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Relevant bibliographies by topics / Viral fusion glycoproteins

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Journal articles

Academic literature on the topic 'Viral fusion glycoproteins'

Author: Grafiati

Published: 14 December 2024

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Journal articles on the topic "Viral fusion glycoproteins"

1

Oliver, Michael R., Kamilla Toon, Charlotte B. Lewis, Stephen Devlin, Robert J. Gifford, and Joe Grove. "Structures of the Hepaci-, Pegi-, and Pestiviruses envelope proteins suggest a novel membrane fusion mechanism." PLOS Biology 21, no. 7 (2023): e3002174. http://dx.doi.org/10.1371/journal.pbio.3002174.

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Enveloped viruses encode specialised glycoproteins that mediate fusion of viral and host membranes. Discovery and understanding of the molecular mechanisms of fusion have been achieved through structural analyses of glycoproteins from many different viruses, and yet the fusion mechanisms of some viral genera remain unknown. We have employed systematic genome annotation and AlphaFold modelling to predict the structures of the E1E2 glycoproteins from 60 viral species in the Hepacivirus, Pegivirus, and Pestivirus genera. While the predicted structure of E2 varied widely, E1 exhibited a very consi

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2

Quinn, Derek J., Neil V. McFerran, John Nelson, and W. Paul Duprex. "Live-cell visualization of transmembrane protein oligomerization and membrane fusion using two-fragment haptoEGFP methodology." Bioscience Reports 32, no. 3 (2012): 333–43. http://dx.doi.org/10.1042/bsr20110100.

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Protein interactions play key roles throughout all subcellular compartments. In the present paper, we report the visualization of protein interactions throughout living mammalian cells using two oligomerizing MV (measles virus) transmembrane glycoproteins, the H (haemagglutinin) and the F (fusion) glycoproteins, which mediate MV entry into permissive cells. BiFC (bimolecular fluorescence complementation) has been used to examine the dimerization of these viral glycoproteins. The H glycoprotein is a type II membrane-receptor-binding homodimeric glycoprotein and the F glycoprotein is a type I di

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3

Libersou, Sonia, Aurélie A. V. Albertini, Malika Ouldali, et al. "Distinct structural rearrangements of the VSV glycoprotein drive membrane fusion." Journal of Cell Biology 191, no. 1 (2010): 199–210. http://dx.doi.org/10.1083/jcb.201006116.

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The entry of enveloped viruses into cells requires the fusion of viral and cellular membranes, driven by conformational changes in viral glycoproteins. Many studies have shown that fusion involves the cooperative action of a large number of these glycoproteins, but the underlying mechanisms are unknown. We used electron microscopy and tomography to study the low pH–induced fusion reaction catalyzed by vesicular stomatitis virus glycoprotein (G). Pre- and post-fusion crystal structures were observed on virions at high and low pH, respectively. Individual fusion events with liposomes were also v

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4

Lay Mendoza, Maria Fernanda, Marissa Danielle Acciani, Courtney Nina Levit, Christopher Santa Maria, and 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, no. 12 (2020): 1457. http://dx.doi.org/10.3390/v12121457.

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Viral entry is the first stage in the virus replication cycle and, for enveloped viruses, is mediated by virally encoded glycoproteins. Viral glycoproteins have different receptor affinities and triggering mechanisms. We employed vesicular stomatitis virus (VSV), a BSL-2 enveloped virus that can incorporate non-native glycoproteins, to examine the entry efficiencies of diverse viral glycoproteins. To compare the glycoprotein-mediated entry efficiencies of VSV glycoprotein (G), Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike (S), Ebola (EBOV) glycoprotein (GP), Lassa (LASV) G

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5

Jambunathan, Nithya, Carolyn M. Clark, Farhana Musarrat, Vladimir N. Chouljenko, Jared Rudd, and 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, no. 9 (2021): 1849. http://dx.doi.org/10.3390/v13091849.

