Academic literature on the topic 'Subvirale Partikel'
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Journal articles on the topic "Subvirale Partikel"
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Rausch, Andreas, and Thomas Schanze. "Fractal Dimensions of Subviral Particle Movement." Current Directions in Biomedical Engineering 4, no. 1 (September 1, 2018): 79–82. http://dx.doi.org/10.1515/cdbme-2018-0020.
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AbstractThe development of new medicines against virus infections like the Marburg virus disease requires an accurate knowledge of the respective pathogens. Conventionally, this process is very time expensive. In cooperation with the Virology of the Philipps-University in Marburg an automatic tracking algorithm for subviral particles in fluorescence image sequences was developed and programmed. To expand the benefit for the pharmaceutical researchers, also the trackevaluations need to be widely automated. In this work, a new parameterizing-method facing the fractal dimensions of spline interpolated subviral particle tracks is presented and tested with simulated and real data. The results reveal a good potential to classify tracks and, thus, types of subviral particles in infected cells.
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Kaak, Michelle, Andreas Rausch, Dennis Müller, and Thomas Schanze. "Visualization and Parametrization of the Motion Behaviour of Subviral Particles." Current Directions in Biomedical Engineering 4, no. 1 (September 1, 2018): 359–62. http://dx.doi.org/10.1515/cdbme-2018-0086.
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AbstractThe development of a drug against pathogens of hemorrhagic fever, like the Marburg virus, is a great challenge. Therefore, accurate knowledge of the properties of subviral particles in the host cell must be obtained. The base for subviral particle analysis is a special fluorescence microscopy technique. In order to automate and visualize the subviral particles’ motion patterns, previously a tracking algorithm was developed. In this article a new algorithm to parameterize and visualize the achieved particle tracks is introduced. A good potential for a fast data recognition is shown, with constantly respecting a high usability for pharmaceutical researchers. This algorithm was tested on both simulated and real data and provides reproducible results.
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Patient, Romuald, Christophe Hourioux, Pierre-Yves Sizaret, Sylvie Trassard, Camille Sureau, and Philippe Roingeard. "Hepatitis B Virus Subviral Envelope Particle Morphogenesis and Intracellular Trafficking." Journal of Virology 81, no. 8 (January 31, 2007): 3842–51. http://dx.doi.org/10.1128/jvi.02741-06.
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ABSTRACT Hepatitis B virus (HBV) is unusual in that its surface proteins (small [S], medium, and large [L]) are not only incorporated into the virion envelope but they also bud into empty subviral particles in great excess over virions. The morphogenesis of these subviral envelope particles remains unclear, but the S protein is essential and sufficient for budding. We show here that, in contrast to the presumed model, the HBV subviral particle formed by the S protein self-assembles into branched filaments in the lumen of the endoplasmic reticulum (ER). These long filaments are then folded and bridged for packing into crystal-like structures, which are then transported by ER-derived vesicles to the ER-Golgi intermediate compartment (ERGIC). Within the ERGIC, they are unpacked and relaxed, and their size and shape probably limits further progression through the secretory pathway. Such progression requires their conversion into spherical particles, which occurred spontaneously during the purification of these filaments by affinity chromatography. Small branched filaments are also formed by the L protein in the ER lumen, but these filaments are not packed into transport vesicles. They are transported less efficiently to the ERGIC, potentially accounting for the retention of the L protein within cells. These findings shed light on an important step in the HBV infectious cycle, as the intracellular accumulation of HBV subviral filaments may be directly linked to viral pathogenesis.
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Tan, Ming, and Xi Jiang. "Subviral particle as vaccine and vaccine platform." Current Opinion in Virology 6 (June 2014): 24–33. http://dx.doi.org/10.1016/j.coviro.2014.02.009.
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Stange, Annett, Daniel Lüftenegger, Juliane Reh, Winfried Weissenhorn, and Dirk Lindemann. "Subviral Particle Release Determinants of Prototype Foamy Virus." Journal of Virology 82, no. 20 (August 6, 2008): 9858–69. http://dx.doi.org/10.1128/jvi.00949-08.
