Relevant bibliographies by topics / Pr55gag

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Academic literature on the topic 'Pr55gag'

Author: Grafiati
Published: 4 June 2021
Last updated: 14 February 2022

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Journal articles on the topic "Pr55gag"

1

Wyma, Donald J., Alexander Kotov, and Christopher Aiken. "Evidence for a Stable Interaction of gp41 with Pr55Gag in Immature Human Immunodeficiency Virus Type 1 Particles." Journal of Virology 74, no. 20 (October 15, 2000): 9381–87. http://dx.doi.org/10.1128/jvi.74.20.9381-9387.2000.

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ABSTRACT Assembly of infectious human immunodeficiency virus type 1 (HIV-1) virions requires incorporation of the viral envelope glycoproteins gp41 and gp120. Several lines of evidence have suggested that the cytoplasmic tail of the transmembrane glycoprotein, gp41, associates with Pr55Gag in infected cells to facilitate the incorporation of HIV-1 envelope proteins into budding virions. However, direct evidence for an interaction between gp41 and Pr55Gagin HIV-1 particles has not been reported. To determine whether gp41 is associated with Pr55Gag in HIV-1 particles, viral cores were isolated from immature HIV-1 virions by sedimentation through detergent. The cores contained a major fraction of the gp41 that was present on untreated virions. Association of gp41 with cores required the presence of the gp41 cytoplasmic tail. In HIV-1 particles containing a functional protease, a mutation that prevents cleavage of Pr55Gag at the matrix-capsid junction was sufficient for the detergent-resistant association of gp41 with the isolated cores. In addition to gp41, a major fraction of virion-associated gp120 was also detected on immature HIV-1 cores. Isolation of cores under conditions known to disrupt lipid rafts resulted in the removal of a raft-associated protein incorporated into virions but not the HIV-1 envelope proteins. These results provide biochemical evidence for a stable interaction between Pr55Gag and the cytoplasmic tail of gp41 in immature HIV-1 particles. Moreover, findings in this study suggest that the interaction of Pr55Gag with gp41 may regulate the function of the envelope proteins during HIV-1 maturation.
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Fritz, Joëlle V., Denis Dujardin, Julien Godet, Pascal Didier, Jan De Mey, Jean-Luc Darlix, Yves Mély, and Hugues de Rocquigny. "HIV-1 Vpr Oligomerization but Not That of Gag Directs the Interaction between Vpr and Gag." Journal of Virology 84, no. 3 (November 18, 2009): 1585–96. http://dx.doi.org/10.1128/jvi.01691-09.

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ABSTRACT During HIV-1 assembly, the viral protein R (Vpr) is incorporated into newly made viral particles via an interaction with the C-terminal domain of the Gag polyprotein precursor Pr55Gag. Vpr has been implicated in the nuclear import of newly made viral DNA and subsequently in its transcription. In addition, Vpr can affect the cell physiology by causing G2/M cell cycle arrest and apoptosis. Vpr can form oligomers, but their roles have not yet been investigated. We have developed fluorescence lifetime imaging microscopy-fluorescence resonance energy transfer-based assays to monitor the interaction between Pr55Gag and Vpr in HeLa cells. To that end, we used enhanced green fluorescent protein-Vpr that can be incorporated into the virus and tetracysteine (TC)-tagged Pr55Gag-TC. This TC motif is tethered to the C terminus of Pr55Gag and does not interfere with Pr55Gag trafficking and the assembly of virus-like particles (VLPs). Results show that the Pr55Gag-Vpr complexes accumulated mainly at the plasma membrane. In addition, results with Pr55Gag-TC mutants confirm that the 41LXXLF domain of Gag-p6 is essential for Pr55Gag-Vpr interaction. We also report that Vpr oligomerization is crucial for Pr55Gag recognition and its accumulation at the plasma membrane. On the other hand, Pr55Gag-Vpr complexes are still formed when Pr55Gag carries mutations impairing its multimerization. These findings suggest that Pr55Gag-Vpr recognition and complex formation occur early during Pr55Gag assembly.
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3

Chatel-Chaix, Laurent, Levon Abrahamyan, Céline Fréchina, Andrew J. Mouland, and Luc DesGroseillers. "The Host Protein Staufen1 Participates in Human Immunodeficiency Virus Type 1 Assembly in Live Cells by Influencing pr55Gag Multimerization." Journal of Virology 81, no. 12 (April 11, 2007): 6216–30. http://dx.doi.org/10.1128/jvi.00284-07.

