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Artykuły w czasopismach na temat „Virus Cell Fusion”

Autor: Grafiati

Data publikacji: 7 września 2023

Data aktualizacji: 31 lipca 2025

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1

Zhang, Chuyuan, Xinjie Meng, and Hanjun Zhao. "Comparison of Cell Fusions Induced by Influenza Virus and SARS-CoV-2." International Journal of Molecular Sciences 23, no. 13 (2022): 7365. http://dx.doi.org/10.3390/ijms23137365.

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Virus–cell fusion is the key step for viral infection in host cells. Studies on virus binding and fusion with host cells are important for understanding the virus–host interaction and viral pathogenesis for the discovery of antiviral drugs. In this review, we focus on the virus–cell fusions induced by the two major pandemic viruses, including the influenza virus and SARS-CoV-2. We further compare the cell fusions induced by the influenza virus and SARS-CoV-2, especially the pH-dependent fusion of the influenza virus and the fusion of SARS-CoV-2 in the type-II transmembrane serine protease 2 ne

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Leroy, Héloïse, Mingyu Han, Marie Woottum, et al. "Virus-Mediated Cell-Cell Fusion." International Journal of Molecular Sciences 21, no. 24 (2020): 9644. http://dx.doi.org/10.3390/ijms21249644.

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Cell-cell fusion between eukaryotic cells is a general process involved in many physiological and pathological conditions, including infections by bacteria, parasites, and viruses. As obligate intracellular pathogens, viruses use intracellular machineries and pathways for efficient replication in their host target cells. Interestingly, certain viruses, and, more especially, enveloped viruses belonging to different viral families and including human pathogens, can mediate cell-cell fusion between infected cells and neighboring non-infected cells. Depending of the cellular environment and tissue

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3

Hernandez, L. D., L. R. Hoffman, T. G. Wolfsberg, and J. M. White. "VIRUS-CELL AND CELL-CELL FUSION." Annual Review of Cell and Developmental Biology 12, no. 1 (1996): 627–61. http://dx.doi.org/10.1146/annurev.cellbio.12.1.627.

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Podbilewicz, Benjamin. "Virus and Cell Fusion Mechanisms." Annual Review of Cell and Developmental Biology 30, no. 1 (2014): 111–39. http://dx.doi.org/10.1146/annurev-cellbio-101512-122422.

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5

Gianopulos, Katrina A., Albina O. Makio, Suzanne M. Pritchard, Cristina W. Cunha, McKenna A. Hull, and Anthony V. Nicola. "Herpes Simplex Virus 1 Glycoprotein B from a Hyperfusogenic Virus Mediates Enhanced Cell–Cell Fusion." Viruses 16, no. 2 (2024): 251. http://dx.doi.org/10.3390/v16020251.

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Herpes simplex virus 1 (HSV-1) causes significant morbidity and death in humans worldwide. Herpes simplex virus 1 has a complex fusion mechanism that is incompletely understood. The HSV-1 strain ANG has notable fusion and entry activities that distinguish it from wild type. HSV-1 ANG virions fused with the Vero cell surface at 4 °C and also entered cells more efficiently at 15 °C, relative to wild type HSV-1 strain KOS virions, consistent with a hyperfusogenic phenotype. Understanding the molecular basis for the unique entry and fusion activities of HSV-1 strain ANG will help decipher the HSV

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6

Melancon, Jeffrey M., Timothy P. Foster, and Konstantin G. Kousoulas. "Genetic Analysis of the Herpes Simplex Virus Type 1 UL20 Protein Domains Involved in Cytoplasmic Virion Envelopment and Virus-Induced Cell Fusion." Journal of Virology 78, no. 14 (2004): 7329–43. http://dx.doi.org/10.1128/jvi.78.14.7329-7343.2004.

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ABSTRACT The herpes simplex virus type 1 UL20 protein (UL20p) is an important determinant for cytoplasmic virion morphogenesis and virus-induced cell fusion. To delineate the functional domains of the UL20 protein, we generated a panel of single and multiple (cluster) alanine substitutions as well as UL20p carboxyl-terminal truncations. The UL20 mutant genes could be broadly categorized into four main groups: Group I UL20 mutant genes complemented for both virus production and virus-induced cell fusion; Group II UL20 mutant genes did not complement for either virus-induced cell fusion or infec

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7

Schmid, Erik, Andreas Zurbriggen, Uta Gassen, Bert Rima, Volker ter Meulen, and Jürgen Schneider-Schaulies. "Antibodies to CD9, a Tetraspan Transmembrane Protein, Inhibit Canine Distemper Virus-Induced Cell-Cell Fusion but Not Virus-Cell Fusion." Journal of Virology 74, no. 16 (2000): 7554–61. http://dx.doi.org/10.1128/jvi.74.16.7554-7561.2000.