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ABSTRACT Glycoproteins of several viruses have the capacity to induce release of noninfectious, capsidless particulate structures containing only the viral glycoprotein. Such structures are often called subviral particles (SVP). Foamy viruses (FVs), a special type of retroviruses with a replication strategy combining features of both orthoretroviruses and hepadnaviruses, express a glycoprotein (Env) which has the ability to induce SVP release. However, unlike human hepatitis B virus, prototype FV (PFV) naturally secretes only small amounts of SVPs, because ubiquitination of the Env protein seems to suppress the intrinsic capacity for induction of SVP release. In this study, we characterized the structural determinants influencing PFV SVP release, examined the role of specific Env ubiquitination sites in the regulation of this process, and analyzed the requirement of the cellular vacuolar protein sorting (VPS) machinery for SVP egress. We observed that the cytoplasmic and membrane-spanning domains of both the leader peptide (LP) and the transmembrane (TM) subunit harbor essential as well as inhibitory domains. Furthermore, only ubiquitination at the most N-terminal lysine residues (K14 and K15) in LP reduced cell surface expression and suppressed SVP release to wild-type levels. This suggests that interaction of Env with cellular components required for SVP release suppression is effective only when Env is ubiquitinated at these lysine residues but not at others. Finally, SVP release was sensitive to dominant-negative mutants of late components, but not early components, of the cellular VPS machinery. PFV therefore differs from hepatitis B virus in using the same cellular pathway for egress of both virions and SVPs.
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Zhang, Jing, Yongxiang Wang, Shuwen Fu, Quan Yuan, Qianru Wang, Ningshao Xia, Yumei Wen, Jisu Li, and Shuping Tong. "Role of Small Envelope Protein in Sustaining the Intracellular and Extracellular Levels of Hepatitis B Virus Large and Middle Envelope Proteins." Viruses 13, no. 4 (April 2, 2021): 613. http://dx.doi.org/10.3390/v13040613.
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Hepatitis B virus (HBV) expresses co-terminal large (L), middle (M), and small (S) envelope proteins. S protein drives virion and subviral particle secretion, whereas L protein inhibits subviral particle secretion but coordinates virion morphogenesis. We previously found that preventing S protein expression from a subgenomic construct eliminated M protein. The present study further examined impact of S protein on L and M proteins. Mutations were introduced to subgenomic construct of genotype A or 1.1 mer replication construct of genotype A or D, and viral proteins were analyzed from transfected Huh7 cells. Mutating S gene ATG to prevent expression of full-length S protein eliminated M protein, reduced intracellular level of L protein despite its blocked secretion, and generated a truncated S protein through translation initiation from a downstream ATG. Truncated S protein was secretion deficient and could inhibit secretion of L, M, S proteins from wild-type constructs. Providing full-length S protein in trans rescued L protein secretion and increased its intracellular level from mutants of lost S gene ATG. Lost core protein expression reduced all the three envelope proteins. In conclusion, full-length S protein could sustain intracellular and extracellular L and M proteins, while truncated S protein could block subviral particle secretion.
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Garcia, Tamako, Jisu Li, Camille Sureau, Kiyoaki Ito, Yanli Qin, Jack Wands, and Shuping Tong. "Drastic Reduction in the Production of Subviral Particles Does Not Impair Hepatitis B Virus Virion Secretion." Journal of Virology 83, no. 21 (August 12, 2009): 11152–65. http://dx.doi.org/10.1128/jvi.00905-09.
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ABSTRACT Hepatitis B virus (HBV) contains three coterminal envelope proteins on the virion surface: large (L), middle (M), and small (S). The M and S proteins are also secreted as empty “subviral particles,” which exceed virions by at least 1,000-fold. The S protein serves as the morphogenic factor for both types of particles, while the L protein is required only for virion formation. We found that cotransfecting replication constructs with a small dose of the expression construct for the missing L, M, and S proteins reconstituted efficient virion secretion but only 5 to 10% of subviral particles. The L protein inhibited secretion of subviral particles in a dose-dependent manner, whereas a too-high or too-low L/S protein ratio inhibited virion secretion. Consistent with the results of cotransfection experiments, a point mutation at the −3 position of the S gene AUG codon reduced HBsAg secretion by 60 to 70% but maintained efficient virion secretion. Surprisingly, ablating M protein expression reduced virion secretion but markedly increased the maturity of virion-associated genomes, which could be reversed by providing in trans both L and M proteins but not just M protein. M protein stability was dependent on the coexpression of S protein. Our findings suggest that efficient HBV virion secretion could be maintained despite drastic reduction in subviral particle production, which supports the recent demonstration of separate secretion pathways adopted by the two types of particles. The M protein appears to facilitate core particle envelopment, thus shortening the window of plus strand DNA elongation.