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ABSTRACT Human immunodeficiency virus type 1 (HIV-1) requires the sequential activities of virus-encoded proteins during replication. The activities of several host cell proteins and machineries are also critical to the completion of virus assembly and the release of infectious virus particles from cells. One of these proteins, the double-stranded RNA-binding protein Staufen1 (Stau1), selectively associates with the HIV-1 genomic RNA and the viral precursor Gag protein, pr55Gag. In this report, we tested whether Stau1 modulates pr55Gag assembly using a new and specific pr55Gag oligomerization assay based on bioluminescence resonance energy transfer (BRET) in both live cells and extracts after cell fractionation. Our results show that both the overexpression and knockdown of Stau1 increase the pr55Gag-pr55Gag BRET levels, suggesting a role for Stau1 in regulating pr55Gag oligomerization during assembly. This effect of Stau1 on pr55Gag oligomerization was observed only in membranes, a cellular compartment in which pr55Gag assembly primarily occurs. Consistently, expression of Stau1 harboring a vSrc myristylation signal led to a 6.5-fold enrichment of Stau1 in membranes and a corresponding enhancement in the Stau1-mediated effect on pr55Gag-pr55Gag BRET, demonstrating that Stau1 acts on assembly when targeted to membranes. A role for Stau1 in the formation of particles is further supported by the detection of membrane-associated detergent-resistant pr55Gag complexes and the increase of virus-like particle release when Stau1 expression levels are modulated. Our results indicate that Stau1 influences HIV-1 assembly by modulating pr55Gag-pr55Gag interactions, as shown in a live cell interaction assay. This likely occurs when Stau1 interacts with membrane-associated assembly intermediates.
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Rue, Sarah M., Jason W. Roos, Patrick M. Tarwater, Janice E. Clements, and Sheila A. Barber. "Phosphorylation and Proteolytic Cleavage of Gag Proteins in Budded Simian Immunodeficiency Virus." Journal of Virology 79, no. 4 (February 15, 2005): 2484–92. http://dx.doi.org/10.1128/jvi.79.4.2484-2492.2005.

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ABSTRACT The lentiviral Gag polyprotein (Pr55Gag) is cleaved by the viral protease during the late stages of the virus life cycle. Proteolytic cleavage of Pr55Gag is necessary for virion maturation, a structural rearrangement required for infectivity that occurs in budded virions. In this study, we investigate the relationship between phosphorylation of capsid (CA) domains in Pr55Gag and its cleavage intermediates and their cleavage by the viral protease in simian immunodeficiency virus (SIV). First, we demonstrate that phosphorylated forms of Pr55Gag, several CA-containing cleavage intermediates of Pr55Gag, and the free CA protein are detectable in SIV virions but not in virus-producing cells, indicating that phosphorylation of these CA-containing Gag proteins may require an environment that is unique to the virion. Second, we show that the CA domain of Pr55Gag can be phosphorylated in budded virus and that this phosphorylation does not require the presence of an active viral protease. Further, we provide evidence that CA domains (i.e., incompletely cleaved CA) are phosphorylated to a greater extent than free (completely cleaved) CA and that CA-containing Gag proteins can be cleaved by the viral protease in SIV virions. Finally, we demonstrate that Pr55Gag and several of its intermediates, but not free CA, are actively phosphorylated in budded virus. Taken together, these data indicate that, in SIV virions, phosphorylation of CA domains in Pr55Gag and several of its cleavage intermediates likely precedes the cleavage of these domains by the viral protease.
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Nicholson, Michael G., Sheila A. Barber, and Janice E. Clements. "The SIVmac239 Pr55Gag isoform, SIV p43, suppresses proteolytic cleavage of Pr55Gag." Virology 360, no. 1 (March 2007): 84–91. http://dx.doi.org/10.1016/j.virol.2006.10.003.