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ABSTRACT Canine distemper virus (CDV) causes a life-threatening disease in several carnivores including domestic dogs. Recently, we identified a molecule, CD9, a member of the tetraspan transmembrane protein family, which facilitates, and antibodies to which inhibit, the infection of tissue culture cells with CDV (strain Onderstepoort). Here we describe that an anti-CD9 monoclonal antibody (MAb K41) did not interfere with binding of CDV to cells and uptake of virus. In addition, in single-step growth experiments, MAb K41 did not induce differences in the levels of viral mRNA and proteins. Howe

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8

Markosyan, Ruben M., Shan Lu Liu, and Fredric S. Cohen. "Cell-Cell Fusion Mediated by the Fusion Protein of Ebola Virus." Biophysical Journal 106, no. 2 (2014): 707a. http://dx.doi.org/10.1016/j.bpj.2013.11.3921.

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Tsurudome, Masato, Machiko Nishio, Morihiro Ito, et al. "Effects of Hemagglutinin-Neuraminidase Protein Mutations on Cell-Cell Fusion Mediated by Human Parainfluenza Type 2 Virus." Journal of Virology 82, no. 17 (2008): 8283–95. http://dx.doi.org/10.1128/jvi.00460-08.

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ABSTRACT The monoclonal antibody M1-1A, specific for the hemagglutinin-neuraminidase (HN) protein of human parainfluenza type 2 virus (HPIV2), blocks virus-induced cell-cell fusion without affecting the hemagglutinating and neuraminidase activities. F13 is a neutralization escape variant selected with M1-1A and contains amino acid mutations N83Y and M186I in the HN protein, with no mutation in the fusion protein. Intriguingly, F13 exhibits reduced ability to induce cell-cell fusion despite its multistep replication. To investigate the potential role of HPIV2 HN protein in the regulation of cel

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10

Connolly, Sarah A., and Robert A. Lamb. "Paramyxovirus fusion: Real-time measurement of parainfluenza virus 5 virus–cell fusion." Virology 355, no. 2 (2006): 203–12. http://dx.doi.org/10.1016/j.virol.2006.07.021.

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11

Zhou, Momei, Vivek Kamarshi, Ann M. Arvin, and Stefan L. Oliver. "Calcineurin phosphatase activity regulates Varicella-Zoster Virus induced cell-cell fusion." PLOS Pathogens 16, no. 11 (2020): e1009022. http://dx.doi.org/10.1371/journal.ppat.1009022.

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Cell-cell fusion (abbreviated as cell fusion) is a characteristic pathology of medically important viruses, including varicella-zoster virus (VZV), the causative agent of chickenpox and shingles. Cell fusion is mediated by a complex of VZV glycoproteins, gB and gH-gL, and must be tightly regulated to enable skin pathogenesis based on studies with gB and gH hyperfusogenic VZV mutants. Although the function of gB and gH-gL in the regulation of cell fusion has been explored, whether host factors are directly involved in this regulation process is unknown. Here, we discovered host factors that mod

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12

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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13

Huerta, Leonor, Nayali López-Balderas, Evelyn Rivera-Toledo, et al. "HIV-Envelope–Dependent Cell-Cell Fusion: Quantitative Studies." Scientific World JOURNAL 9 (2009): 746–63. http://dx.doi.org/10.1100/tsw.2009.90.

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Interactionin vitrobetween cells infected with human immunodeficiency virus (HIV) and surrounding, uninfected, target cells often leads to cell fusion and the formation of multinucleated cells, called syncytia. The presence in HIV-infected individuals of virus strains able to induce syncytia in cultures of T cells is associated with disease progression and AIDS. Even in the asymptomatic stage of infection, multinucleated cells have been observed in different organs, indicating that fused cells may be generated and remain viable in the tissues of patients. We used lymphocytic cells transfected

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14

Valansi, Clari, David Moi, Evgenia Leikina, et al. "Arabidopsis HAP2/GCS1 is a gamete fusion protein homologous to somatic and viral fusogens." Journal of Cell Biology 216, no. 3 (2017): 571–81. http://dx.doi.org/10.1083/jcb.201610093.