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Op De Beeck, Anne, Richard Molenkamp, Mélanie Caron, Amena Ben Younes, Peter Bredenbeek, and Jean Dubuisson. "Role of the Transmembrane Domains of prM and E Proteins in the Formation of Yellow Fever Virus Envelope." Journal of Virology 77, no. 2 (January 15, 2003): 813–20. http://dx.doi.org/10.1128/jvi.77.2.813-820.2003.
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ABSTRACT Flavivirus envelope proteins have been shown to play a major role in virus assembly. These proteins are anchored into cellular and viral membranes by their C-terminal domain. These domains are composed of two hydrophobic stretches separated by a short hydrophilic segment containing at least one charged residue. We investigated the role of the transmembrane domains of prM and E in the envelope formation of the flavivirus yellow fever virus (YFV). Alanine scanning insertion mutagenesis has been used to examine the role of the transmembrane domains of prM and E in YFV subviral particle formation. Most of the insertions had a dramatic effect on the release of YFV subviral particles. Some of these mutations were introduced into the viral genome. The ability of these mutant viruses to produce infectious particles was severely reduced. The alanine insertions did not affect prM-E heterodimerization. In addition, replacement of the charged residues present in the middle of the transmembrane domains had no effect on subviral particle release. Taken together, these data indicate that the transmembrane domains of prM and E play a crucial role in the biogenesis of YFV envelope. In addition, these data indicate some differences between the transmembrane domains of the hepaciviruses and the flaviviruses.
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Chiang, Ying-Wei, Jaw-Chin Wu, Kuei-Chun Wang, Szu-Ting Chou, and Yu-Chen Hu. "Varied Properties of Hepatitis-Delta Virus-like Particles Produced by Baculovirus-Transduced Mammalian Cells." Open Biotechnology Journal 1, no. 1 (August 28, 2007): 34–40. http://dx.doi.org/10.2174/1874070700701010034.
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Hepatitis delta virus (HDV) is a defective virus that requires the supply of hepatitis B virus surface antigen (HBsAg) for replication and transmission. We have previously demonstrated that co-transduction of BHK cells with Bac- GD, a recombinant baculovirus expressing large hepatitis delta antigen (L-HDAg), and Bac-GS2, another recombinant baculovirus expressing HBsAg, gives rise to the assembly and secretion of 22 nm HBsAg subviral particles and 35-37 nm HDV-like particles (HDV VLP). In this study we uncovered oversize particles (>50 nm in diameter) comprised of HBsAg and L-HDAg and the particle properties varied with the relative dosages of Bac-GD and Bac-GS2, as demonstrated by Western blot, transmission electron microscopy and immunogold labeling. At a given Bac-GS2 dosage, decreasing the Bac-GD dosage resulted in the expression of more HBsAg, elevated secretion of HBsAg subviral particles, incorporation of more HBsAg into the HDV VLP, narrower particle size distribution and lower particle density. These data collectively demonstrated that the composition, and hence the properties, of HDV VLPs could be manipulated by altering the relative expression levels of structure proteins.
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Lawton, Jeffrey A., Mary K. Estes, and B. V. Venkataram Prasad. "Identification and Characterization of a Transcription Pause Site in Rotavirus." Journal of Virology 75, no. 4 (February 15, 2001): 1632–42. http://dx.doi.org/10.1128/jvi.75.4.1632-1642.2001.
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ABSTRACT In rotavirus, transcription of the 11 double-stranded RNA genome segments occurs within the structurally intact subviral particle, and nascent transcripts are released through channels penetrating the two capsid layers at the icosahedral vertices. To gain insight into the early molecular events in transcription, we used high-resolution polyacrylamide gel electrophoresis to investigate the length distribution of transcription products at various times following initiation. We observed that, in the subviral particle under normal conditions, transcript initiation and capping are followed by a momentary pause in elongation after the addition of 6 to 7 nucleotides. In the absence of the capping reaction cofactorS-adenosylmethionine, conditions under which the rate of nucleotide incorporation is reduced, we observe a significant decrease in the ratio of paused to full-length transcripts. We propose that this pause site may represent the point at which specific molecular events take place to facilitate processive elongation. Furthermore, our results indicate that the presence of specific ligands on the viral surface, such as VP7 in the mature virion, inhibits polymerase function. From the perspective of the viral replication cycle, this inhibition may serve to ensure that transcription occurs with greatest efficiency only after the virus has entered the cytoplasm and assumed the form of a double-layered particle.
