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Auswahl der wissenschaftlichen Literatur zum Thema „Viral fusion glycoproteins“
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Zeitschriftenartikel zum Thema "Viral fusion glycoproteins"
Oliver, Michael R., Kamilla Toon, Charlotte B. Lewis, Stephen Devlin, Robert J. Gifford und Joe Grove. „Structures of the Hepaci-, Pegi-, and Pestiviruses envelope proteins suggest a novel membrane fusion mechanism“. PLOS Biology 21, Nr. 7 (11.07.2023): e3002174. http://dx.doi.org/10.1371/journal.pbio.3002174.
Der volle Inhalt der QuelleQuinn, Derek J., Neil V. McFerran, John Nelson und W. Paul Duprex. „Live-cell visualization of transmembrane protein oligomerization and membrane fusion using two-fragment haptoEGFP methodology“. Bioscience Reports 32, Nr. 3 (29.03.2012): 333–43. http://dx.doi.org/10.1042/bsr20110100.
Der volle Inhalt der QuelleLibersou, Sonia, Aurélie A. V. Albertini, Malika Ouldali, Virginie Maury, Christine Maheu, Hélène Raux, Felix de Haas, Stéphane Roche, Yves Gaudin und Jean Lepault. „Distinct structural rearrangements of the VSV glycoprotein drive membrane fusion“. Journal of Cell Biology 191, Nr. 1 (04.10.2010): 199–210. http://dx.doi.org/10.1083/jcb.201006116.
Der volle Inhalt der QuelleLay Mendoza, Maria Fernanda, Marissa Danielle Acciani, Courtney Nina Levit, Christopher Santa Maria und Melinda Ann Brindley. „Monitoring Viral Entry in Real-Time Using a Luciferase Recombinant Vesicular Stomatitis Virus Producing SARS-CoV-2, EBOV, LASV, CHIKV, and VSV Glycoproteins“. Viruses 12, Nr. 12 (17.12.2020): 1457. http://dx.doi.org/10.3390/v12121457.
Der volle Inhalt der QuelleJambunathan, Nithya, Carolyn M. Clark, Farhana Musarrat, Vladimir N. Chouljenko, Jared Rudd und Konstantin G. Kousoulas. „Two Sides to Every Story: Herpes Simplex Type-1 Viral Glycoproteins gB, gD, gH/gL, gK, and Cellular Receptors Function as Key Players in Membrane Fusion“. Viruses 13, Nr. 9 (16.09.2021): 1849. http://dx.doi.org/10.3390/v13091849.
Der volle Inhalt der QuelleZhang, You, Joanne York, Melinda A. Brindley, Jack H. Nunberg und Gregory B. Melikyan. „Fusogenic structural changes in arenavirus glycoproteins are associated with viroporin activity“. PLOS Pathogens 19, Nr. 7 (26.07.2023): e1011217. http://dx.doi.org/10.1371/journal.ppat.1011217.
Der volle Inhalt der QuelleJackson, Julia O., und Richard Longnecker. „Reevaluating Herpes Simplex Virus Hemifusion“. Journal of Virology 84, Nr. 22 (15.09.2010): 11814–21. http://dx.doi.org/10.1128/jvi.01615-10.
Der volle Inhalt der QuelleMelder, Deborah C., Xueqian Yin, Sue E. Delos und Mark J. Federspiel. „A Charged Second-Site Mutation in the Fusion Peptide Rescues Replication of a Mutant Avian Sarcoma and Leukosis Virus Lacking Critical Cysteine Residues Flanking the Internal Fusion Domain“. Journal of Virology 83, Nr. 17 (10.06.2009): 8575–86. http://dx.doi.org/10.1128/jvi.00526-09.
Der volle Inhalt der QuelleYang, Xinzhen, Svetla Kurteva, Xinping Ren, Sandra Lee und Joseph Sodroski. „Subunit Stoichiometry of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers during Virus Entry into Host Cells“. Journal of Virology 80, Nr. 9 (01.05.2006): 4388–95. http://dx.doi.org/10.1128/jvi.80.9.4388-4395.2006.
Der volle Inhalt der QuelleKinzler, Eric R., und Teresa Compton. „Characterization of Human Cytomegalovirus Glycoprotein-Induced Cell-Cell Fusion“. Journal of Virology 79, Nr. 12 (15.06.2005): 7827–37. http://dx.doi.org/10.1128/jvi.79.12.7827-7837.2005.
Der volle Inhalt der QuelleDissertationen zum Thema "Viral fusion glycoproteins"
Vasiliauskaite, Ieva. „Structural characterization of viral envelope glycoproteins“. Thesis, Paris 6, 2014. http://www.theses.fr/2014PA066507/document.