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Chatel-Chaix, Laurent, Jean-Francois Clément, Catherine Martel, Véronique Bériault, Anne Gatignol, Luc DesGroseillers, and Andrew J. Mouland. "Identification of Staufen in the Human Immunodeficiency Virus Type 1 Gag Ribonucleoprotein Complex and a Role in Generating Infectious Viral Particles." Molecular and Cellular Biology 24, no. 7 (April 1, 2004): 2637–48. http://dx.doi.org/10.1128/mcb.24.7.2637-2648.2004.

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ABSTRACT Staufen is a host protein that is selectively incorporated into human immunodeficiency virus type 1 (HIV-1) particles in a poorly defined process that involves the selection of HIV-1 genomic RNA for encapsidation and the activity of its third double-stranded RNA-binding domain (dsRBD3). To better understand this, we characterized its interactions with pr55Gag, the principal mediator of HIV-1 genomic RNA encapsidation. Chimeric proviruses harboring wild-type or mutant forms of Staufen were expressed in 293T cells. Cell fractionation analyses demonstrated that Staufen cosedimented with pr55Gag within detergent-resistant, trypsin-sensitive complexes that excluded mature capsid and matrix proteins. Coimmunoprecipitation and bioluminescence resonance energy transfer assays demonstrated a specific and direct interaction between Staufen and the nucleocapsid domain of pr55Gag in vitro and in live cells. This interaction is shown here to be mediated by Staufen's dsRBD3, with a contribution from its C-terminal domain. Immunoprecipitation and reverse transcription-PCR analyses showed that the 9-kb genomic RNA was found within Staufen-containing immune complexes. Spliced HIV-1 RNAs were not detected in these Staufen complexes, indicating a preferential association of Staufen with the 9-kb species. These results substantiate that Staufen and pr55Gag interact directly during HIV-1 expression. Knockdown of Staufen expression by small interfering RNAs in HIV-1-expressing cells demonstrated that this cellular protein was important for the generation of infectious virus. These data show that Staufen, pr55Gag, and genomic RNA are part of the same intracellular complex and support a role for Staufen in pr55Gag function in viral assembly, genomic RNA encapsidation, and the generation of infectious viral particles.
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Ding, Lingmei, Aaron Derdowski, Jaang-Jiun Wang, and Paul Spearman. "Independent Segregation of Human Immunodeficiency Virus Type 1 Gag Protein Complexes and Lipid Rafts." Journal of Virology 77, no. 3 (February 1, 2003): 1916–26. http://dx.doi.org/10.1128/jvi.77.3.1916-1926.2003.

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ABSTRACT Formation of human immunodeficiency virus type 1 (HIV-1) particles takes place at the plasma membrane of cells and is directed by the Pr55Gag polyprotein. A functional assembly domain (the M domain) within the N-terminal portion of Pr55Gag mediates the interaction of Gag with cellular membranes. However, the determinants that provide specificity for assembly on the plasma membrane, as opposed to intracellular membranes, have not been identified. Recently, it was reported that Pr55Gag interacts with lipid raft microdomains of the plasma membrane. We sought to identify the domains within Pr55Gag that contribute to lipid raft association of Gag. Here we demonstrate that the I domain is required for interaction with detergent-resistant membrane fractions (DRMs). Mutation of key I-domain residues or loss of myristylation abrogated the association of Gag with DRMs. Thus, the I domain and the M domain combine to mediate Gag-lipid raft interactions as defined by these biochemical criteria. However, Gag protein complexes defined by flotation studies were much denser than classical lipid rafts, failed to incorporate classical lipid raft marker proteins, and were not disrupted by cholesterol extraction. Large sheets of Gag protein were identified in DRM fractions upon examination by electron microscopy. These results indicate that HIV-1 Pr55Gag forms detergent-resistant complexes at the cellular periphery that are distinct from lipid raft microdomains.
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Gerber, Pehuén Pereyra, Mercedes Cabrini, Carolina Jancic, Luciana Paoletti, Claudia Banchio, Catalina von Bilderling, Lorena Sigaut, et al. "Rab27a controls HIV-1 assembly by regulating plasma membrane levels of phosphatidylinositol 4,5-bisphosphate." Journal of Cell Biology 209, no. 3 (May 4, 2015): 435–52. http://dx.doi.org/10.1083/jcb.201409082.