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Cell–cell fusion is inherent to sexual reproduction. Loss of HAPLESS 2/GENERATIVE CELL SPECIFIC 1 (HAP2/GCS1) proteins results in gamete fusion failure in diverse organisms, but their exact role is unclear. In this study, we show that Arabidopsis thaliana HAP2/GCS1 is sufficient to promote mammalian cell–cell fusion. Hemifusion and complete fusion depend on HAP2/GCS1 presence in both fusing cells. Furthermore, expression of HAP2 on the surface of pseudotyped vesicular stomatitis virus results in homotypic virus–cell fusion. We demonstrate that the Caenorhabditis elegans Epithelial Fusion Failu

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15

Zavorotinskaya, Tatiana, Zhaohui Qian, John Franks, and Lorraine M. Albritton. "A Point Mutation in the Binding Subunit of a Retroviral Envelope Protein Arrests Virus Entry at Hemifusion." Journal of Virology 78, no. 1 (2004): 473–81. http://dx.doi.org/10.1128/jvi.78.1.473-481.2004.

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ABSTRACT The transmembrane subunits of viral envelope proteins are thought to perform all of the functions required for membrane fusion during entry of enveloped viruses. However, changes in a conserved SPHQ motif near the N terminus of the receptor binding subunit of a murine leukemia virus (MLV) envelope protein block infection and induction of cell-cell fusion but not receptor binding. Here we report evidence that a histidine-to-arginine change at position 8 (H8R) in the SPHQ motif of Moloney MLV blocks infection by arresting virus-cell fusion at the hemifusion state. In cell-cell fusion as

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16

Kielian, M., M. R. Klimjack, S. Ghosh, and W. A. Duffus. "Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus." Journal of Cell Biology 134, no. 4 (1996): 863–72. http://dx.doi.org/10.1083/jcb.134.4.863.

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Semliki Forest virus (SFV) infects cells by an acid-dependent membrane fusion reaction catalyzed by the virus spike protein, a complex containing E1 and E2 transmembrane subunits. E1 carries the putative virus fusion peptide, and mutations in this domain of the spike protein were previously shown to shift the pH threshold of cell-cell fusion (G91A), or block cell-cell fusion (G91D). We have used an SFV infectious clone to characterize virus particles containing these mutations. In keeping with the previous spike protein results, G91A virus showed limited secondary infection and an acid-shifted

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17

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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18

Kempf, Christoph, Marcel R. Michel, Adames Omar, Pia Jentsch, and Andreas Morell. "Semliki Forest virus induced cell-cell fusion at neutral extracellular pH." Bioscience Reports 10, no. 4 (1990): 363–74. http://dx.doi.org/10.1007/bf01117236.

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Semliki Forest virus-induced cell-cell fusion from within was considered to exclusively occur at mildly acidic pH (<6.2). Data of this study show that such cell fusion can also be triggered by transient acidification of the cytoplasm of infected cells at an extracellular, neutral pH. Results were obtained by utilizing NH4Cl pulses combined with covalent modification of cell surface proteins. The observation implies a revision of the current consensus regarding the mechanism of Semliki Forest virus induced cell-cell fusion. We propose a model in which at least two peptide segments of the vir

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19

Muggeridge, Martin I. "Characterization of cell–cell fusion mediated by herpes simplex virus 2 glycoproteins gB, gD, gH and gL in transfected cells." Journal of General Virology 81, no. 8 (2000): 2017–27. http://dx.doi.org/10.1099/0022-1317-81-8-2017.

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The mechanisms by which herpes simplex viruses (HSV) mediate fusion between their envelope and the plasma membrane during entry into cells, and between the plasma membranes of adjacent infected and uninfected cells to form multinucleated giant cells, are poorly understood. Four viral glycoproteins (gB, gD, gH and gL) are required for virus–cell fusion, whereas these plus several others are required for cell–cell fusion (syncytium formation). A better understanding would be aided by the availability of a model system, whereby fusion could be induced with a minimal set of proteins, in the absenc

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20

Shmulevitz, Maya, Jennifer Corcoran, Jayme Salsman, and Roy Duncan. "Cell-Cell Fusion Induced by the Avian Reovirus Membrane Fusion Protein Is Regulated by Protein Degradation." Journal of Virology 78, no. 11 (2004): 5996–6004. http://dx.doi.org/10.1128/jvi.78.11.5996-6004.2004.