Der volle Inhalt der QuelleViral glycoproteins are responsible for the two major steps in entry into host cells by enveloped viruses: 1) attachment to cellular receptor/s and 2) fusion of the viral and cellular membranes. My thesis concentrated first on the structural analysis of the major envelope glycoprotein E2 of two hepaciviruses: GB virus B (GBV-B) and hepatitis C virus (HCV). Crystallization of the GBV-B E2 ectodomain remained unsuccessful, but the characterization of truncated versions of E2 suggested an important role of its C-terminal moiety in receptor binding. In parallel, I co-crystallized a synthetic peptide mimicking HCV E2 with an antibody fragment directed against the major receptor-binding loop of E2 that is targeted by broadly neutralizing antibodies. The structure unexpectedly revealed an α-helical peptide conformation, which is in stark contrast to the extended conformation of this region observed in the structure of an E2 core fragment. Together with further biochemical evidence this suggests an unanticipated structural flexibility within this region in the context of the soluble E2 ectodomain. Secondly, I focused on the structural analysis of the baculovirus glycoprotein F. I determined the crystal structure of the post-fusion trimer of a trypsin-truncated F fragment. This structure confirmed previous predictions that baculovirus F protein adopts a class I fusion protein fold and is homologous to the paramyxovirus F protein. Baculovirus F is therefore the first class I fusion protein encoded by a DNA virus. My results support the hypothesis that F proteins may have a common ancestor and imply interesting evolutionary links between DNA and RNA viruses and their hosts
Vasiliauskaite, Ieva. „Structural characterization of viral envelope glycoproteins“. Electronic Thesis or Diss., Paris 6, 2014. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2014PA066507.pdf.
Der volle Inhalt der QuelleViral glycoproteins are responsible for the two major steps in entry into host cells by enveloped viruses: 1) attachment to cellular receptor/s and 2) fusion of the viral and cellular membranes. My thesis concentrated first on the structural analysis of the major envelope glycoprotein E2 of two hepaciviruses: GB virus B (GBV-B) and hepatitis C virus (HCV). Crystallization of the GBV-B E2 ectodomain remained unsuccessful, but the characterization of truncated versions of E2 suggested an important role of its C-terminal moiety in receptor binding. In parallel, I co-crystallized a synthetic peptide mimicking HCV E2 with an antibody fragment directed against the major receptor-binding loop of E2 that is targeted by broadly neutralizing antibodies. The structure unexpectedly revealed an α-helical peptide conformation, which is in stark contrast to the extended conformation of this region observed in the structure of an E2 core fragment. Together with further biochemical evidence this suggests an unanticipated structural flexibility within this region in the context of the soluble E2 ectodomain. Secondly, I focused on the structural analysis of the baculovirus glycoprotein F. I determined the crystal structure of the post-fusion trimer of a trypsin-truncated F fragment. This structure confirmed previous predictions that baculovirus F protein adopts a class I fusion protein fold and is homologous to the paramyxovirus F protein. Baculovirus F is therefore the first class I fusion protein encoded by a DNA virus. My results support the hypothesis that F proteins may have a common ancestor and imply interesting evolutionary links between DNA and RNA viruses and their hosts
Howard, Megan Wilder. „Coronavirus mediated membrane fusion /“. Connect to full text via ProQuest. Limited to UCD Anschutz Medical Campus, 2008. http://proquest.umi.com/pqdweb?did=1552538711&sid=1&Fmt=6&clientId=18952&RQT=309&VName=PQD.
Der volle Inhalt der QuelleTypescript. Includes bibliographical references (leaves 161-183). Free to UCD Anschutz Medical Campus. Online version available via ProQuest Digital Dissertations;
Melanson, Vanessa R. „Characterization of the Interaction Between the Attachment and Fusion Glycoproteins Required for Paramyxovirus Fusion: a Dissertation“. eScholarship@UMMS, 2005. https://escholarship.umassmed.edu/gsbs_diss/24.
Der volle Inhalt der QuelleCorey, Elizabeth Ann. „Characterization of the Relationship Between Measles Virus Fusion, Receptor Binding, and the Virus-Specific Interaction Between the Hemagglutinin and Fusion Glycoproteins: a Dissertation“. eScholarship@UMMS, 2006. https://escholarship.umassmed.edu/gsbs_diss/221.
Der volle Inhalt der QuelleWu, Shang-Rung. „Activation of the spike proteins of alpha- and retroviruses“. Stockholm, 2009. http://diss.kib.ki.se/2009/978-91-7409-736-8/.
Der volle Inhalt der QuelleMinoves, Marie. „Etude fonctionnelle et structurale de la glycoprotéine du virus de la Stomatite Vésiculaire et des Lyssavirus“. Electronic Thesis or Diss., université Paris-Saclay, 2024. http://www.theses.fr/2024UPASL068.
