Academic literature on the topic 'Alpharetrovirus'
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Journal articles on the topic "Alpharetrovirus"
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Suerth, Julia D., Tobias Maetzig, Melanie Galla, Christopher Baum, and Axel Schambach. "Self-Inactivating Alpharetroviral Vectors with a Split-Packaging Design." Journal of Virology 84, no. 13 (2010): 6626–35. http://dx.doi.org/10.1128/jvi.00182-10.
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ABSTRACT Accidental insertional activation of proto-oncogenes and potential vector mobilization pose serious challenges for human gene therapy using retroviral vectors. Comparative analyses of integration sites of different retroviral vectors have elucidated distinct target site preferences, highlighting vectors based on the alpharetrovirus Rous sarcoma virus (RSV) as those with the most neutral integration spectrum. To date, alpharetroviral vector systems are based mainly on single constructs containing viral coding sequences and intact long terminal repeats (LTR). Even though they are considered to be replication incompetent in mammalian cells, the transfer of intact viral genomes is unacceptable for clinical applications, due to the risk of vector mobilization and the potentially immunogenic expression of viral proteins, which we minimized by setting up a split-packaging system expressing the necessary viral proteins in trans. Moreover, intact LTRs containing transcriptional elements are capable of activating cellular genes. By removing most of these transcriptional elements, we were able to generate a self-inactivating (SIN) alpharetroviral vector, whose LTR transcriptional activity is strongly reduced and whose transgene expression can be driven by an internal promoter of choice. Codon optimization of the alpharetroviral Gag/Pol expression construct and further optimization steps allowed the production of high-titer self-inactivating vector particles in human cells. We demonstrate proof of principle for the versatility of alpharetroviral SIN vectors for the genetic modification of murine and human hematopoietic cells at a low multiplicity of infection.
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Wiegand, Heather L., and Bryan R. Cullen. "Inhibition of Alpharetrovirus Replication by a Range of Human APOBEC3 Proteins." Journal of Virology 81, no. 24 (2007): 13694–99. http://dx.doi.org/10.1128/jvi.01646-07.
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ABSTRACT The mammalian APOBEC3 family of cytidine deaminases includes members that can act as potent inhibitors of retroviral infectivity and retrotransposon mobility. Here, we have examined whether the alpharetrovirus Rous sarcoma virus (RSV) is susceptible to inhibition by a range of human APOBEC3 proteins. We report that RSV is highly susceptible to inhibition by human APOBEC3G, APOBEC3F, and APOBEC3B and moderately susceptible to inhibition by human APOBEC3C and APOBEC3A. For all five proteins, inhibition of RSV infectivity was associated with selective virion incorporation and with C-to-T editing of the proviral DNA minus strand. In the case of APOBEC3G, editing appeared to be critical for effective inhibition. These data represent the first report of inhibition of retroviral infectivity and induction of proviral DNA editing by human APOBEC3A and reveal that alpharetroviruses, which do not normally encounter APOBEC3 proteins in their avian hosts, are susceptible to inhibition by all human APOBEC3 proteins tested. These data further suggest that the resistance of mammalian retroviruses to inhibition by the APOBEC3 proteins expressed in their normal host species is likely to have evolved subsequent to the appearance of this family of mammalian antiretroviral proteins some 35 million years ago; i.e., the base state of a naïve retrovirus is susceptibility to inhibition.
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Rainey, G. Jonah A., and John M. Coffin. "Evolution of Broad Host Range in Retroviruses Leads to Cell Death Mediated by Highly Cytopathic Variants." Journal of Virology 80, no. 2 (2006): 562–70. http://dx.doi.org/10.1128/jvi.80.2.562-570.2006.
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ABSTRACT The ability of many retroviruses to cause disease can be correlated to their cytopathic effect (CPE) in tissue culture characterized by an acute period of cell death and viral DNA accumulation. Here, we show that mutants of a subgroup B avian retrovirus (Alpharetrovirus) cause a very dramatic CPE in certain susceptible avian cells that is coincident with elevated levels of apoptosis, as measured by nuclear morphology, and persistent viral DNA accumulation. These mutants also have a broadly extended host range that includes rodent, cat, dog, monkey, and human cells (31). Previously, we have shown that the mutants exhibit diminished resistance to superinfection. The results presented here have important implications for the process of evolution of retroviruses to use distinct cellular receptors.