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ABSTRACT The p10 fusion-associated small transmembrane protein of avian reovirus induces extensive syncytium formation in transfected cells. Here we show that p10-induced cell-cell fusion is restricted by rapid degradation of the majority of newly synthesized p10. The small ectodomain of p10 targets the protein for degradation following p10 insertion into an early membrane compartment. Paradoxically, conservative amino acid substitutions in the p10 ectodomain hydrophobic patch that eliminate fusion activity also increase p10 stability. The small amount of p10 that escapes intracellular degrada

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Jeetendra, E., Kakoli Ghosh, Derek Odell, Jin Li, Hara P. Ghosh, and Michael A. Whitt. "The Membrane-Proximal Region of Vesicular Stomatitis Virus Glycoprotein G Ectodomain Is Critical for Fusion and Virus Infectivity." Journal of Virology 77, no. 23 (2003): 12807–18. http://dx.doi.org/10.1128/jvi.77.23.12807-12818.2003.

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ABSTRACT The glycoprotein (G) of vesicular stomatitis virus (VSV) is responsible for binding of virus to cells and for mediating virus entry following endocytosis by inducing fusion of the viral envelope with the endosomal membrane. The fusion peptide of G is internal (residues 116 to 137) and exhibits characteristics similar to those of other internal fusion peptides, but recent studies have implicated the region adjacent to the transmembrane domain as also being important for G-mediated membrane fusion. Sequence alignment of the membrane-proximal region of G from several different vesiculovi

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Chouljenko, Vladimir N., Arun V. Iyer, Sona Chowdhury, Dmitry V. Chouljenko, and Konstantin G. Kousoulas. "The Amino Terminus of Herpes Simplex Virus Type 1 Glycoprotein K (gK) Modulates gB-Mediated Virus-Induced Cell Fusion and Virion Egress." Journal of Virology 83, no. 23 (2009): 12301–13. http://dx.doi.org/10.1128/jvi.01329-09.

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ABSTRACT Herpes simplex virus type 1 (HSV-1)-induced cell fusion is mediated by viral glycoproteins and other membrane proteins expressed on infected cell surfaces. Certain mutations in the carboxyl terminus of HSV-1 glycoprotein B (gB) and in the amino terminus of gK cause extensive virus-induced cell fusion. Although gB is known to be a fusogenic glycoprotein, the mechanism by which gK is involved in virus-induced cell fusion remains elusive. To delineate the amino-terminal domains of gK involved in virus-induced cell fusion, the recombinant viruses gKΔ31-47, gKΔ31-68, and gKΔ31-117, express

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Greengard, Olga, Natalia Poltoratskaia, Evgenia Leikina, Joshua Zimmerberg, and Anne Moscona. "The Anti-Influenza Virus Agent 4-GU-DANA (Zanamivir) Inhibits Cell Fusion Mediated by Human Parainfluenza Virus and Influenza Virus HA." Journal of Virology 74, no. 23 (2000): 11108–14. http://dx.doi.org/10.1128/jvi.74.23.11108-11114.2000.

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ABSTRACT 4-GU-DANA (zanamivir) (as well as DANA and 4-AM-DANA) was found to inhibit the neuraminidase activity of human parainfluenza virus type 3 (HPF3). The viral neuraminidase activity is attributable to hemagglutinin-neuraminidase (HN), an envelope protein essential for viral attachment and for fusion mediated by the other envelope protein, F. While there is no evidence that HN's neuraminidase activity is essential for receptor binding and syncytium formation, we found that 4-GU-DANA prevented hemadsorption and fusion of persistently infected cells with uninfected cells. In plaque assays,

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Sharma, Nishi R., Prashant Mani, Neha Nandwani, Rajakishore Mishra, Ajay Rana, and Debi P. Sarkar. "Reciprocal Regulation of AKT and MAP Kinase Dictates Virus-Host Cell Fusion." Journal of Virology 84, no. 9 (2010): 4366–82. http://dx.doi.org/10.1128/jvi.01940-09.