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During the late stages of the HIV-1 replication cycle, the viral polyprotein Pr55Gag is recruited to the plasma membrane (PM), where it binds phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and directs HIV-1 assembly. We show that Rab27a controls the trafficking of late endosomes carrying phosphatidylinositol 4-kinase type 2 α (PI4KIIα) toward the PM of CD4+ T cells. Hence, Rab27a promotes high levels of PM phosphatidylinositol 4-phosphate and the localized production of PI(4,5)P2, therefore controlling Pr55Gag membrane association. Rab27a also controls PI(4,5)P2 levels at the virus-containing compartments of macrophages. By screening Rab27a effectors, we identified that Slp2a, Slp3, and Slac2b are required for the association of Pr55Gag with the PM and that Slp2a cooperates with Rab27a in the recruitment of PI4KIIα to the PM. We conclude that by directing the trafficking of PI4KIIα-positive endosomes toward the PM, Rab27a controls PI(4,5)P2 production and, consequently, HIV-1 replication.
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Bardy, Martine, Bernard Gay, Stéphanie Pébernard, Nathalie Chazal, Marianne Courcoul, Robert Vigne, Etienne Decroly, and Pierre Boulanger. "Interaction of human immunodeficiency virus type 1 Vif with Gag and Gag–Pol precursors: co-encapsidation and interference with viral protease-mediated Gag processing." Journal of General Virology 82, no. 11 (November 1, 2001): 2719–33. http://dx.doi.org/10.1099/0022-1317-82-11-2719.

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Interactions of human immunodeficiency virus type 1 (HIV-1) Vif protein with various forms of Gag and Gag–Pol precursors expressed in insect cells were investigated in vivo and in vitro by co-encapsidation, co-precipitation and viral protease (PR)-mediated Gag processing assays. Addressing of Gag to the plasma membrane, its budding as extracellular virus-like particles (VLP) and the presence of the p6 domain were apparently not required for Vif encapsidation, as non-N-myristoylated Δp6-Gag and Vif proteins were co-encapsidated into intracellular VLP. Encapsidation of Vif occurred at significantly higher copy numbers in extracellular VLP formed from N-myristoylated, budding-competent Gag–Pol precursors harbouring an inactive PR domain or in chimaeric VLP composed of Gag and Gag–Pol precursors compared with the Vif content of Pr55Gag VLP. Vif encapsidation efficiency did not seem to correlate directly with VLP morphology, since these chimaeric VLP were comparable in size and shape to Pr55Gag VLP. Vif apparently inhibited PR-mediated Pr55Gag processing in vitro, with preferential protection of cleavage sites at the MA–CA and CA–NC junctions. Vif was resistant to PR action in vitro under conditions that allowed full Gag processing, and no direct interaction between Vif and PR was detected in vivo or in vitro. This suggested that inhibition by Vif of PR-mediated Gag processing resulted from interaction of Vif with the Gag substrate and not with the enzyme. Likewise, the higher efficiency of Vif encapsidation by Gag–Pol precursor compared with Pr55Gag was probably not mediated by direct binding of Vif to the Gag–Pol-embedded PR domain, but more likely resulted from a particular conformation of the Gag structural domains of the Gag–Pol precursor.
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Bussienne, Charlotte, Roland Marquet, Jean-Christophe Paillart, and Serena Bernacchi. "Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role." International Journal of Molecular Sciences 22, no. 6 (March 11, 2021): 2871. http://dx.doi.org/10.3390/ijms22062871.