Dissertations / Theses on the topic "Subvirale Partikel"
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Stange, Annett. "Determinanten und Mechanismen der foamyviralen Partikelfreisetzung." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2008. http://nbn-resolving.de/urn:nbn:de:bsz:14-ds-1210174421492-57147.
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Die Spumaretrovirinae, mit ihrer einzigen Gattung der Foamyviren (FV), nehmen aufgrund einer recht ungewöhnlichen Replikationsstrategie und Ähnlichkeiten mit den Hepadnaviren eine Sonderstellung innerhalb der Familie der Retroviren ein. Eine Besonderheit der FV ist, daß sie für die Partikelfreisetzung, im Gegensatz zu den Orthoretroviren, die beiden strukturellen Proteine Gag und Env benötigen. Das Gag- Protein trägt alle für den Kapsidzusammenbau nötigen strukturellen Komponenten, kann jedoch durch eine fehlende Membranbindungsdomäne nicht mit Zellmembranen assoziieren. Der Membrantransport der bereits im Zytoplasma zusammen gebauten FV Kapside wird vermutlich durch das FV Env-Protein vermittelt. Das FV Hüllprotein ist jedoch auch alleine zur Freisetzung von Kapsidlosen, Hüllprotein-haltigen subviralen Partikeln (SVP) fähig. Da eine Envunabhängige Freisetzung virus-ähnlicher Partikel durch ein FV Gag-Protein mit künstlichem Membrananker möglich ist, scheint das FV Gag-Protein auch essentielle strukturelle Elemente für die Partikelfreisetzung zu enthalten. In den letzten Jahren wurden große Fortschritte in der Erforschung der Freisetzung von membranumhüllten Viren und den daran beteiligten viralen Determinanten und zellulären Mechanismen gemacht. Wobei den meist in den viralen Kapsidproteinen vorkommenden Late (L)-Domänen und deren Interaktion mit dem zellulären Proteinsortierungsweg in Multivesikuläre Körperchen (MVB) eine besondere Bedeutung zu kommt. Über die FV virale und subvirale Partikelfreisetzung und die dabei involvierten strukturellen viralen Domänen und zellulären Proteinen war jedoch bisher wenig bekannt. Im Rahmen dieser Arbeit konnte durch Mutationsanalysen von drei potentiellen L-Domän Sequenzmotiven im Prototyp FV (PFV) Gag-Protein ein, innerhalb der Primaten FV konserviertes, PSAP Konsensusmotiv als funktionelle L-Domäne charakterisiert werden. Dessen Mutation führte zu klassischen L-Domän Defekten mit verringerter Partikelfreisetzung, sowie einer elektronenmikroskopisch sichtbaren Arretierung der Virusknospung und seine Funktion war durch homo- und heterologe L-Domän Motive anderer Retroviren teilweise oder vollständig ersetzbar. Ein PPPI Motiv in PFV Gag, mit Ähnlichkeit zur L-Domän PPXY Konsensussequenz, schien jedoch keinen Einfluß auf die FV Freisetzung zu besitzen. Die Charakterisierung eines in allen FV Gag-Proteinen konservierten YXXL Motivs ließ eher auf eine wichtige Rolle beim korrekten Kapsidzusammenbau, als auf eine klassische LDomän Funktion schließen. Eine korrekte Kapsidmorphogenese schien entscheidend für die reverse Transkription des Virusgenoms zu sein. Durch Koexpression verschiedener dominant-negativer Mutanten des zellulären ESCRT-Proteinssortierungsweges konnte gezeigt werden, daß die virale Partikelfreisetzung von PFV augenscheinlich dem generellen Model der Freisetzung vieler membranumhüllter Viren über das VPS-System folgt. Eine spezifische Interaktion des PFV Gag PSAP L-Domän Motivs mit TSG101, einer frühen Komponente der ESCRT-Komplexe, verbindet PFV mit dem VPS-Sortierungsweg der Zelle. Die besondere Fähigkeit des FV Env-Proteins zur Freisetzung von SVPs wurde bereits vor einiger Zeit entdeckt, dennoch war bisher nichts über die viralen