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Herpes simplex virus type-1 (HSV-1) and type-2 (HSV-2) are prototypical alphaherpesviruses that are characterized by their unique properties to infect trigeminal and dorsal root ganglionic neurons, respectively, and establish life-long latent infections. These viruses initially infect mucosal epithelial tissues and subsequently spread to neurons. They are associated with a significant disease spectrum, including orofacial and ocular infections for HSV-1 and genital and neonatal infections for HSV-2. Viral glycoproteins within the virion envelope bind to specific cellular receptors to mediate v

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6

Zhang, You, Joanne York, Melinda A. Brindley, Jack H. Nunberg, and Gregory B. Melikyan. "Fusogenic structural changes in arenavirus glycoproteins are associated with viroporin activity." PLOS Pathogens 19, no. 7 (2023): e1011217. http://dx.doi.org/10.1371/journal.ppat.1011217.

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Many enveloped viruses enter host cells by fusing with acidic endosomes. The fusion activity of multiple viral envelope glycoproteins does not generally affect viral membrane permeability. However, fusion induced by the Lassa virus (LASV) glycoprotein complex (GPc) is always preceded by an increase in viral membrane permeability and the ensuing acidification of the virion interior. Here, systematic investigation of this LASV fusion phenotype using single pseudovirus tracking in live cells reveals that the change in membrane barrier function is associated with the fusogenic conformational reorg

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7

Jackson, Julia O., and Richard Longnecker. "Reevaluating Herpes Simplex Virus Hemifusion." Journal of Virology 84, no. 22 (2010): 11814–21. http://dx.doi.org/10.1128/jvi.01615-10.

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ABSTRACT Membrane fusion induced by enveloped viruses proceeds through the actions of viral fusion proteins. Once activated, viral fusion proteins undergo large protein conformational changes to execute membrane fusion. Fusion is thought to proceed through a “hemifusion” intermediate in which the outer membrane leaflets of target and viral membranes mix (lipid mixing) prior to fusion pore formation, enlargement, and completion of fusion. Herpes simplex virus type 1 (HSV-1) requires four glycoproteins—glycoprotein D (gD), glycoprotein B (gB), and a heterodimer of glycoprotein H and L (gH/gL)—to

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8

Melder, Deborah C., Xueqian Yin, Sue E. Delos, and 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, no. 17 (2009): 8575–86. http://dx.doi.org/10.1128/jvi.00526-09.

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ABSTRACT The entry process of the avian sarcoma and leukosis virus (ASLV) family of retroviruses requires first a specific interaction between the viral surface (SU) glycoproteins and a receptor on the cell surface at a neutral pH, triggering conformational changes in the viral SU and transmembrane (TM) glycoproteins, followed by exposure to low pH to complete fusion. The ASLV TM glycoprotein has been proposed to adopt a structure similar to that of the Ebola virus GP2 protein: each contains an internal fusion peptide flanked by cysteine residues predicted to be in a disulfide bond. In a previ

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9

Yang, Xinzhen, Svetla Kurteva, Xinping Ren, Sandra Lee, and Joseph Sodroski. "Subunit Stoichiometry of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers during Virus Entry into Host Cells." Journal of Virology 80, no. 9 (2006): 4388–95. http://dx.doi.org/10.1128/jvi.80.9.4388-4395.2006.

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ABSTRACT The envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) function as a homotrimer of gp120/gp41 heterodimers to support virus entry. During the process of virus entry, an individual HIV-1 envelope glycoprotein trimer binds the cellular receptors CD4 and CCR5/CXCR4 and mediates the fusion of the viral and the target cellular membranes. By studying the function of heterotrimers between wild-type and nonfunctional mutant envelope glycoproteins, we found that two wild-type subunits within an envelope glycoprotein trimer are required to support virus entry. Complementation

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10

Kinzler, Eric R., and Teresa Compton. "Characterization of Human Cytomegalovirus Glycoprotein-Induced Cell-Cell Fusion." Journal of Virology 79, no. 12 (2005): 7827–37. http://dx.doi.org/10.1128/jvi.79.12.7827-7837.2005.

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ABSTRACT Human cytomegalovirus (CMV) infection is dependent on the functions of structural glycoproteins at multiple stages of the viral life cycle. These proteins mediate the initial attachment and fusion events that occur between the viral envelope and a host cell membrane, as well as virion-independent cell-cell spread of the infection. Here we have utilized a cell-based fusion assay to identify the fusogenic glycoproteins of CMV. To deliver the glycoprotein genes to various cell lines, we constructed recombinant retroviruses encoding gB, gH, gL, and gO. Cells expressing individual CMV glyc

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