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Journal articles on the topic 'Viral fusion glycoproteins'

Author: Grafiati
Published: 14 December 2024

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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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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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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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11

Vallbracht, Melina, Barbara G. Klupp, and Thomas C. Mettenleiter. "Die komplexe Fusionsmaschinerie der Herpesviren." BIOspektrum 28, no. 2 (2022): 168–70. http://dx.doi.org/10.1007/s12268-022-1718-5.

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AbstractEnveloped viruses enter cells by fusion between viral and cellular membranes which is catalyzed by specialized fusogenic glycoproteins (g) on the viral surface. Many viruses use a single fusion protein for entry. In contrast, herpesviruses depend on a complex fusion machinery. Here, we discuss the role of the individual herpesvirus fusion machinery components and answer two basic questions: why does the herpesvirus fusion protein gB depend on other glycoproteins for fusion, and can gB be transformed to function autonomously?
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Lavillette, Dimitri, Alessia Ruggieri, Bertrand Boson, Marielle Maurice, and François-Loïc Cosset. "Relationship between SU Subdomains That Regulate the Receptor-Mediated Transition from the Native (Fusion-Inhibited) to the Fusion-Active Conformation of the Murine Leukemia Virus Glycoprotein." Journal of Virology 76, no. 19 (2002): 9673–85. http://dx.doi.org/10.1128/jvi.76.19.9673-9685.2002.

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ABSTRACT Envelope glycoproteins (Env) of retroviruses are trimers of SU (surface) and TM (transmembrane) heterodimers and are expressed on virions in fusion-competent forms that are likely to be metastable. Activation of the viral receptor-binding domain (RBD) via its interaction with a cell surface receptor is thought to initiate a cascade of events that lead to refolding of the Env glycoprotein into its stable fusion-active conformation. While the fusion-active conformation of the TM subunit has been described in detail for several retroviruses, little is known about the fusion-competent str
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13

Bude, Sara Amanuel, Zengjun Lu, Zhixun Zhao, and Qiang Zhang. "Pseudorabies Virus Glycoproteins E and B Application in Vaccine and Diagnosis Kit Development." Vaccines 12, no. 9 (2024): 1078. http://dx.doi.org/10.3390/vaccines12091078.

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Background: Pseudorabies virus (PRV) is a highly infectious pathogen that affects a wide range of mammals and imposes a significant economic burden on the global pig industry. The viral envelope of PRV contains several glycoproteins, including glycoprotein E (gE) and glycoprotein B (gB), which play critical roles in immune recognition, vaccine development, and diagnostic procedures. Mutations in these glycoproteins may enhance virulence, highlighting the need for updated vaccines. Method: This review examines the functions of PRV gE and gB in vaccine development and diagnostics, focusing on th
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14

Garry, Courtney E., та Robert F. Garry. "Proteomics Computational Analyses Suggest that the Antennavirus Glycoprotein Complex Includes a Class I Viral Fusion Protein (α-Penetrene) with an Internal Zinc-Binding Domain and a Stable Signal Peptide". Viruses 11, № 8 (2019): 750. http://dx.doi.org/10.3390/v11080750.

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A metatranscriptomic study of RNA viruses in cold-blooded vertebrates identified two related viruses from frogfish (Antennarius striatus) that represent a new genus Antennavirus in the family Arenaviridae (Order: Bunyavirales). Computational analyses were used to identify features common to class I viral fusion proteins (VFPs) in antennavirus glycoproteins, including an N-terminal fusion peptide, two extended alpha-helices, an intrahelical loop, and a carboxyl terminal transmembrane domain. Like mammarenavirus and hartmanivirus glycoproteins, the antennavirus glycoproteins have an intracellula
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15

Earnest, James T., Michael P. Hantak, Jung-Eun Park, and Tom Gallagher. "Coronavirus and Influenza Virus Proteolytic Priming Takes Place in Tetraspanin-Enriched Membrane Microdomains." Journal of Virology 89, no. 11 (2015): 6093–104. http://dx.doi.org/10.1128/jvi.00543-15.