und zellulären Determinanten bekannt, die zu einer Knospung des Env-Proteins in Vesikel führten. Durch eine Reihe von Deletions- und Mutationsanalysen des PFV Env-Proteins konnten in dieser Arbeit zwei für die SVP-Freisetzung inhibitorische Abschnitte am N- und C-Terminus der zytoplasmatischen Domänen des Env- Proteins ermittelt werden. Weiterhin wurden essentielle Sequenzen im Leaderpeptid, sowie die Notwendigkeit der Membranspannenden Domäne der Transmembran- Untereinheit für die SVP-Freisetzung festgestellt. Obwohl das PFV Env-Protein kein bekanntes L-Domän Sequenzmotiv enthält, konnte ein Einfluß später Komponenten der ESCRT-Maschinerie auf die SVP-Bildung beobachtet werden. Wobei die genaue Eintrittsstelle in den VPS-Weg im Rahmen dieser Arbeit nicht definiert werden konnte. Die vorgenommen Analysen lassen vermuten, daß die Bildung von SVPs durch die Konzentration der Env-Proteine in der Zellmembranen reguliert wird. Welche genauen Mechanismen dabei zu Grunde liegen und wieweit die zelluläre Ubiquitinylierungsmaschinerie involviert ist, bedarf jedoch weiterer Erforschung. Die Ergebnisse dieser Arbeit verdeutlichen erneut die Sonderstellung der FV innerhalb der Familie der Retroviren. Auf der einen Seite folgt die foamyvirale Viruspartikelfreisetzung den typischen Mechanismen der retroviralen Virusknospung. Andererseits zeigt die Freisetzung von subviralen Partikeln, die bei keinem anderen Retrovirus bisher beobachtet wurde, eine weitere Parallele zur Replikationsstrategie der Hepadnaviren auf.
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Stange, Annett. "Determinanten und Mechanismen der foamyviralen Partikelfreisetzung." Doctoral thesis, Technische Universität Dresden, 2007. https://tud.qucosa.de/id/qucosa%3A23849.
Full textAbstract:
Die Spumaretrovirinae, mit ihrer einzigen Gattung der Foamyviren (FV), nehmen aufgrund einer recht ungewöhnlichen Replikationsstrategie und Ähnlichkeiten mit den Hepadnaviren eine Sonderstellung innerhalb der Familie der Retroviren ein. Eine Besonderheit der FV ist, daß sie für die Partikelfreisetzung, im Gegensatz zu den Orthoretroviren, die beiden strukturellen Proteine Gag und Env benötigen. Das Gag- Protein trägt alle für den Kapsidzusammenbau nötigen strukturellen Komponenten, kann jedoch durch eine fehlende Membranbindungsdomäne nicht mit Zellmembranen assoziieren. Der Membrantransport der bereits im Zytoplasma zusammen gebauten FV Kapside wird vermutlich durch das FV Env-Protein vermittelt. Das FV Hüllprotein ist jedoch auch alleine zur Freisetzung von Kapsidlosen, Hüllprotein-haltigen subviralen Partikeln (SVP) fähig. Da eine Envunabhängige Freisetzung virus-ähnlicher Partikel durch ein FV Gag-Protein mit künstlichem Membrananker möglich ist, scheint das FV Gag-Protein auch essentielle strukturelle Elemente für die Partikelfreisetzung zu enthalten. In den letzten Jahren wurden große Fortschritte in der Erforschung der Freisetzung von membranumhüllten Viren und den daran beteiligten viralen Determinanten und zellulären Mechanismen gemacht. Wobei den meist in den viralen Kapsidproteinen vorkommenden Late (L)-Domänen und deren Interaktion mit dem zellulären Proteinsortierungsweg in Multivesikuläre Körperchen (MVB) eine besondere Bedeutung zu kommt. Über die FV virale und subvirale Partikelfreisetzung und die dabei involvierten strukturellen viralen Domänen und zellulären Proteinen war jedoch bisher wenig bekannt. Im Rahmen dieser Arbeit konnte durch Mutationsanalysen von drei potentiellen L-Domän Sequenzmotiven im Prototyp FV (PFV) Gag-Protein ein, innerhalb der Primaten FV konserviertes, PSAP Konsensusmotiv