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Butterfield-Gerson, Kristin L., Lisa Z. Scheifele, Eileen P. Ryan, Anita K. Hopper та Leslie J. Parent. "Importin-β Family Members Mediate Alpharetrovirus Gag Nuclear Entry via Interactions with Matrix and Nucleocapsid". Journal of Virology 80, № 4 (2006): 1798–806. http://dx.doi.org/10.1128/jvi.80.4.1798-1806.2006.
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ABSTRACT The retroviral Gag polyprotein orchestrates the assembly and release of virus particles from infected cells. We previously reported that nuclear transport of the Rous sarcoma virus (RSV) Gag protein is intrinsic to the virus assembly pathway. To identify cis- and trans-acting factors governing nucleocytoplasmic trafficking, we developed novel vectors to express regions of Gag in Saccharomyces cerevisiae. The localization of Gag proteins was examined in the wild type and in mutant strains deficient in members of the importin-β family. We confirmed the Crm1p dependence of the previously identified Gag p10 nuclear export signal. The known nuclear localization signal (NLS) in MA (matrix) was also functional in S. cerevisiae, and additionally we discovered a novel NLS within the NC (nucleocapsid) domain of Gag. MA utilizes Kap120p and Mtr10p import receptors while nuclear entry of NC involves the classical importin-α/β (Kap60p/95p) pathway. NC also possesses nuclear targeting activity in avian cells and contains the primary signal for the import of the Gag polyprotein. Thus, the nucleocytoplasmic dynamics of RSV Gag depend upon the counterbalance of Crm1p-mediated export with two independent NLSs, each interacting with distinct nuclear import factors.
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Obr, Martin, Florian K. M. Schur, and Robert A. Dick. "A Structural Perspective of the Role of IP6 in Immature and Mature Retroviral Assembly." Viruses 13, no. 9 (2021): 1853. http://dx.doi.org/10.3390/v13091853.
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The small cellular molecule inositol hexakisphosphate (IP6) has been known for ~20 years to promote the in vitro assembly of HIV-1 into immature virus-like particles. However, the molecular details underlying this effect have been determined only recently, with the identification of the IP6 binding site in the immature Gag lattice. IP6 also promotes formation of the mature capsid protein (CA) lattice via a second IP6 binding site, and enhances core stability, creating a favorable environment for reverse transcription. IP6 also enhances assembly of other retroviruses, from both the Lentivirus and the Alpharetrovirus genera. These findings suggest that IP6 may have a conserved function throughout the family Retroviridae. Here, we discuss the different steps in the viral life cycle that are influenced by IP6, and describe in detail how IP6 interacts with the immature and mature lattices of different retroviruses.
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Harper, Amy L., Malgorzata Sudol, and Michael Katzman. "An Amino Acid in the Central Catalytic Domain of Three Retroviral Integrases That Affects Target Site Selection in Nonviral DNA." Journal of Virology 77, no. 6 (2003): 3838–45. http://dx.doi.org/10.1128/jvi.77.6.3838-3845.2003.
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ABSTRACT Integrase can insert retroviral DNA into almost any site in cellular DNA; however, target site preferences are noted in vitro and in vivo. We recently demonstrated that amino acid 119, in the α2 helix of the central domain of the human immunodeficiency virus type 1 integrase, affected the choice of nonviral target DNA sites. We have now extended these findings to the integrases of a nonprimate lentivirus and a more distantly related alpharetrovirus. We found that substitutions at the analogous positions in visna virus integrase and Rous sarcoma virus integrase changed the target site preferences in five assays that monitor insertion into nonviral DNA. Thus, the importance of this protein residue in the selection of nonviral target DNA sites is likely to be a general property of retroviral integrases. Moreover, this amino acid might be part of the cellular DNA binding site on integrase proteins.
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Lee, Eun-Gyung, and Maxine L. Linial. "Deletion of a Cys–His motif from the Alpharetrovirus nucleocapsid domain reveals late domain mutant-like budding defects." Virology 347, no. 1 (2006): 226–33. http://dx.doi.org/10.1016/j.virol.2005.11.048.
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Jouvenet, Nolwenn, Stuart J. D. Neil, Maria Zhadina, et al. "Broad-Spectrum Inhibition of Retroviral and Filoviral Particle Release by Tetherin." Journal of Virology 83, no. 4 (2008): 1837–44. http://dx.doi.org/10.1128/jvi.02211-08.