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ABSTRACT Viruses of the Paramyxoviridae family bind to their host cells by using hemagglutinin-neuraminidase (HN), which enhances fusion protein (F)-mediated membrane fusion. Although respiratory syncytial virus and parainfluenza virus 5 of this family are suggested to trigger host cell signaling during infection, the virus-induced intracellular signals dictating virus-cell fusion await elucidation. Using an F- or HN-F-containing reconstituted envelope of Sendai virus, another paramyxovirus, we revealed the role and regulation of AKT1 and Raf/MEK/ERK cascades during viral fusion with liver cel

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Kobayashi, Mariko, Michael C. Bennett, Theodore Bercot, and Ila R. Singh. "Functional Analysis of Hepatitis C Virus Envelope Proteins, Using a Cell-Cell Fusion Assay." Journal of Virology 80, no. 4 (2006): 1817–25. http://dx.doi.org/10.1128/jvi.80.4.1817-1825.2006.

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ABSTRACT Hepatitis C virus (HCV) envelope proteins mediate the entry of virus into cells by binding to cellular receptors, resulting in fusion of the viral membrane with the host cell membrane and permitting the viral genome to enter the cytoplasm. We report the development of a robust and reproducible cell-cell fusion assay using envelope proteins from commonly occurring genotypes of HCV. The assay scored HCV envelope protein-mediated fusion by the production of fluorescent green syncytia and allowed us to elucidate many aspects of HCV fusion, including the pH of fusion, cell types that permi

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Gaudin, Yves. "Rabies Virus-Induced Membrane Fusion Pathway." Journal of Cell Biology 150, no. 3 (2000): 601–12. http://dx.doi.org/10.1083/jcb.150.3.601.

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Fusion of rabies virus with membranes is triggered at low pH and is mediated by the viral glycoprotein (G). The rabies virus-induced fusion pathway was studied by investigating the effects of exogenous lipids having various dynamic molecular shapes on the fusion process. Inverted cone-shaped lysophosphatidylcholines (LPCs) blocked fusion at a stage subsequent to fusion peptide insertion into the target membrane. Consistent with the stalk-hypothesis, LPC with shorter alkyl chains inhibited fusion at lower membrane concentrations and this inhibition was compensated by the presence of oleic acid.

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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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Okazaki, Katsunori. "Proteolytic cleavage of glycoprotein B is dispensable for in vitro replication, but required for syncytium formation of pseudorabies virus." Journal of General Virology 88, no. 7 (2007): 1859–65. http://dx.doi.org/10.1099/vir.0.82610-0.

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Glycoprotein B (gB) is the most conserved glycoprotein among herpesviruses and it plays important roles in virus infectivity. In most herpesviruses, including pseudorabies virus (PRV), gB is cleaved by a cellular protease into two disulfide-linked subunits. In the present study, I found that the PRV gB generated in human colon carcinoma LoVo cells, which lack the ubiquitous protease furin, remained in the uncleaved form and the virus replicated in these cells without cell fusion. The uncleaved gB was converted into its subunits after furin digestion. The virus also replicated in Madin–Darby bo

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Cosset, François-Loic, Philippe Marianneau, Geraldine Verney, et al. "Characterization of Lassa Virus Cell Entry and Neutralization with Lassa Virus Pseudoparticles." Journal of Virology 83, no. 7 (2009): 3228–37. http://dx.doi.org/10.1128/jvi.01711-08.

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ABSTRACT The cell entry and humoral immune response of the human pathogen Lassa virus (LV), a biosafety level 4 (BSL4) Old World arenavirus, are not well characterized. LV pseudoparticles (LVpp) are a surrogate model system that has been used to decipher factors and routes involved in LV cell entry under BSL2 conditions. Here, we describe LVpp, which are highly infectious, with titers approaching those obtained with pseudoparticles displaying G protein of vesicular stomatitis virus and their the use for the characterization of LV cell entry and neutralization. Upon cell attachment, LVpp utiliz

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Pedersen, Simon Metz, Bodil Øster, Bettina Bundgaard, and Per Höllsberg. "Induction of Cell-Cell Fusion from Without by Human Herpesvirus 6B." Journal of Virology 80, no. 19 (2006): 9916–20. http://dx.doi.org/10.1128/jvi.02693-05.