Der volle Inhalt der QuelleVesicular stomatitis virus (VSV), an enveloped virus, is the prototype species of the genus Vesiculovirus within the family Rhabdoviridae. Its G glycoprotein is responsible for receptor recognition, on the host cell surface, that triggers clathrin-mediated endocytosis of VSV. Then, within the acidic environment of the endosome, VSV G undergoes a fusogenic conformational change from the pre-fusion form of G to its post-fusion form, leading the fusion of both membranes. G is also the target of virus-neutralizing antibodies. Both structures of the pre- and post-fusion forms of the soluble ectodomain of G (i.e. without its transmembrane part) were determined by radiocrystallography. These structures established G as the prototype of class III fusion glycoproteins. However, the organization of the carboxyterminal part of the ectodomain and the transmembrane domain of G, which play an important role during the fusion process, remains unknown. Therefore, we carried out a cryo-electron microscopy study on the complete glycoprotein, directly purified from viral particles, alone or in complex with a monoclonal antibody. This study led to complete the structures of the ectodomain in its pre- and post-fusion conformations. It also revealed that the transmembrane domains are mobile within the membrane. We have also solved two structures of G in complex with a FAb derived from a neutralizing antibody, recognizing both pre- and post-fusion forms of G from several strains of Vesiculovirus. Based on these first structures of a complex between G and an antibody, we could characterize the epitope, identify the key G residues in the interaction and propose a neutralization mechanism. This work significantly increases our knowledge of the structure of G, which is the most widely used glycoprotein in biotechnology for cargo delivery and in gene therapy (by lentivirus pseudotyping).We also initiated a study aimed at characterizing the glycoproteins of Lyssaviruses, a genus also part of the Rhabdoviridae family, and for which rabies virus is the prototype. We produced and purified the ectodomains of several Lyssaviruses, and we were able to obtain a crystallographic structure of the ectodomain of Ikoma virus (IKOV G), which corresponds to a late monomeric intermediate. Several approaches are underway to further characterize this structure. We also carried out a phage display selection of alphaReps directed against IKOV G. Alphareps are artificial proteins binders consisting of helical repeats. 6 out of 11 alphareps are able to bind IKOVG. Complexes of IKOV G with alphareps are currently being characterized. We plan to i) use these tools as crystallization helpers to trap different conformations of G in crystallography or cryo-EM ii) evaluate the potential antiviral activity of these alphareps
Ferlin, Anna. „Characterization of vesicular stomatitis virus of glycoprotein mutants affected in their structural transition“. Paris 7, 2013. http://www.theses.fr/2013PA077262.
Der volle Inhalt der QuelleThe structure of the pre- and post-fusion of VSV G states have been elucidated by X-ray crystallography,allowing the identification of some amino acid residues which could play the role of pH-dependent molecular switches,triggering the conformational change from the post- toward the pre-fusion state. To confirm this,these acidic amino acids were mutated,creating single(D268L,N,V;D274N;E276Q;D393N;D395N) and double mutants (D274N-D395N,E276Q-D393N). Their expression,folding and transport to the tell membrane were analyzed by immunofluorescence and FACS. A cell-cell fusion assay showed that most of these mutants are affected in their membrane fusion properties. Particularly,mutants D268L/V/N have completely lost their fusion activity. We demonstrated that D268LN are trapped in their post-fusion state whereas the mutation D268N,which results in the creation of an efficient glycosylation, is unable to form the post fusion trimer. All these mutants, except mutant E276Q, do not or very inefficiently pseudotype a virus lacking the glycoprotein gene. Surprisingly,the stabilization of the post fusion trimer precludes G incorporation into the viral particles. We used a reverse genetic approach to produce recombinant viral particles. Most of the mutants immediately reverted toward the wild type sequence indicating the importance of the wild type sequence in this region. These data demonstrate that the residues identified are indeed regulators of G conformational change and that D268 is the major pH sensitive switch. It also suggests that the conformation of G regulates its incorporation in nascent particles and/or the release of viral nucleocapsid into the cytoplasm alter fusion
Hutchinson, Lloyd M. „Glycoprotein K of herpes simplex virus (HSV), role in viral egress and HSV-induced cell-cell fusion“. Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0016/NQ30094.pdf.
Der volle Inhalt der QuelleVoss, James. „Chikungunya envelope glycoprotein structure at neutral PH determined by X-ray crystallography“. Paris 7, 2011. http://www.theses.fr/2011PA077021.