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ABSTRACT The expression of many putative antiviral genes is upregulated when cells encounter type I interferon (IFN), but the actual mechanisms by which many IFN-induced gene products inhibit virus replication are poorly understood. A recently identified IFN-induced antiretroviral protein, termed tetherin (previously known as BST-2 or CD317), blocks the release of nascent human immunodeficiency virus type 1 (HIV-1) particles from infected cells, and an HIV-1 accessory protein, Vpu, acts as a viral antagonist of tetherin. Here, we show that tetherin is capable of blocking not only the release of HIV-1 particles but also the release of particles assembled using the major structural proteins of a variety of prototype retroviruses, including members of the alpharetrovirus, betaretrovirus, deltaretrovirus, lentivirus, and spumaretrovirus families. Moreover, we show that the release of particles assembled using filovirus matrix proteins from Marburg virus and Ebola virus is also sensitive to inhibition by tetherin. These findings indicate that tetherin is a broadly specific inhibitor of enveloped particle release, and therefore, inhibition is unlikely to require specific interactions with viral proteins. Nonetheless, tetherin colocalized with nascent virus-like particles generated by several retroviral and filoviral structural proteins, indicating that it is present at, or recruited to, sites of particle assembly. Overall, tetherin is potentially active against many enveloped viruses and likely to be an important component of the antiviral innate immune defense.
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Derse, David, Bruce Crise, Yuan Li, et al. "Human T-Cell Leukemia Virus Type 1 Integration Target Sites in the Human Genome: Comparison with Those of Other Retroviruses." Journal of Virology 81, no. 12 (2007): 6731–41. http://dx.doi.org/10.1128/jvi.02752-06.
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ABSTRACT Retroviral integration into the host genome is not entirely random, and integration site preferences vary among different retroviruses. Human immunodeficiency virus (HIV) prefers to integrate within active genes, whereas murine leukemia virus (MLV) prefers to integrate near transcription start sites and CpG islands. On the other hand, integration of avian sarcoma-leukosis virus (ASLV) shows little preference either for genes, transcription start sites, or CpG islands. While host cellular factors play important roles in target site selection, the viral integrase is probably the major viral determinant. It is reasonable to hypothesize that retroviruses with similar integrases have similar preferences for target site selection. Although integration profiles are well defined for members of the lentivirus, spumaretrovirus, alpharetrovirus, and gammaretrovirus genera, no members of the deltaretroviruses, for example, human T-cell leukemia virus type 1 (HTLV-1), have been evaluated. We have mapped 541 HTLV-1 integration sites in human HeLa cells and show that HTLV-1, like ASLV, does not specifically target transcription units and transcription start sites. Comparing the integration sites of HTLV-1 with those of ASLV, HIV, simian immunodeficiency virus, MLV, and foamy virus, we show that global and local integration site preferences correlate with the sequence/structure of virus-encoded integrases, supporting the idea that integrase is the major determinant of retroviral integration site selection. Our results suggest that the global integration profiles of other retroviruses could be predicted from phylogenetic comparisons of the integrase proteins. Our results show that retroviruses that engender different insertional mutagenesis risks can have similar integration profiles.
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Lee, Eun-Gyung, та Maxine L. Linial. "Basic Residues of the Retroviral Nucleocapsid Play Different Roles in Gag-Gag and Gag-Ψ RNA Interactions". Journal of Virology 78, № 16 (2004): 8486–95. http://dx.doi.org/10.1128/jvi.78.16.8486-8495.2004.
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ABSTRACT The Orthoretrovirus Gag interaction (I) domain maps to the nucleocapsid (NC) domain in the Gag polyprotein. We used the yeast two-hybrid system to analyze the role of Alpharetrovirus NC in Gag-Gag interactions and also examined the efficiency of viral assembly and release in vivo. We could delete either or both of the two Cys-His (CH) boxes without abrogating Gag-Gag interactions. We found that as few as eight clustered basic residues, attached to the C terminus of the spacer peptide separating the capsid (CA) and NC domains in the absence of NC, was sufficient for Gag-Gag interactions. Our results support the idea that a sufficient number of basic residues, rather than the CH boxes, play the important role in Gag multimerization. We also examined the requirement for basic residues in Gag for packaging of specific packaging signal (Ψ)-containing RNA. Using a yeast three-hybrid RNA-protein interaction assay, second-site suppressors of a packaging-defective Gag mutant were isolated, which restored Ψ RNA binding. These suppressors mapped to the p10 or CA domains in Gag and resulted in either introduction of a positively charged residue or elimination of a negatively charged one. These results imply that the structural interactions of NC with other domains of Gag are necessary for Ψ RNA binding. Taken together, our results show that while Gag assembly only requires a certain number of positively charged amino acids, Gag binding to genomic RNA for packaging requires more complex interactions inherent in the protein tertiary structure.