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ABSTRACT Human herpesvirus (HHV) 6A induce fusion from without (FFWO), whereas HHV-6B is believed to be ineffective in this process. Here, we demonstrate that HHV-6B induces rapid fusion in both epithelial cells and lymphocytes. The fusion was identified 1 h postinfection, could be inhibited by antibodies to HHV-6B gH and to the cellular receptor CD46, and was dependent on virus titer but independent of de novo protein synthesis and UV inactivation of the virus. Comparisons indicate that HHV-6A is only 10-fold more effective in inducing FFWO than HHV-6B. These data demonstrate that HHV-6B can

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Bär, Séverine, Ayato Takada, Yoshihiro Kawaoka, and Marc Alizon. "Detection of Cell-Cell Fusion Mediated by Ebola Virus Glycoproteins." Journal of Virology 80, no. 6 (2006): 2815–22. http://dx.doi.org/10.1128/jvi.80.6.2815-2822.2006.

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ABSTRACT Ebola viruses (EboV) are enveloped RNA viruses infecting cells by a pH-dependent process mediated by viral glycoproteins (GP) involving endocytosis of virions and their routing into acidic endosomes. As with well-characterized pH-dependent viral entry proteins, in particular influenza virus hemagglutinin, it is thought that EboV GP require activation by low pH in order to mediate fusion of the viral envelope with the membrane of endosomes. However, it has not yet been possible to confirm the direct role of EboV GP in membrane fusion and the requirement for low-pH activation. It was in

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Weissenhorn, Winfried, Andreas Hinz, and Yves Gaudin. "Virus membrane fusion." FEBS Letters 581, no. 11 (2007): 2150–55. http://dx.doi.org/10.1016/j.febslet.2007.01.093.

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Ogino, Michiko, Kumiko Yoshimatsu, Hideki Ebihara, et al. "Cell Fusion Activities of Hantaan Virus Envelope Glycoproteins." Journal of Virology 78, no. 19 (2004): 10776–82. http://dx.doi.org/10.1128/jvi.78.19.10776-10782.2004.

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ABSTRACT Hantaan virus (HTNV)-infected Vero E6 cells undergo cell fusion with both infected and uninfected cells under low-pH conditions. Flow cytometry and fluorescence microscopy of HTNV-infected Vero E6 cells showed that envelope glycoproteins (GPs) were located both on the cell surface and in the cytoplasm. Neutralizing monoclonal antibodies (MAbs) against the G1 and G2 envelope GPs inhibited cell fusion, whereas nonneutralizing MAbs against G1 or G2 and MAbs against the nucleocapsid protein (NP) did not. Transfected Vero E6 cells that expressed GPs but not those that expressed NP fused an

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Ren, Guijie, Yunlong Zhuang, Keli Tian, et al. "Acidic amino acids increase fusion activity in the specific fusion domain of Newcastle disease virus fusion protein." Canadian Journal of Microbiology 59, no. 9 (2013): 641–44. http://dx.doi.org/10.1139/cjm-2013-0133.

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To explore the effects of amino acids Gln and Asn within the specific fusion domain of fusion (F) protein on the specific membrane fusion in Newcastle disease virus (NDV), the mutants Q204E–Q205E and N245D were constructed in the specific fusion domain of F protein. The mutant genes were co-expressed with homologous or heterologous hemagglutinin–neuraminidase (HN) in BHK21 cells. Cell fusion functions of mutants were analyzed with Giemsa staining and reporter gene methods. Cell surface expression efficiency was analyzed with immunofluorescence assay and fluorescence-activated cell sorter analy

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Atanasiu, Doina, Wan Ting Saw, Roselyn J. Eisenberg, and Gary H. Cohen. "Regulation of Herpes Simplex Virus Glycoprotein-Induced Cascade of Events Governing Cell-Cell Fusion." Journal of Virology 90, no. 23 (2016): 10535–44. http://dx.doi.org/10.1128/jvi.01501-16.