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ABSTRACTCoronaviruses (CoVs) and low-pathogenicity influenza A viruses (LP IAVs) depend on target cell proteases to cleave their viral glycoproteins and prime them for virus-cell membrane fusion. Several proteases cluster into tetraspanin-enriched microdomains (TEMs), suggesting that TEMs are preferred virus entry portals. Here we found that several CoV receptors and virus-priming proteases were indeed present in TEMs. Isolated TEMs, when mixed with CoV and LP IAV pseudoparticles, cleaved viral fusion proteins to fusion-primed fragments and potentiated viral transductions. That entering viruse
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16

Fan, Qing, Richard Longnecker, and Sarah A. Connolly. "A Functional Interaction between Herpes Simplex Virus 1 Glycoprotein gH/gL Domains I and II and gD Is Defined by Using Alphaherpesvirus gH and gL Chimeras." Journal of Virology 89, no. 14 (2015): 7159–69. http://dx.doi.org/10.1128/jvi.00740-15.

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ABSTRACTWhereas most viruses require only a single protein to bind to and fuse with cells, herpesviruses use multiple glycoproteins to mediate virus entry, and thus communication among these proteins is required. For most alphaherpesviruses, the minimal set of viral proteins required for fusion with the host cell includes glycoproteins gD, gB, and a gH/gL heterodimer. In the current model of entry, gD binds to a cellular receptor and transmits a signal to gH/gL. This signal then triggers gB, the conserved fusion protein, to insert into the target membrane and refold to merge the viral and cell
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17

Federspiel, Mark J. "Reverse Engineering Provides Insights on the Evolution of Subgroups A to E Avian Sarcoma and Leukosis Virus Receptor Specificity." Viruses 11, no. 6 (2019): 497. http://dx.doi.org/10.3390/v11060497.

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The initial step of retrovirus entry—the interaction between the virus envelope glycoprotein trimer and a cellular receptor—is complex, involving multiple, noncontiguous determinants in both proteins that specify receptor choice, binding affinity and the ability to trigger conformational changes in the viral glycoproteins. Despite the complexity of this interaction, retroviruses have the ability to evolve the structure of their envelope glycoproteins to use a different cellular protein as receptors. The highly homologous subgroup A to E Avian Sarcoma and Leukosis Virus (ASLV) glycoproteins bel
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Snyder, Aleksandra, Todd W. Wisner, and David C. Johnson. "Herpes Simplex Virus Capsids Are Transported in Neuronal Axons without an Envelope Containing the Viral Glycoproteins." Journal of Virology 80, no. 22 (2006): 11165–77. http://dx.doi.org/10.1128/jvi.01107-06.

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ABSTRACT Electron micrographic studies of neuronal axons have produced contradictory conclusions on how alphaherpesviruses are transported from neuron cell bodies to axon termini. Some reports have described unenveloped capsids transported on axonal microtubules with separate transport of viral glycoproteins within membrane vesicles. Others have observed enveloped virions in proximal and distal axons. We characterized transport of herpes simplex virus (HSV) in human and rat neurons by staining permeabilized neurons with capsid- and glycoprotein-specific antibodies. Deconvolution microscopy was
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Bowden, Thomas A., Max Crispin, Stephen C. Graham, et al. "Unusual Molecular Architecture of the Machupo Virus Attachment Glycoprotein." Journal of Virology 83, no. 16 (2009): 8259–65. http://dx.doi.org/10.1128/jvi.00761-09.

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ABSTRACT New World arenaviruses, which cause severe hemorrhagic fever, rely upon their envelope glycoproteins for attachment and fusion into their host cell. Here we present the crystal structure of the Machupo virus GP1 attachment glycoprotein, which is responsible for high-affinity binding at the cell surface to the transferrin receptor. This first structure of an arenavirus glycoprotein shows that GP1 consists of a novel α/β fold. This provides a blueprint of the New World arenavirus attachment glycoproteins and reveals a new architecture of viral attachment, using a protein fold of unknown
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Tischler, Nicole D., Angel Gonzalez, Tomas Perez-Acle, Mario Rosemblatt, and Pablo D. T. Valenzuela. "Hantavirus Gc glycoprotein: evidence for a class II fusion protein." Journal of General Virology 86, no. 11 (2005): 2937–47. http://dx.doi.org/10.1099/vir.0.81083-0.

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Hantavirus cell entry is promoted by its envelope glycoproteins, Gn and Gc, through cell attachment and by fusion between viral and endosomal membranes at low pH. However, the role of Gn and Gc in receptor binding and cell fusion has not yet been defined. In this work, a sequence presenting characteristics similar to those of class II fusion peptides (FPs) of alphavirus E1 and flavivirus E proteins is identified within the hantavirus Gc glycoprotein. A three-dimensional comparative molecular model based on crystallographic data of tick-borne encephalitis virus E protein is proposed for the And
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Snyder, Aleksandra, Birgitte Bruun, Helena M. Browne, and David C. Johnson. "A Herpes Simplex Virus gD-YFP Fusion Glycoprotein Is Transported Separately from Viral Capsids in Neuronal Axons." Journal of Virology 81, no. 15 (2007): 8337–40. http://dx.doi.org/10.1128/jvi.00520-07.