Dissertations / Theses on the topic "Alpharetrovirus"
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Li, Ruoping. "Effets de mutations ponctuelles ou de délétions dans l'oncongène v-myb des virus AMW et E26 sur la transformation des cellules myéloi͏̈des et sur la prolifération des cellules de neurorétine de poulet." Lille 1, 1989. http://www.theses.fr/1989LIL10072.
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Clonage moléculaire et séquençage du gène v-myb du rétrovirus aviaire thermosensible ts 143 E26 et mise en évidence d'une mutation impliquée dans la fixation de la protéine myb à l'ADN. Démonstration par mutagénèse du virus E26 que cette mutation est responsable du phénotype thermosensible des cellules transformées par ce virus. Mise en évidence du rôle du gène v-myb dans la stimulation in vitro des cellules de neurorétine de poulet
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Melet, Fabrice. "Évènements moléculaires impliqués dans la différenciation érythrocytique aviaire." Lyon 1, 1992. http://www.theses.fr/1992LYO1T003.
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Banks, Jennifer Dawn. "Characterization of a minimal avian leukosis-sarcoma virus packaging signal /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/11528.
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Pain, Bertrand. "Rôles des protooncogènes c-erbA et c-erbB et de leurs homologues viraux dans la prolifération et la différenciation des cellules érythrocytaires avaires." Lyon 1, 1990. http://www.theses.fr/1990LYO1T211.
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Rascle, Anne. "Régulation de la transcription du gène de l'anhydrase carbonique II par les récepteurs hormonaux nucléaires de la famille c-ErbA dans les cellules érythrocytaires aviaires : modèle d'action de l'oncogène v-ErbA." Lyon 1, 1994. http://www.theses.fr/1994LYO1T308.
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Tracy, Sharon Elizabeth. "Characterization of a Deletion in erb [subscript erb]B Sequences Associated with Angiosarcoma: a Thesis." eScholarship@UMMS, 1998. http://escholarship.umassmed.edu/gsbs_diss/299.
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Analyses of 11 new erbB transducing viruses had previously correlated differences in disease potential with deletions or truncations in sequences encoding the carboxy-terminal domain of the chicken EGF receptor. erbB sequences of two of these viruses, one inducing only erythroblastosis (AEV-5005) and the other inducing only angiosarcoma (AAV-5005), were molecularly cloned. Sequence analysis confirmed the presence of an internal deletion in AAV-5005. The deletion was found to be inframe and to have removed 177 nucleotides. The deleted sequence had encoded a region between the kinase domain and the autophosphorylation sites of the EGF receptor. To establish that the deletion was responsible for the change in disease potential two recombinant viruses were constructed. One recombinant virus (srE) contained erbB sequences from AEV-5005. The other recombinant virus (srE/A) was identical to srE except that a restriction fragment from AAV-5005 which contained the deletion was substituted for the homologous fragment of AEV-5005. The srE virus induced only erythroblastosis, while the srE/A virus induced angiosarcoma as well as erythroblastosis. This demonstrated that the deletion was sufficient to induce angiosarcoma. Metabolic labelling did not reveal any difference in the expression or processing of these proteins and both became phosphorylated in an in vitro kinase assay. The biochemical basis for the difference in disease potential of these two related proteins remains to be determined.
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Bonamy, Ghislain. "Etude de la distribution et du transit subcellulaire de l'oncoprotéine V-ERBA : implication dans ses propriétés carcinogéniques." Paris 7, 2006. http://www.theses.fr/2006PA077075.