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ABSTRACTReceptor-dependent herpes simplex virus (HSV)-induced cell-cell fusion requires glycoproteins gD, gH/gL, and gB. Our current model posits that during fusion, receptor-activated conformational changes in gD activate gH/gL, which subsequently triggers the transformation of the prefusion form of gB into a fusogenic state. To examine the role of each glycoprotein in receptor-dependent cell-cell fusion, we took advantage of our discovery that fusion by wild-type herpes simplex virus 2 (HSV-2) glycoproteins occurs twice as fast as that achieved by HSV-1 glycoproteins. By sequentially swappin

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Lu, Chi-Wei, and Monica J. Roth. "Role of the Mutation Q252R in Activating Membrane Fusion in the Murine Leukemia Virus Surface Envelope Protein." Journal of Virology 77, no. 20 (2003): 10841–49. http://dx.doi.org/10.1128/jvi.77.20.10841-10849.2003.

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ABSTRACT Entry of retroviruses into host cells requires the fusion between the viral and cellular membranes. It is unclear how receptor binding induces conformational changes within the surface envelope protein (SU) that activate the fusion machinery residing in the transmembrane envelope protein (TM). In this report, we have isolated a point mutation, Q252R, within the proline-rich region of the 4070A murine leukemia virus SU that altered the virus-cell binding characteristics and induced cell-cell fusion. Q252R displays a SU shedding-sensitive phenotype. Cell-cell fusion is receptor dependen

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RUDY. "Virus-cell fusion targeted for drug development." Chemical & Engineering News 74, no. 20 (1996): 45. http://dx.doi.org/10.1021/cen-v074n020.p045.

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Singethan, K., E. Topfstedt, S. Schubert, W. P. Duprex, B. K. Rima, and Jürgen Schneider-Schaulies. "CD9-dependent regulation of Canine distemper virus-induced cell–cell fusion segregates with the extracellular domain of the haemagglutinin." Journal of General Virology 87, no. 6 (2006): 1635–42. http://dx.doi.org/10.1099/vir.0.81629-0.

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Antibodies to CD9, a member of the tetraspan transmembrane-protein family, selectively inhibit Canine distemper virus (CDV)-induced cell–cell fusion. Neither CDV-induced virus–cell fusion nor cell–cell fusion induced by the closely related morbillivirus Measles virus (MV) is affected by anti-CD9 antibodies. As CDV does not bind CD9, an unknown, indirect mechanism is responsible for the observed inhibition of cell–cell fusion. It was investigated whether this effect was restricted to only one viral glycoprotein, either the haemagglutinin (H) or the fusion (F) protein, which form a fusion comple

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Harman, Andrew, Helena Browne, and Tony Minson. "The Transmembrane Domain and Cytoplasmic Tail of Herpes Simplex Virus Type 1 Glycoprotein H Play a Role in Membrane Fusion." Journal of Virology 76, no. 21 (2002): 10708–16. http://dx.doi.org/10.1128/jvi.76.21.10708-10716.2002.

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ABSTRACT Herpes simplex virus glycoprotein H (gH) is one of the four virion envelope proteins which are required for virus entry and for cell-cell fusion in a transient system. In this report, the role of the transmembrane and cytoplasmic tail domains of gH in membrane fusion was investigated by generating chimeric constructs in which these regions were replaced with analogous domains from other molecules and by introducing amino acid substitutions within the membrane-spanning sequence. gH molecules which lack the authentic transmembrane domain or cytoplasmic tail were unable to mediate cell-c

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Lifson, J., S. Coutré, E. Huang, and E. Engleman. "Role of envelope glycoprotein carbohydrate in human immunodeficiency virus (HIV) infectivity and virus-induced cell fusion." Journal of Experimental Medicine 164, no. 6 (1986): 2101–6. http://dx.doi.org/10.1084/jem.164.6.2101.

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Human immunodeficiency virus (HIV) envelope glycoprotein interactions with cell surface CD4 are involved in both virion infectivity and virally mediated cell fusion. D-mannose-specific lectins such as Con A specifically blocked virion infectivity and cell fusion. Studies with a recombinant vaccinia virus containing the HIV envelope gene demonstrated that Con A-mediated inhibition of HIV-induced fusion involved lectin binding to the viral envelope glycoprotein. These results indicate the importance of envelope glycosylation in the pathobiology of HIV infection, and suggest potential mechanisms

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Qing, Enya, Julisa Salgado, Alexandria Wilcox, and Tom Gallagher. "SARS-CoV-2 Omicron variations reveal mechanisms controlling cell entry dynamics and antibody neutralization." PLOS Pathogens 20, no. 12 (2024): e1012757. https://doi.org/10.1371/journal.ppat.1012757.