als funktionelle L-Domäne charakterisiert werden. Dessen Mutation führte zu klassischen L-Domän Defekten mit verringerter Partikelfreisetzung, sowie einer elektronenmikroskopisch sichtbaren Arretierung der Virusknospung und seine Funktion war durch homo- und heterologe L-Domän Motive anderer Retroviren teilweise oder vollständig ersetzbar. Ein PPPI Motiv in PFV Gag, mit Ähnlichkeit zur L-Domän PPXY Konsensussequenz, schien jedoch keinen Einfluß auf die FV Freisetzung zu besitzen. Die Charakterisierung eines in allen FV Gag-Proteinen konservierten YXXL Motivs ließ eher auf eine wichtige Rolle beim korrekten Kapsidzusammenbau, als auf eine klassische LDomän Funktion schließen. Eine korrekte Kapsidmorphogenese schien entscheidend für die reverse Transkription des Virusgenoms zu sein. Durch Koexpression verschiedener dominant-negativer Mutanten des zellulären ESCRT-Proteinssortierungsweges konnte gezeigt werden, daß die virale Partikelfreisetzung von PFV augenscheinlich dem generellen Model der Freisetzung vieler membranumhüllter Viren über das VPS-System folgt. Eine spezifische Interaktion des PFV Gag PSAP L-Domän Motivs mit TSG101, einer frühen Komponente der ESCRT-Komplexe, verbindet PFV mit dem VPS-Sortierungsweg der Zelle. Die besondere Fähigkeit des FV Env-Proteins zur Freisetzung von SVPs wurde bereits vor einiger Zeit entdeckt, dennoch war bisher nichts über die viralen und zellulären Determinanten bekannt, die zu einer Knospung des Env-Proteins in Vesikel führten. Durch eine Reihe von Deletions- und Mutationsanalysen des PFV Env-Proteins konnten in dieser Arbeit zwei für die SVP-Freisetzung inhibitorische Abschnitte am N- und C-Terminus der zytoplasmatischen Domänen des Env- Proteins ermittelt werden. Weiterhin wurden essentielle Sequenzen im Leaderpeptid, sowie die Notwendigkeit der Membranspannenden Domäne der Transmembran- Untereinheit für die SVP-Freisetzung festgestellt. Obwohl das PFV Env-Protein kein bekanntes L-Domän Sequenzmotiv enthält, konnte ein Einfluß später Komponenten der ESCRT-Maschinerie auf die SVP-Bildung beobachtet werden. Wobei die genaue Eintrittsstelle in den VPS-Weg im Rahmen dieser Arbeit nicht definiert werden konnte. Die vorgenommen Analysen lassen vermuten, daß die Bildung von SVPs durch die Konzentration der Env-Proteine in der Zellmembranen reguliert wird. Welche genauen Mechanismen dabei zu Grunde liegen und wieweit die zelluläre Ubiquitinylierungsmaschinerie involviert ist, bedarf jedoch weiterer Erforschung. Die Ergebnisse dieser Arbeit verdeutlichen erneut die Sonderstellung der FV innerhalb der Familie der Retroviren. Auf der einen Seite folgt die foamyvirale Viruspartikelfreisetzung den typischen Mechanismen der retroviralen Virusknospung. Andererseits zeigt die Freisetzung von subviralen Partikeln, die bei keinem anderen Retrovirus bisher beobachtet wurde, eine weitere Parallele zur Replikationsstrategie der Hepadnaviren auf.
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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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Sauer, Caroline [Verfasser]. "Einfluss subviraler Partikel des humanen Cytomegalovirus auf die Induktion der antiviralen Immunantwort / Caroline Sauer." Mainz : Universitätsbibliothek Mainz, 2014. http://d-nb.info/1046925202/34.
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Lo, Chung-yan Joanne, and 羅頌恩. "Characterization by electron microscopy of dengue virus egress using dengue recombinant subviral particle (RSPs) as a model." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2012. http://hub.hku.hk/bib/B48330115.