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Le virus de l'érythroblastose aviaire induit une erythroblastose chez les oiseaux via la surproduction de deux oncoprotéines, v-ErbA et v-ErbB, qui dérivent de proto-oncogènes impliqués dans la régulation de la balance cruciale prolifération/différenciation chez les érythrocytes. V-ErbA est une protéine venant de la fusion entre la polyprotéine virale Gag et une portion du récepteur aux hormones thyroïdiennes a (TRα). Suite à l'ensemble de ses modifications, v-ErbA a acquis des propriétés qui diffèrent de son homologue cellulaire. En particulier, l'oncoprotéine v-ErbA est activement exportée hors du noyau par CRM1. Ici, nous avons montré que le signal d'export de v-ErbA est situé dans son domaine Gag et plus précisément dans sa région p10 riche en leucines. Parce que l'activité de v-ErbA avait été décrite comme nucléaire via la compétition pour la liaison à l'ADN et pour des cofacteurs, la distribution cytoplasmique de la protéine est surprenante. De manière intéressante lorsque v-ErbA est coexprimée avec TRa, ou avec le récepteur ß de l'acide rétinoïque, une fraction importante de ces deux récepteurs est délocalisée dans le cytoplasme. Grâce à des techniques variées, nous avons fourni des évidences que cette délocalisation est liée à une séquestration ou à un export via une interaction directe avec v-ErbA. Ainsi, ces résultats suggèrent que la délocalisation de TRα et probablement d'autres corégulateurs contribuent, au moins en partie, à l'effet dominant négatif de l'oncoprotéine. Ces résultats soulignent aussi le rôle du transport nucléaire dans les réglages fins de l'activité transcriptionnelle et son implication dans des pathologies telles que les cancers<br>The avian erythroblastosis virus induces erythroleukemia in birds through the overproduction of two oncoproteins, v-ErbA and v-ErbB. These two proteins correspond to two highly mutated proto-oncogenes which normally regulate the tightly controlled balance of differentiation/proliferation in erythrocytes. V-ErbA is a fusion protein of the viral Gag polyprotein to part of thé thyroid hormone receptor a (TRα). As a result of its numerous modifications and mutations, v-ErbA acquired properties which differ from its cellular homolog. In particular, the oncoprotein v-ErbA is actively exported from the nucleus via the export receptor CRM1. Here, we showed that the nuclear export signal of v-ErbA resides in the Gag domain and more precisely in the leucine-rich, p10 région, of the Gag moiety. Because the activity of v-ErbA is believed to occur within the cell nucleus through competition for DMA binding and for cofactors, the cytoplasmic distribution of the oncoprotein is surprising. Interestingly when v-ErbA is coexpressed with TRa, or with the retinoid X receptor ß, a significant fraction of these two receptors is mislocalized to the cytoplasm. Using various techniques we provide evidence that the mislocalization is caused by the capacity of v-ErbA to sequester or to piggyback out of the nucleus these two receptors via a direct interaction. Together, these results suggest that the mislocalization of TRα and probably other coregulators contributes, at least in part, to oncoprotein dominant negative activity, and illustrate clearly the role of nuclear transport for the fine-tuning of transcription and its implication in pathologies such as cancer
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Diaz, Jean-Jacques. "Étude des variations de phosphorylation de la protéine ribosomique S6 dans le foie de rat et dans des cellules infectées par des rétrovirus porteurs d'oncogènes." Lyon 1, 1988. http://www.theses.fr/1988LYO1T061.
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Ekstedt, Elias, Inna Fryckstedt, Hanna Hyllander, Josefin Jonsson, Elin Ring, and Felix Wærn. "The future of viral vectors for gene therapy." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2021. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-444138.
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Gene therapy is a fast growing technology that offers treatments for genetic diseases. The method is based on introducing genetic material into a patient to replace the disease-causing gene, using a vector. This report examines the potential of some viral vectors for gene therapy, to give Bio-Works Technologies a recommendation on what the future market demands. Oncolytic viruses, vaccines and gene editing are not treated in the report as a delimitation. Viral vectors have different biological properties and require different purification methods, making them suitable for different applications in gene therapy. In the purification of the viruses it can be challenging to obtain a high purity and large-scale manufacturing. One major drawback with most purification methods is that they are not specific to just one virus, which leads to contaminants in the solution and lower purity. The viral vectors handled in the report are the adenovirus, adeno-associated virus, gammaretrovirus, lentivirus, alpharetrovirus, foamy virus, herpes simplex virus and baculovirus. These were chosen as they are relevant vectors for gene therapy and stay within the scope of the report. Lentiviral vectors (LVs) and adeno-associated viral vectors (AAVs) will dominate the gene therapy field in the coming years. This is based on the information that the use of AAVs and LVs in clinical trials have increased in recent years, while the other vectors mentioned above have slightly decreased or show no apparent change. However, challenges still remain in the purification processes. Ligands used in affinity chromatography for purification of AAVs are effective at removing most contaminants, but cannot distinguish between empty and loaded capsids, which can induce immune response when used clinically. This is the main challenge when purifying AAVs. The empty capsids can be removed with ion exchange chromatography, which results in higher purity but also lower recovery. There is no specific purifying method for LVs, therefore a lentivirus-specific affinity ligand, such as an antibody ligand, would be beneficial for the purification and manufacturing procedure. In addition to AAVs and LVs, baculoviral vectors and foamy viral vectors show great potential in a long-term perspective but they only have been researched in preclinical studies. Moreover, herpes simplex viral vectors and adenoviral vectors show potential in cancer treatments or as vaccines rather than in augmentation gene therapy.