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Protein post-translational modifications (PTMs) play key roles in eukaryotes since they finely regulate numerous mechanisms used to diversify the protein functions and to modulate their signaling networks. Besides, these chemical modifications also take part in the viral hijacking of the host, and also contribute to the cellular response to viral infections. All domains of the human immunodeficiency virus type 1 (HIV-1) Gag precursor of 55-kDa (Pr55Gag), which is the central actor for viral RNA specific recruitment and genome packaging, are post-translationally modified. In this review, we summarize the current knowledge about HIV-1 Pr55Gag PTMs such as myristoylation, phosphorylation, ubiquitination, sumoylation, methylation, and ISGylation in order to figure out how these modifications affect the precursor functions and viral replication. Indeed, in HIV-1, PTMs regulate the precursor trafficking between cell compartments and its anchoring at the plasma membrane, where viral assembly occurs. Interestingly, PTMs also allow Pr55Gag to hijack the cell machinery to achieve viral budding as they drive recognition between viral proteins or cellular components such as the ESCRT machinery. Finally, we will describe and compare PTMs of several other retroviral Gag proteins to give a global overview of their role in the retroviral life cycle.
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Dissertations / Theses on the topic "Pr55gag"

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Lavigueur, Olivier. "Identification of newly synthesized HIV-1 pr55gag on Lysosmal-associated membrane protein-1 late endosomal vesicles." Thesis, McGill University, 2010. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=86856.

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Recent work published from our lab showed that modulation of the dynein motor complex affected HIV-1 viral production but not viral infectivity and that trafficking of viral components played an important role in assembly. It was further demonstrated that viral genomic RNA and the HIV-1 structural protein pr55Gag co-localized on LAMP-1 - a transmembrane glycoprotein found on endosomal and lysosomal membranes - late endosomal vesicles. Using the Lumio™ dyes fluorescein arsenical helix binder (FlAsH) and resorufin arsenical helix binder (ReAsH) and TC-tagged Gag-TC and pNL4-3TC constructs, we show the localization of newly synthesized pr55Gag through dual biarsenical labeling in the perinuclear region of HeLa cells. By overexpressing the p50/dynamitin-HA and RILP-myc proteins, we also show the physical interaction of newly synthesized pr55Gag and LAMP-1 late endosomal membranes.
Les récents travaux de notre laboratoire ont montré que la modulation du complexe moteur dynein (Dynein motor complex) avait un impact sur la production virale du VIH-1 mais pas sur son infectivité. Ainsi, le trafic de composantes virales joue un rôle important dans l'assemblage du virus. De plus, l'ARN génomique viral et la protéine structurelle pr55Gag du VIH-1 sont co-localisés sur les vésicules d'endosome tardif portant le marqueur LAMP-1, une glycoprotéine transmembranaire que l'on retrouve sur les membranes endosomales et lysosomales. En utilisant les molécules fluorescentes Lumio™ fluorescein arsenical helix binder (FlAsH) et resorufin arsenical helix binder (ReAsH) et des construits viraux portant une étiquette TC (Gag-TC et pNL4-3-TC), nous montrons que l'emplacement de pr55Gag nouvellement synthétisé se trouve dans la région péri-nucléique de cellules HeLa. En sur-exprimant les protéines p50/dynamitin-HA et RILP-myc, nous montrons également l'interaction physique entre les protéines pr55Gag nouvellement synthétisées et les vésicules d'endosomes tardifs marqués par LAMP-1.
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2

Wassim, Ekram. "Mécanismes moléculaires gouvernant la sélection et l'encapsidation de l'ARN génomique du VIH-1 : l’encapsidation sélective de l’ARN génomique du VIH-1." Thesis, Strasbourg, 2012. http://www.theses.fr/2012STRAJ027.