Der volle Inhalt der QuelleChikungunya is an emerging mosquito-bome alphavirus that has caused widespread outbreaks of debilitating human disease in the past five years. CHIKV invasion of susceptible cells is mediated by two viral glycoproteins, E1 and E2, which carry the main antigenic determinants and form an icosahedral shell at the virion surface. Glycoprotein E2, derived from furin cleavage of the p62 precursor to E3 and E2 is responsible for receptor binding and is the major viral antigen. The E1 protein is responsible for inducing the fusion of viral and cellular membranes in the target cell endosome which is required for release of the viral nucleocapsid into the cytoplasm to initiale infection of a cell. While the structure of E1 has been determined, the structure of E2"has remained elusive over the years. This thesis reports the atomic structures of the mature (E3/E2/E1) and immature (P62/E1) envelope glycoprotein complexes from Chikungunya virus determined by X-ray crystallography using a recombinant protein construct. This construct contained the covalently linked ectodomains of p62 and E1. Diffracting crystals of the purified complexes were obtained at neutral pH when the linker joining the ectodomains was cleaved. The glycoprotein structures were fit into reconstructions of the alphavirus virion obtained from cryo-electron microscopy (cryoEM). This analysis resulted in an inferred atomic model of the entire 25MDa surface of the highly conserved alphavirus virion and allowed for the synthesis of a wealth of genetic, biochemical, immunological and electron microscopy data accumulated over the years on alphaviruses in general
Buchteile zum Thema "Viral fusion glycoproteins"
Bossart, Katharine N., und Christopher C. Broder. „Viral Glycoprotein-Mediated Cell Fusion Assays Using Vaccinia Virus Vectors“. In Vaccinia Virus and Poxvirology, 309–31. Totowa, NJ: Humana Press, 2004. http://dx.doi.org/10.1385/1-59259-789-0:309.
Der volle Inhalt der QuelleYi, Yanjie, Anjali Singh, Joanne Cutilli und Ronald G. Collman. „Use of Dual Recombinant Vaccinia Virus Vectors to Assay Viral Glycoprotein-Mediated Fusion with Transfection-Resistant Primary Cell Targets“. In Vaccinia Virus and Poxvirology, 333–46. Totowa, NJ: Humana Press, 2004. http://dx.doi.org/10.1385/1-59259-789-0:333.
Der volle Inhalt der QuelleOpstal, O. Van, L. Fabry, M. Francotte, C. Thiriart und C. Bruck. „Envelope expression and purification“. In HIV, 105–22. Oxford University PressOxford, 1995. http://dx.doi.org/10.1093/oso/9780199634996.003.0007.
Der volle Inhalt der QuelleMorris, Stephen J., Joshua Zimmerberg, Debi P. Sarkar und Robert Blumenthal. „[4] Kinetics of cell fusion mediated by viral spike glycoproteins“. In Methods in Enzymology, 42–58. Elsevier, 1993. http://dx.doi.org/10.1016/0076-6879(93)21006-t.
Der volle Inhalt der QuelleKumar Chatterjee, Swapan, und Snigdha Saha. „Glycan and Its Role in Combating COVID-19“. In Biotechnology to Combat COVID-19 [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97240.
Der volle Inhalt der QuelleMcknight, Aine, Paul R. ClaPham und Thomas F. Schulz. „Detection of HIV entry into cells“. In HIV, 129–42. Oxford University PressOxford, 1995. http://dx.doi.org/10.1093/oso/9780199634934.003.0008.
Der volle Inhalt der QuelleScholar, Eric M., und William B. Pratt. „Chemotherapy of Viral Infections, II“. In The Antimicrobial Drugs, 550–86. Oxford University PressNew York, NY, 2000. http://dx.doi.org/10.1093/oso/9780195125283.003.0017.
Der volle Inhalt der QuelleClercq, Erik De, Anne-Mieke Vandamme, Dominique Schols und Zeger Debyser. „Enzyme Targets as an Approach to Therapy for HIV Infections“. In Pre-Equilibrium Nuclear Reactions, 192–343. Oxford University PressOxford, 1992. http://dx.doi.org/10.1093/oso/9780198517344.003.0006.
Der volle Inhalt der QuelleMulchandani, Manisha, Amit Kumar Palai, Anjali Bhosale, Farhan Mazahir und Awesh K. Yadav. „Targeting the Viral Entry Pathways through Repurposed Drugs in Sars-Cov-2 Infection“. In Drug Repurposing Against SARS-CoV-2, 72–99. BENTHAM SCIENCE PUBLISHERS, 2023. http://dx.doi.org/10.2174/9789815123197123010007.
Der volle Inhalt der QuelleRay, Sujay, und Arundhati Banerjee. „In Silico Perspective into Interactions and Mutations in Human TLR4 and Ebola Glycoprotein“. In Advances in Medical Technologies and Clinical Practice, 209–31. IGI Global, 2016. http://dx.doi.org/10.4018/978-1-5225-0362-0.ch008.
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