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Bar, Aileen. "Étude structurale et fonctionnelle de l’élément NRS régulateur négatif de l’épissage de l’ARN du virus du Sarcome de Rous." Thesis, Nancy 1, 2011. http://www.theses.fr/2011NAN10153/document.
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Afin de se répliquer, les rétrovirus doivent disposer à la fois d’ARN épissés et non épissés. Chez le virus du Sarcome de Rous (RSV), l’accumulation de l’ARN non épissé dépend de l’élément NRS (Negative Regulator of Splicing). L’élément NRS est un élément bipartite. Sa région 5’ est assimilée à une séquence ESE (Exon Splicing Enhancer) à laquelle se fixent de nombreuses protéines SR tandis que sa région 3’ contient un pseudo-site 5’ non fonctionnel qui constitue un leurre qui est responsable de l’inhibition de l’épissage à l’unique site 5’ fonctionnel du virus. Seule la structure 3D de la partie 3’ du NRS qui contient le pseudo-site a été expérimentalement établie. Dans ce travail, nous avons déterminé la structure 2D de la totalité de l’élément NRS à l’aide de sondes chimiques et enzymatiques. La comparaison de cette structure expérimentale à celles que nous avons établies pour d’autres éléments NRS mutants fonctionnels et non fonctionnel ainsi qu’à celles théoriques de la totalité des virus aviaires séquencés argumente en faveur de la forte signification biologique de notre modèle. Des expériences d’épissage in vitro réalisées sur l’élément NRS sauvage ainsi que ses formes tronquées ont permis de mettre en évidence le rôle crucial de deux structures tige-boucles dans la fonction du NRS. Les expériences de purification de complexes formés avec un extrait nucléaire de cellules HeLa sur ces différents éléments NRS par des techniques chromatographie d’affinité ont permis de démontrer l’importance de l’association de ces deux structures tige-boucles avec les protéines SR et la snRNP U1. Nous avons défini un nouvel élément NRS minimal fonctionnel capable d’inhiber l’épissage et nous avons démontré l’activation de l’inhibition de l’épissage de l’élément NRS par la protéine 9G8 in vitro et in cellulo<br>Retroviruses require both spliced and unspliced RNAs for productive replication. Accumulation of unspliced RNA in Rous Sarcoma Virus (RSV) depends on the NRS element, (Negative Regulator of Splicing). The NRS element is bipartite. Its 5’ terminal part is considered as an ESE that binds SR proteins and its 3’ part contains a decoy 5’-splice site (ss), which inhibits splicing at the bona fide 5’ ss. Only the 3D structure of a small NRS fragment including the decoy 5’ ss had been experimentally studied. Here, by chemical and enzymatic probing of entire RSV NRS, we determine its 2D structure. By comparative analysis of 2D structures of functional and non-functional avian NRS variants and of all sequenced avian NRSs, we bring strong arguments for a biological significance of the established structure. By in vitro splicing assays, we show a crucial role of two of the established stem-loop structures and by affinity purification of complexes formed by WT and truncated NRSs in HeLa cell nuclear extract, we demonstrate their importance for SR protein and U1 snRNP association. We define a new small NRS element retaining splicing inhibitory properties and finally demonstrate the capability of the SR protein 9G8 to increase NRS activity in vitro and in cellulo
Book chapters on the topic "Alpharetrovirus"
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Leis, Jonathan, Michael Johnson, and Elena Brin. "Alpharetrovirus‡." In The Springer Index of Viruses. Springer New York, 2011. http://dx.doi.org/10.1007/978-0-387-95919-1_270.
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Barnard, R. J. O., and J. A. T. Young. "Alpharetrovirus Envelope-Receptor Interactions." In Current Topics in Microbiology and Immunology. Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-19012-4_3.
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