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La sélection de l’ARNg des rétrovirus repose sur des interactions entre le domaine nucléocapside (NC) du précurseur Gag et des régions de l’ARN viral appelées ψ (ou Psi) localisées dans la région 5’ non traduite (5’-UTR) de l’ARNg et/ou dans le début du gène gag.Malgré des nombreuses études, les mécanismes moléculaires gouvernant l’incorporation de l’ARNg dans les particules virales en cours d’assemblage sont encore mal compris. La protéine Gag est notoirement sensible à la protéolyse et la plupart des études ont été menées avec une Gag dépourvue du domaine p6 (GagΔp6) qui ne reflètepas correctement les propriétés de fixation de la protéine Gag entière à l’ARNg. Les travaux réalisés aux cours de cette thèse nous ont permis de montrer que Pr55Gag et ses produits de maturation NCp15 et NCp7 sont capables de distinguer l’ARNg du VIH-1 des ARN viraux épissés. La stabilisation des formes dimériques ou la perturbation des interactions à longue distance n’ont aucune influence sur la reconnaissance spécifique de Gag pour l’ARNg. Par des expériences de mutagénèse dirigée et de compétition, nous avons montré non seulement que la dimérisation de l’ARNg et le motif SL1 (surtout sa boucle interne) joue un rôle crucial pour la fixation de Gag mais aussi que l’intégrité de la région Psi est indispensable pour une fixation optimale. Ces résultats nous ont amené à déterminer plus précisément l’empreinte de Gag sur l’ARNg et les résidus requis pour la fixation de Gag qui on confirmé le rôle crucial de SL1 comme le siganl major pour la reconnaissance spécifique de l’ARNg par le pr55Gag
Packaging of HIV-1 genomic RNA (gRNA) is a highly regulated and selective process that leads to prefrential selection and packaging of dimeric gRNA from a cellular medium containing a large excess of cellular and spliced viral mRNAs. This event underlies interaction between the nucleocapsid domain in the context of the uncleaved Gag precursor and a Packaging signal located in the 5’ untranslated region (5’ UTR) of the gRNA and/or the beginning of gag gene. Despite a considerable effort, the molecular mechanisms beyond the selective encapsidation of HIV-1 gRNA is still unknown. To address this, we first characterized the relative affinities of Pr55gag to various HIV-1 RNA fragments (spliced and unspliced) by biochemical and spectroscopic approaches which all revealed that Pr55gag exhibits a higher binding affinity for viral gRNA than for viral spliced species. Interestingly, we noticed that Pr55Gag, through its nucleic acid chaperone activity, was able to stabilize the dimeric form of almost all viral RNA species (spliced and unspliced) suggesting that RNA dimermaturation does not allow the gRNA discrimination. Further characterization of specific Gag binding sites to short RNA fragments corresponding to the minimal packaging signal by competition experiments, inhibition of Gag/RNA interaction by antisense oligo-deoxynucleotides, as well as the detection of Pr55Gag RNA binding sites on gRNA by enzymatic and chemical footprinting confirmed the crucial role of SL1 (or DIS) as a specific binding site for Pr55Gag. Taken together, our results strongly suggest that SL1 and/or RNA dimerization is a specific recognition signal for Pr55Gag to specifically select and probably induce HIV-1 gRNA packaging
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Gay, Bernard. "Analyse ultra-microscopique de la morphologie et des interactions des protéines de capside de l'Adénovirus et du rétrovirus HIV-1 : I. Protéines de l'apex de la capside d'Adénovirus humain, penton base et fibre : oligomérisation et assemblage en cellules d'insecte. II. Précurseur de la protéine de capside du HIV-1(Pr55Gag) : expression et assemblage sous forme de protéine recombinante en système baculovirus-cellule d'insecte." Montpellier 1, 1994. http://www.theses.fr/1994MON1T025.

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4

Orthwein, Alexandre. "Analyse du trafic et de la distribution intracellulaire de la protéine Gag du VIH-1 dans les cellules HEK 293T : importance de l'efficacité de la relâche virale." Thèse, 2007. http://hdl.handle.net/1866/15171.

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Ajamian, Lara. "Interactions virus-hôte : implication de la protéine cellulaire Upf1 au niveau de la régulation de l'ARN du VIH-1." Thèse, 2007. http://hdl.handle.net/1866/7641.

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