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ABSTRACT Two models describing how alphaherpesviruses exit neurons differ with respect to whether nucleocapsids and envelope glycoproteins travel toward axon termini separately or as assembled enveloped virions. Recently, a pseudorabies virus glycoprotein D (gD)-green fluorescent protein fusion was found to colocalize with viral capsids, supporting anterograde transport of enveloped virions. Previous antibody staining experiments demonstrated that herpes simplex virus (HSV) glycoproteins and capsids are separately transported in axons. Here, we generated an HSV expressing a gD-yellow fluoresce
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Drummer, Heidi E., Irene Boo, and Pantelis Poumbourios. "Mutagenesis of a conserved fusion peptide-like motif and membrane-proximal heptad-repeat region of hepatitis C virus glycoprotein E1." Journal of General Virology 88, no. 4 (2007): 1144–48. http://dx.doi.org/10.1099/vir.0.82567-0.

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The E1E2 glycoprotein heterodimer of Hepatitis C virus mediates viral entry. E2 attaches the virus to cellular receptors; however, the function of E1 is unknown. We tested the hypothesis that E1 is a truncated class II fusion protein. We mutated amino acids within a predicted fusion peptide (residues 276–286) and a truncated C-terminal stem-like motif, containing a membrane-proximal heptad-repeat sequence (residues 330–347). The fusion peptide mutation F285A abolished viral entry, while mutation of other hydrophobic residues had no effect. Alanine replacement of heptad-repeat residues blocked
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Santos, Joy Ramielle L., Weijie Sun, Tarana A. Mangukia, Eduardo Reyes-Serratos, and Marcelo Marcet-Palacios. "Challenging the Existing Model of the Hexameric HIV-1 Gag Lattice and MA Shell Superstructure: Implications for Viral Entry." Viruses 13, no. 8 (2021): 1515. http://dx.doi.org/10.3390/v13081515.

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Despite type 1 human immunodeficiency virus (HIV-1) being discovered in the early 1980s, significant knowledge gaps remain in our understanding of the superstructure of the HIV-1 matrix (MA) shell. Current viral assembly models assume that the MA shell originates via recruitment of group-specific antigen (Gag) polyproteins into a hexagonal lattice but fails to resolve and explain lattice overlapping that occurs when the membrane is folded into a spherical/ellipsoidal shape. It further fails to address how the shell recruits, interacts with and encompasses the viral spike envelope (Env) glycopr
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Stone, Jacquelyn A., Bhadra M. Vemulapati, Birgit Bradel-Tretheway, and Hector C. Aguilar. "Multiple Strategies Reveal a Bidentate Interaction between the Nipah Virus Attachment and Fusion Glycoproteins." Journal of Virology 90, no. 23 (2016): 10762–73. http://dx.doi.org/10.1128/jvi.01469-16.

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ABSTRACTThe paramyxoviral family contains many medically important viruses, including measles virus, mumps virus, parainfluenza viruses, respiratory syncytial virus, human metapneumovirus, and the deadly zoonotic henipaviruses Hendra and Nipah virus (NiV). To both enter host cells and spread from cell to cell within infected hosts, the vast majority of paramyxoviruses utilize two viral envelope glycoproteins: the attachment glycoprotein (G, H, or hemagglutinin-neuraminidase [HN]) and the fusion glycoprotein (F). Binding of G/H/HN to a host cell receptor triggers structural changes in G/H/HN th
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Bradel-Tretheway, Birgit G., Qian Liu, Jacquelyn A. Stone, Samantha McInally, and Hector C. Aguilar. "Novel Functions of Hendra Virus G N-Glycans and Comparisons to Nipah Virus." Journal of Virology 89, no. 14 (2015): 7235–47. http://dx.doi.org/10.1128/jvi.00773-15.

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ABSTRACTHendra virus (HeV) and Nipah virus (NiV) are reportedly the most deadly pathogens within theParamyxoviridaefamily. These two viruses bind the cellular entry receptors ephrin B2 and/or ephrin B3 via the viral attachment glycoprotein G, and the concerted efforts of G and the viral fusion glycoprotein F result in membrane fusion. Membrane fusion is essential for viral entry into host cells and for cell-cell fusion, a hallmark of the disease pathobiology. HeV G is heavily N-glycosylated, but the functions of the N-glycans remain unknown. We disrupted eight predicted N-glycosylation sites i
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Dollery, Stephen J. "Towards Understanding KSHV Fusion and Entry." Viruses 11, no. 11 (2019): 1073. http://dx.doi.org/10.3390/v11111073.