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Dengue is the most common mosquito-borne human disease, leading to 2.5 billion people at risk, 50-100 millions infections each year worldwide and among them, 500 000 severe dengue cases (dengue hemorrhagic fever, DHF/ dengue shock syndrome, DSS) plus more than 20 000 deaths. It can be caused by any of four dengue virus serotypes, which are antigenicly distinct and belong to the Flaviviridae family, genus Flavivirus. However, up till now there is no specific drug and vaccine against dengue. Understanding mechanisms developed by dengue virus to exploit host cells during all stages of the replication cycle is a first step towards the rationale design of anti-viral strategies. Very little is known about the late stages, which consist of assembly, budding and secretion of the virus. It is therefore very important to develop tools in order to study the egress of the virus.
In this study, I investigated a stable cell line named Hela-prME that expresses serotype 1 dengue virus (DENV-1) prM and E native structural envelope proteins and constitutively produces dengue recombinant subviral particles (RSPs). Biochemical characterization of DENV-1 RSPs has validated that this cell line is a potential tool to study the dengue viral late-stage. Indeed, the maturation process observed with RSPs is similar to the pathway described for real virus (cleavage of prM fragment, homodimerization of E, acquisition of complex sugars).
To better understand and depict the dengue virus late-stage secretion, I combined various electron microscopy (EM) techniques e.g. classical transmission electron microscopy (TEM), negative staining, immunogold labeling on cryo-ultrathin sections (Tokuyashu method) and tomography (ET) with such RSPs tool.
The EM results obtained illustrate that electron dense particles and tubules labeled by antibodies directed against E and prM proteins were abundantly found in the lumen of endoplasmic reticulum (ER)-related cisternae of HeLa prME cells. Epositive particles were also found in other structures such as Golgi stacks and vesicles nearby as well as in aggregates with electron dense materials inside and surrounded by membrane. These particles are most likely corresponding to DENV-1 RSPs whereas the tubules may be other structures induced by assembly of prM and E proteins.
This study has clearly shown that DENV-1 RSPs assemble in the ER and transport through the secretory pathway before being released. This work further validates the use of dengue RSPs and RSPs-producing cells as a model to study viral egress.published_or_final_version
Pathology
Master
Master of Philosophy
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Penner, Inessa [Verfasser]. "The impact of a human cytomegalovirus subviral particle vaccine on the host cell proteome and on virus replication / Inessa Penner." Mainz : Universitätsbibliothek der Johannes Gutenberg-Universität Mainz, 2021. http://d-nb.info/1239239106/34.
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Siegler, Vera [Verfasser], Wolfgang [Akademischer Betreuer] Liebl, and Volker [Akademischer Betreuer] Bruß. "Charakterisierung der Rolle der Transmembrandomänen des kleinen Hepatitis B Virus Hüllproteins für die Bildung von subviralen Partikeln / Vera Siegler. Gutachter: Volker Bruß. Betreuer: Wolfgang Liebl." München : Universitätsbibliothek der TU München, 2012. http://d-nb.info/1021975397/34.
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Wu, Bo-Yi, and 吳柏逸. "Separation and Identification of IBDV Subviral Particle by Capillary Zone Electrophoresis." Thesis, 2013. http://ndltd.ncl.edu.tw/handle/g2283e.
Full textAbstract:
碩士國立中興大學
微生物暨公共衛生學研究所
101
Abstract Capillary zone electrophoresis (CZE) has been successfully used for characterizing and analyzing proteins. Infectious bursal disease virus (IBDV) is a double-stranded RNA virus with an icosahedral capsid of 55-65 nm in diameter (T=13) and belonging to the Birnaviridae family, causes immunosuppression in young chickens. The major structure protein VP2 of IBDV is response to the induction of efficacious protection. To express the VP2 protein alone in E. coli has been demonstrated to produce icosahedral particles of 25 nm in diameter (T=1), subviral particles (SVP). The integrity of SVP is highly related to the induction of protection against IBD. Therefore, a method used to quality control vaccine containing SVP requires the ability to detect the intact SVP. The objective of this study is to setup a CZE for separation and identification of SVP of IBDV expressed by E. coli. The SVP was expressed by E. coli and confirmed by Western blotting and electron microscopy. The expressed SVP were purified and concentrated by acid precipitation, sucrose gradient, and the size-exclusion column (Amicon). The CZE system with an inner diameter of 75 μm fused silica capillary, pressure injection and 50 mM Boric acid pH 9 separation buffer was used to analyze the SVP. The SVP with complete purification and concentration steps showed single peak in CZE with a migration time of 2.65 min. After adding anti-VP2 antibody, the SVP-antibody complex showed single peak with a migration time of 1.8 min. The CZE, were used to detect various amounts of SVP, anti-VP2 ab, and the R2 of standard curve, were 0.99, 0.98, respectively. The results indicated that CZE is valuable method in separation and identification of the SVP. The method is an important tool of SVP statistical quality control.
