-human immunodeficiency virus (HIV) gels called microbicides [1]. Microbicides are delivered to vaginal or rectal epithelium to protect it from HIV and other sexually transmitted infections. Microbicides may provide a physical barrier amplifying the normal vaginal defense, as well as destroy the pathogens chemically or inhibit viral infection. The microbicide may consist of an anti-HIV active agent in some delivery vehicle, such as a gel, cream or foam. Microbicides are a promising solution to provide a low-cost, female-controlled method for protection against HIV and other sexually transmitted pathogens.

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Reports on the topic "Foamy virus"

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Negrete, Oscar A., Catherine Branda, Jasper O. E. Hardesty, Mark David Tucker, Julia N. Kaiser, Carol L. Kozina, and Gabriela S. Chirica. A C. elegans-based foam for rapid on-site detection of residual live virus. Office of Scientific and Technical Information (OSTI), February 2012. http://dx.doi.org/10.2172/1035339.

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