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How viruses enter cells is of critical importance to pathogenesis in the host and for treatment strategies. Over the last several years, the herpesvirus field has made numerous and thoroughly fascinating discoveries about the entry of alpha-, beta-, and gamma-herpesviruses, giving rise to knowledge of entry at the amino acid level and the realization that, in some cases, researchers had overlooked whole sets of molecules essential for entry into critical cell types. Herpesviruses come equipped with multiple envelope glycoproteins which have several roles in many aspects of infection. For herpe
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Hasegawa, Kosei, Chunling Hu, Takafumi Nakamura, James D. Marks, Stephen J. Russell, and Kah-Whye Peng. "Affinity Thresholds for Membrane Fusion Triggering by Viral Glycoproteins." Journal of Virology 81, no. 23 (2007): 13149–57. http://dx.doi.org/10.1128/jvi.01415-07.

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ABSTRACT Enveloped viruses trigger membrane fusion to gain entry into cells. The receptor affinities of their attachment proteins vary greatly, from 10−4 M to 10−9 M, but the significance of this is unknown. Using six retargeted measles viruses that bind to Her-2/neu with a 5-log range in affinity, we show that receptor affinity has little impact on viral attachment but is nevertheless a key determinant of infectivity and intercellular fusion. For a given cell surface receptor density, there is an affinity threshold above which cell-cell fusion proceeds efficiently. Suprathreshold affinities d
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Batonick, Melissa, Antonius G. P. Oomens, and Gail W. Wertz. "Human Respiratory Syncytial Virus Glycoproteins Are Not Required for Apical Targeting and Release from Polarized Epithelial Cells." Journal of Virology 82, no. 17 (2008): 8664–72. http://dx.doi.org/10.1128/jvi.00827-08.

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ABSTRACT Human respiratory syncytial virus (HRSV) is released from the apical membrane of polarized epithelial cells. However, little is known about the processes of assembly and release of HRSV and which viral gene products are involved in the directional maturation of the virus. Based on previous studies showing that the fusion (F) glycoprotein contained an intrinsic apical sorting signal and that N- and O-linked glycans can act as apical targeting signals, we investigated whether the glycoproteins of HRSV were involved in its directional targeting and release. We generated recombinant virus
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Zhao, Xuesen, Fang Guo, Mary Ann Comunale, et al. "Inhibition of Endoplasmic Reticulum-Resident Glucosidases Impairs Severe Acute Respiratory Syndrome Coronavirus and Human Coronavirus NL63 Spike Protein-Mediated Entry by Altering the Glycan Processing of Angiotensin I-Converting Enzyme 2." Antimicrobial Agents and Chemotherapy 59, no. 1 (2014): 206–16. http://dx.doi.org/10.1128/aac.03999-14.

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ABSTRACTEndoplasmic reticulum (ER)-resident glucosidases I and II sequentially trim the three terminal glucose moieties on the N-linked glycans attached to nascent glycoproteins. These reactions are the first steps of N-linked glycan processing and are essential for proper folding and function of many glycoproteins. Because most of the viral envelope glycoproteins contain N-linked glycans, inhibition of ER glucosidases with derivatives of 1-deoxynojirimycin, i.e., iminosugars, efficiently disrupts the morphogenesis of a broad spectrum of enveloped viruses. However, like viral envelope proteins
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Piñón, Josefina D., Sharon M. Kelly, Nicholas C. Price, Jack U. Flanagan, and David W. Brighty. "An Antiviral Peptide Targets a Coiled-Coil Domain of the Human T-Cell Leukemia Virus Envelope Glycoprotein." Journal of Virology 77, no. 5 (2003): 3281–90. http://dx.doi.org/10.1128/jvi.77.5.3281-3290.2003.

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ABSTRACT Retrovirus entry into cells is mediated by the viral envelope glycoproteins which, through a cascade of conformational changes, orchestrate fusion of the viral and cellular membranes. In the absence of membrane fusion, viral entry into the host cell cannot occur. For human T-cell leukemia virus type 1 (HTLV-1), synthetic peptides that mimic a carboxy-terminal region of the transmembrane glycoprotein (TM) ectodomain are potent inhibitors of membrane fusion and virus entry. Here, we demonstrate that this class of inhibitor targets a fusion-active structure of HTLV-1 envelope. In particu
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Nieva, José L., and Tatiana Suárez. "Hydrophobic-at-Interface Regions in Viral Fusion Protein Ectodomains." Bioscience Reports 20, no. 6 (2000): 519–33. http://dx.doi.org/10.1023/a:1010458904487.