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Lo, Chao-Jung, and 羅紹榮. "Isolation of putative Infectious bursal disease virus receptor molecules in DF-1 cells using VP2-formed subviral particle ligand." Thesis, 2006. http://ndltd.ncl.edu.tw/handle/73635734070167036945.
Full textAbstract:
碩士國立中興大學
生物科技學研究所
94
Infectious bursal disease virus (IBDV) causes a highly contagious disease in young chicks and leads to significant economic losses in the poultry industry. The outer capsid protein VP2 of IBDV has been suggested to play an role in virus binding and cell recongnition. VP2 can form a particle called subvirus particle (SVP) of 25 nm in diameter, when it was expressed in insect cells. VP2 SVP can suppress the infection of IBDV to DF-1 cells, an IBDV susceptible cell line and isolated form chicken embryo fibroblast cell. We design a system to isolate proteins which interact with VP2 SVP in DF-1 cells by immobilized metal affinity chromatography (IMAC) using VP2 SVP as a ligand. The results show that an 80~90 kDa protein molecule (p90) from DF-1 cells with a strong interaction with VP2 SVP was purified. We also demonstrate that p90 was located on the surface of the DF-1 cells and identified p90 as chicken heat shock protein 90 (HSP90) by liquid-chromatography mass spectrometry (LC-MS/MS). The results suggest Hsp90 may be involved in the recognition of host cells and IBDV, and the entry of IBDV to DF-1 cells.
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Chen, Yi-Huei, and 陳宜暉. "Investigation of the roles of His249＆His253 on the affinity of Infectious Bursal Disease Virus Subviral particle and IMAC by Site Directed Mutagenesis." Thesis, 2007. http://ndltd.ncl.edu.tw/handle/02113677431280827408.
Full textAbstract:
碩士國立中興大學
生物科技學研究所
95
In previous research, it demonstrated that Immobilized Metal ion Affinity Chormatography column（IMAC）not only can purify the His-tag fusion IBDV VP2-452H subviral particle （SVP）, but also can purify the IBDV VP2-441 subviral particle without his-tag fusion. Therefore, the VP2 protein absorption with IMAC is not depending on the His-tag. It was suggested that SVP purified by IMAC was due to its surface amino acid residues of VP2. Two histidine residues which were located on the most exposed loops (Loop DE) may engage directly in contact with the immobilized Ni2+ ions. In this work, we engineered SVP surface amino acid, His-249 or His-253, which is related with IMAC absorption, and produced three mutants, VP2-441-H249.253A, VP2-441-H253A and VP2-441-H249A. Mutants VP2-441-H249.253A and VP2-441-H249A were expressed in E.coli and VP2-441-H253A was expressed in both E.coli and baculovirus expression system. After purification by ultracentrifugation, the VP2 SVP assembled as 20~23 nm particles which can be visualized under Transmission electromicroscopy (TEM). The results show that histidine mutation will not affect the self assembly of SVP. However, the three SVP mutants are present in the flow-through and pH 7.8 binding buffer eluent after IMAC purification. It indicates that these three mutants had lost the absorption ability with IMAC and provides evidence that the His 249 and His253 of VP2 play an important role in the binding affinity of SVP with Ni2+ ion of IMAC.
Book chapters on the topic "Subvirale Partikel"
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Kienzle, Christian, Gordian Schudt, Stephan Becker, and Thomas Schanze. "Multiple Subviral Particle in Fluorecsence Microscopy Sequences." In Informatik aktuell, 330–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-54111-7_61.
Full textConference papers on the topic "Subvirale Partikel"
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Rausch, Andreas, and Thomas Schanze. "Fractal Characterization of Subviral Particle Motion: On the Influence of Spatio-Temporal Interpolation Methods." In 2019 41st Annual International Conference of the IEEE Engineering in Medicine & Biology Society (EMBC). IEEE, 2019. http://dx.doi.org/10.1109/embc.2019.8857721.
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