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In this chapter we shall describe how to apply the hydrophobicity-at-interface scale, as proposed by Wimley and White [Wimley, W. C. and White, S. H. (1996) Nature Struct. Biol. 3:842–848], to the detection of amino acid sequences of viral envelope glycoproteins putatively engaged in interactions with the target membranes. In addition, a new approach will be briefly introduced to infer the bilayer location at equilibrium of membrane-partitioning sequences. The use of these new procedures may be important in describing the molecular mechanism leading to the formation of a fusion pore by viral g
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Chandra, Sunandini, Raju Kalaivani, Manoj Kumar, Narayanaswamy Srinivasan, and Debi P. Sarkar. "Sendai virus recruits cellular villin to remodel actin cytoskeleton during fusion with hepatocytes." Molecular Biology of the Cell 28, no. 26 (2017): 3801–14. http://dx.doi.org/10.1091/mbc.e17-06-0400.

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Reconstituted Sendai viral envelopes (virosomes) are well recognized for their promising potential in membrane fusion–mediated delivery of bioactive molecules to liver cells. Despite the known function of viral envelope glycoproteins in catalyzing fusion with cellular membrane, the role of host cell proteins remains elusive. Here, we used two-dimensional differential in-gel electrophoresis to analyze hepatic cells in early response to virosome-induced membrane fusion. Quantitative mass spectrometry together with biochemical analysis revealed that villin, an actin-modifying protein, is differen
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Garry, Courtney, та Robert Garry. "Proteomics Computational Analyses Suggest that the Envelope Glycoproteins of Segmented Jingmen Flavi-Like Viruses Are Class II Viral Fusion Proteins (β-Penetrenes) with Mucin-Like Domains". Viruses 12, № 3 (2020): 260. http://dx.doi.org/10.3390/v12030260.

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Jingmen viruses are newly described segmented flavi-like viruses that have a worldwide distribution in ticks and have been associated with febrile illnesses in humans. Computational analyses were used to predict that Jingmen flavi-like virus glycoproteins have structural features of class II viral fusion proteins, including an ectodomain consisting of beta-sheets and short alpha-helices, a fusion peptide with interfacial hydrophobicity and a three-domain architecture. Jingmen flavi-like virus glycoproteins have a sequence enriched in serine, threonine, and proline at the amino terminus, which
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34

Chen, Bing, Yifan Cheng, Lesley Calder, et al. "A Chimeric Protein of Simian Immunodeficiency Virus Envelope Glycoprotein gp140 and Escherichia coli Aspartate Transcarbamoylase." Journal of Virology 78, no. 9 (2004): 4508–16. http://dx.doi.org/10.1128/jvi.78.9.4508-4516.2004.

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ABSTRACT The envelope glycoproteins of the human immunodeficiency virus and the related simian immunodeficiency virus (SIV) mediate viral entry into host cells by fusing viral and target cell membranes. We have reported expression, purification, and characterization of gp140 (also called gp160e), the soluble, trimeric ectodomain of the SIV envelope glycoprotein, gp160 (B. Chen et al., J. Biol. Chem. 275:34946-34953, 2000). We have now expressed and purified chimeric proteins of SIV gp140 and its variants with the catalytic subunit (C) of Escherichia coli aspartate transcarbamoylase (ATCase). T
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35

Balliet, John W., Kristin Gendron, and Paul Bates. "Mutational Analysis of the Subgroup A Avian Sarcoma and Leukosis Virus Putative Fusion Peptide Domain." Journal of Virology 74, no. 8 (2000): 3731–39. http://dx.doi.org/10.1128/jvi.74.8.3731-3739.2000.

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ABSTRACT Short hydrophobic regions referred to as fusion peptide domains (FPDs) at or near the amino terminus of the membrane-anchoring subunit of viral glycoproteins are believed to insert into the host membrane during the initial stage of enveloped viral entry. Avian sarcoma and leukosis viruses (ASLV) are unusual among retroviruses in that the region in the envelope glycoprotein (EnvA) proposed to be the FPD is internal and contains a centrally located proline residue. To begin analyzing the function of this region of EnvA, 20 substitution mutations were introduced into the putative FPD. Th
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36

Chi, Jung Hee I., Carol A. Harley, Aparna Mukhopadhyay, and Duncan W. Wilson. "The cytoplasmic tail of herpes simplex virus envelope glycoprotein D binds to the tegument protein VP22 and to capsids." Journal of General Virology 86, no. 2 (2005): 253–61. http://dx.doi.org/10.1099/vir.0.80444-0.

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Herpes simplex virus (HSV) capsids assemble, mature and package their viral genome in the nucleoplasm. They then exit the nucleus into the cytoplasm, where they acquire their final tegument and envelope. The molecular mechanism of cytoplasmic envelopment is unclear, but evidence suggests that the viral glycoprotein tails play an important role in the recruitment of tegument and capsids at the final envelopment site. However, due to redundancy in protein–protein interactions among the viral glycoproteins, genetic analysis of the role of individual glycoproteins in assembly has been difficult. T
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37

Klupp, Barbara G., Ralf Nixdorf, and Thomas C. Mettenleiter. "Pseudorabies Virus Glycoprotein M Inhibits Membrane Fusion." Journal of Virology 74, no. 15 (2000): 6760–68. http://dx.doi.org/10.1128/jvi.74.15.6760-6768.2000.

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ABSTRACT A transient transfection-fusion assay was established to investigate membrane fusion mediated by pseudorabies virus (PrV) glycoproteins. Plasmids expressing PrV glycoproteins under control of the immediate-early 1 promoter-enhancer of human cytomegalovirus were transfected into rabbit kidney cells, and the extent of cell fusion was quantitated 27 to 42 h after transfection. Cotransfection of plasmids encoding PrV glycoproteins B (gB), gD, gH, and gL resulted in formation of polykaryocytes, as has been shown for homologous proteins of herpes simplex virus type 1 (HSV-1) (A. Turner, B.
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38

De Clercq, Erik. "Antiviral Metal Complexes." Metal-Based Drugs 4, no. 3 (1997): 173–92. http://dx.doi.org/10.1155/mbd.1997.173.

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The initial events (virus adsorption and fusion with the cells) in the replicative cycle of human immunodeficiency virus (HIV) can serve as targets for the antiviral action of metal-binding compounds such as polyanionic compounds (polysulfates, polysulfonates, polycarboxylates, polyoxometalates, and sulfonated or carboxylated metalloporphyrins), bicyclams and G-octet-forming oligonucleotides. The adsorption and fusion of HIV with its target cells depends on the interaction of the viral envelope glycoproteins (gp 120) with the receptors (CD4, CXCR4) at the outer cell membrane. We are currently
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39

Plemper, Richard K., Anthea L. Hammond, Denis Gerlier, Adele K. Fielding, and Roberto Cattaneo. "Strength of Envelope Protein Interaction Modulates Cytopathicity of Measles Virus." Journal of Virology 76, no. 10 (2002): 5051–61. http://dx.doi.org/10.1128/jvi.76.10.5051-5061.2002.

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ABSTRACT To understand the molecular determinants of measles virus (MV) cytopathicity, we have characterized mutant viruses exhibiting a more-extensive cell-to-cell fusion while maintaining efficient replication to high titers. A virus which is modified by the addition of an 8-amino-acid Flag epitope tag at the cytoplasmic tail of its H (for MV hemagglutinin) envelope glycoprotein replicates efficiently, has an increased cytopathicity, possesses a greater infectivity per particle, and has an altered protein composition compared with that of unmodified MV. The mutant phenotype is not specifical
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40

Pertel, Peter E. "Human Herpesvirus 8 Glycoprotein B (gB), gH, and gL Can Mediate Cell Fusion." Journal of Virology 76, no. 9 (2002): 4390–400. http://dx.doi.org/10.1128/jvi.76.9.4390-4400.2002.

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ABSTRACT Herpesvirus entry into cells and herpesvirus-induced cell fusion are related processes in that virus penetration proceeds by fusion of the viral envelope and cell membrane. To characterize the human herpesvirus 8 (HHV-8) glycoproteins that can mediate cell fusion, a luciferase reporter gene activation assay was used. Chinese hamster ovary (CHO) cells expressing the HHV-8 glycoproteins of interest along with a luciferase reporter gene under the control of the T7 promoter were cocultivated with human cells transfected with T7 RNA polymerase. Because HHV-8 glycoprotein B (gB) expressed i
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41

Webb, Stacy R., Stacy E. Smith, Michael G. Fried, and Rebecca Ellis Dutch. "Transmembrane Domains of Highly Pathogenic Viral Fusion Proteins Exhibit Trimeric Association In Vitro." mSphere 3, no. 2 (2018): e00047-18. http://dx.doi.org/10.1128/msphere.00047-18.

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ABSTRACT Enveloped viruses require viral fusion proteins to promote fusion of the viral envelope with a target cell membrane. To drive fusion, these proteins undergo large conformational changes that must occur at the right place and at the right time. Understanding the elements which control the stability of the prefusion state and the initiation of conformational changes is key to understanding the function of these important proteins. The construction of mutations in the fusion protein transmembrane domains (TMDs) or the replacement of these domains with lipid anchors has implicated the TMD
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42

Lavillette, Dimitri, Eve-Isabelle Pécheur, Peggy Donot, et al. "Characterization of Fusion Determinants Points to the Involvement of Three Discrete Regions of Both E1 and E2 Glycoproteins in the Membrane Fusion Process of Hepatitis C Virus." Journal of Virology 81, no. 16 (2007): 8752–65. http://dx.doi.org/10.1128/jvi.02642-06.

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ABSTRACT Infection of eukaryotic cells by enveloped viruses requires the merging of viral and cellular membranes. Highly specific viral surface glycoproteins, named fusion proteins, catalyze this reaction by overcoming inherent energy barriers. Hepatitis C virus (HCV) is an enveloped virus that belongs to the genus Hepacivirus of the family Flaviviridae. Little is known about the molecular events that mediate cell entry and membrane fusion for HCV, although significant progress has been made due to recent developments in infection assays. Here, using infectious HCV pseudoparticles (HCVpp), we
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43

Madani, Navid, Amy M. Hubicki, Ana Luisa Perdigoto, Martin Springer, and Joseph Sodroski. "Inhibition of Human Immunodeficiency Virus Envelope Glycoprotein- Mediated Single Cell Lysis by Low-Molecular-Weight Antagonists of Viral Entry." Journal of Virology 81, no. 2 (2006): 532–38. http://dx.doi.org/10.1128/jvi.01079-06.

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ABSTRACT The coexpression of human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins and receptors leads to the lysis of single cells by a process that is dependent upon membrane fusion. This cell lysis was inhibited by low-molecular-weight compounds that interfere with receptor binding or with receptor-induced conformational transitions in the envelope glycoproteins. A peptide, T20, potently inhibited cell-cell fusion but had no effect on single cell lysis mediated by the HIV-1 envelope glycoproteins. Thus, critical events in the lysis of single cells by the HIV-1 envelope glycopro
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44

Kelly, James T., Stacey Human, Joseph Alderman, et al. "BST2/Tetherin Overexpression Modulates Morbillivirus Glycoprotein Production to Inhibit Cell–Cell Fusion." Viruses 11, no. 8 (2019): 692. http://dx.doi.org/10.3390/v11080692.

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The measles virus (MeV), a member of the genus Morbillivirus, is an established pathogen of humans. A key feature of morbilliviruses is their ability to spread by virus–cell and cell–cell fusion. The latter process, which leads to syncytia formation in vitro and in vivo, is driven by the viral fusion (F) and haemagglutinin (H) glycoproteins. In this study, we demonstrate that MeV glycoproteins are sensitive to inhibition by bone marrow stromal antigen 2 (BST2/Tetherin/CD317) proteins. BST2 overexpression causes a large reduction in MeV syncytia expansion. Using quantitative cell–cell fusion as
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45

Zhou, Xuan, Giorgia Cimato, Yihua Zhou, Giada Frascaroli, and Wolfram Brune. "A Virus Genetic System to Analyze the Fusogenicity of Human Cytomegalovirus Glycoprotein B Variants." Viruses 15, no. 4 (2023): 979. http://dx.doi.org/10.3390/v15040979.

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Viruses can induce the fusion of infected and neighboring cells, leading to the formation of syncytia. Cell–cell fusion is mediated by viral fusion proteins on the plasma membrane of infected cells that interact with cellular receptors on neighboring cells. Viruses use this mechanism to spread rapidly to adjacent cells or escape host immunity. For some viruses, syncytium formation is a hallmark of infection and a known pathogenicity factor. For others, the role of syncytium formation in viral dissemination and pathogenicity remains poorly understood. Human cytomegalovirus (HCMV) is an importan
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46

Jeetendra, E., Clinton S. Robison, Lorraine M. Albritton, and Michael A. Whitt. "The Membrane-Proximal Domain of Vesicular Stomatitis Virus G Protein Functions as a Membrane Fusion Potentiator and Can Induce Hemifusion." Journal of Virology 76, no. 23 (2002): 12300–12311. http://dx.doi.org/10.1128/jvi.76.23.12300-12311.2002.

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ABSTRACT Recently we showed that the membrane-proximal stem region of the vesicular stomatitis virus (VSV) G protein ectodomain (G stem [GS]), together with the transmembrane and cytoplasmic domains, was sufficient to mediate efficient VSV budding (C. S. Robison and M. A. Whitt, J. Virol. 74:2239-2246, 2000). Here, we show that GS can also potentiate the membrane fusion activity of heterologous viral fusion proteins when GS is coexpressed with those proteins. For some fusion proteins, there was as much as a 40-fold increase in syncytium formation when GS was coexpressed compared to that seen w
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47

Zelus, Bruce D., Jeanne H. Schickli, Dianna M. Blau, Susan R. Weiss, and Kathryn V. Holmes. "Conformational Changes in the Spike Glycoprotein of Murine Coronavirus Are Induced at 37°C either by Soluble Murine CEACAM1 Receptors or by pH 8." Journal of Virology 77, no. 2 (2003): 830–40. http://dx.doi.org/10.1128/jvi.77.2.830-840.2003.

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ABSTRACT The spike glycoprotein (S) of the murine coronavirus mouse hepatitis virus (MHV) binds to viral murine CEACAM receptor glycoproteins and causes membrane fusion. On virions, the 180-kDa S glycoprotein of the MHV-A59 strain can be cleaved by trypsin to form the 90-kDa N-terminal receptor-binding subunit (S1) and the 90-kDa membrane-anchored fusion subunit (S2). Incubation of virions with purified, soluble CEACAM1a receptor proteins at 37°C and pH 6.5 neutralizes virus infectivity (B. D. Zelus, D. R. Wessner, R. K. Williams, M. N. Pensiero, F. T. Phibbs, M. deSouza, G. S. Dveksler, and K
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48

Klupp, Barbara, Jan Altenschmidt, Harald Granzow, Walter Fuchs, and Thomas C. Mettenleiter. "Glycoproteins Required for Entry Are Not Necessary for Egress of Pseudorabies Virus." Journal of Virology 82, no. 13 (2008): 6299–309. http://dx.doi.org/10.1128/jvi.00386-08.

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ABSTRACT In the current perception of the herpesvirus replication cycle, two fusion processes are thought to occur during entry and nuclear egress. For penetration, glycoproteins gB and gH/gL have been shown to be essential, whereas a possible role of these glycoproteins in nuclear egress remains unclear. Viral envelope glycoproteins have been detected by immunolabeling in the nuclear membrane as well as in primary enveloped particles in several herpesviruses, indicating that they might be involved in the fusion process. Moreover, a herpes simplex virus type 1 mutant simultaneously lacking gB
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49

Eisfeld, Hannah S., Alexander Simonis, Sandra Winter, et al. "Viral Glycoproteins Induce NLRP3 Inflammasome Activation and Pyroptosis in Macrophages." Viruses 13, no. 10 (2021): 2076. http://dx.doi.org/10.3390/v13102076.

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Infections with viral pathogens are widespread and can cause a variety of different diseases. In-depth knowledge about viral triggers initiating an immune response is necessary to decipher viral pathogenesis. Inflammasomes, as part of the innate immune system, can be activated by viral pathogens. However, viral structural components responsible for inflammasome activation remain largely unknown. Here we analyzed glycoproteins derived from SARS-CoV-1/2, HCMV and HCV, required for viral entry and fusion, as potential triggers of NLRP3 inflammasome activation and pyroptosis in THP-1 macrophages.
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50

Brighty, David W., and Sushma R. Jassal. "The Synthetic Peptide P-197 Inhibits Human T-Cell Leukemia Virus Type 1 Envelope-Mediated Syncytium Formation by a Mechanism That Is Independent of Hsc70." Journal of Virology 75, no. 21 (2001): 10472–78. http://dx.doi.org/10.1128/jvi.75.21.10472-10478.2001.

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ABSTRACT Entry of human T-cell leukemia virus type 1 (HTLV-1) into cells is mediated by the viral envelope glycoproteins gp46 and gp21. The gp46 surface glycoprotein binds to a poorly characterized cell surface receptor, thereby promoting the gp21-dependent fusion of the viral and cellular membranes. Interestingly, a synthetic peptide (P-197) simulating amino acids 197 to 216 of gp46 strongly inhibits envelope-dependent membrane fusion with Molt-4 target cells. It has been suggested that this peptide acts by competitively binding to Hsc70, a putative cellular receptor for HTLV-1. We now demons
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