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Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) is adapting to continuous presence in humans. Transitions to endemic infection patterns are associated with changes in the spike (S) proteins that direct virus-cell entry. These changes generate antigenic drift and thereby allow virus maintenance in the face of prevalent human antiviral antibodies. These changes also fine tune virus-cell entry dynamics in ways that optimize transmission and infection into human cells. Focusing on the latter aspect, we evaluated the effects of several S protein substitutions on virus-cell membrane fus

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Yang, Yanling, Yuchen Wang, Danielle E. Campbell, et al. "SLC35A2 modulates paramyxovirus fusion events during infection." PLOS Pathogens 21, no. 1 (2025): e1012531. https://doi.org/10.1371/journal.ppat.1012531.

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Paramyxoviruses are significant human and animal pathogens that include mumps virus (MuV), Newcastle disease virus (NDV) and the murine parainfluenza virus Sendai (SeV). Despite their importance, few host factors implicated in paramyxovirus infection are known. Using a recombinant SeV expressing destabilized eGFP (rSeVCdseGFP) in a loss-of-function CRISPR screen, we identified the CMP-sialic acid transporter (CST) gene SLC35A1 and the UDP-galactose transporter (UGT) gene SLC35A2 as essential for paramyxovirus infection. As expected, SLC35A1 knockout (KO) cells showed drastic reduction in infec

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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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Marquardt, M. T., T. Phalen, and M. Kielian. "Cholesterol is required in the exit pathway of Semliki Forest virus." Journal of Cell Biology 123, no. 1 (1993): 57–65. http://dx.doi.org/10.1083/jcb.123.1.57.

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The enveloped alphavirus Semliki Forest virus (SFV) infects cells via a membrane fusion reaction triggered by low pH. For fusion to occur cholesterol is required in the target membrane, as demonstrated both in in vitro fusion assays and in vivo for virus infection of a host cell. In this paper we examine the role of cholesterol in postfusion events in the SFV life cycle. Cholesterol-depleted insect cells were transfected with SFV RNA or infected at very high multiplicities to circumvent the fusion block caused by the absence of cholesterol. Under these conditions, the viral spike proteins were

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Herschke, F., S. Plumet, T. Duhen, et al. "Cell-Cell Fusion Induced by Measles Virus Amplifies the Type I Interferon Response." Journal of Virology 81, no. 23 (2007): 12859–71. http://dx.doi.org/10.1128/jvi.00078-07.

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ABSTRACT Measles virus (MeV) infection is characterized by the formation of multinuclear giant cells (MGC). We report that beta interferon (IFN-β) production is amplified in vitro by the formation of virus-induced MGC derived from human epithelial cells or mature conventional dendritic cells. Both fusion and IFN-β response amplification were inhibited in a dose-dependent way by a fusion-inhibitory peptide after MeV infection of epithelial cells. This effect was observed at both low and high multiplicities of infection. While in the absence of virus replication, the cell-cell fusion mediated by

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Rawling, Joanna, Blanca García-Barreno, and José A. Melero. "Insertion of the Two Cleavage Sites of the Respiratory Syncytial Virus Fusion Protein in Sendai Virus Fusion Protein Leads to Enhanced Cell-Cell Fusion and a Decreased Dependency on the HN Attachment Protein for Activity." Journal of Virology 82, no. 12 (2008): 5986–98. http://dx.doi.org/10.1128/jvi.00078-08.

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ABSTRACT Cell entry by paramyxoviruses requires fusion of the viral envelope with the target cell membrane. Fusion is mediated by the viral fusion (F) glycoprotein and usually requires the aid of the attachment glycoprotein (G, H or HN, depending on the virus). Human respiratory syncytial virus F protein (FRSV) is able to mediate membrane fusion in the absence of the attachment G protein and is unique in possessing two multibasic furin cleavage sites, separated by a region of 27 amino acids (pep27). Cleavage at both sites is required for cell-cell fusion. We have investigated the significance

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Cheliout Da Silva, Sofia, Lianying Yan, Ha V. Dang, et al. "Functional Analysis of the Fusion and Attachment Glycoproteins of Mojiang Henipavirus." Viruses 13, no. 3 (2021): 517. http://dx.doi.org/10.3390/v13030517.

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Mojiang virus (MojV) is the first henipavirus identified in a rodent and known only by sequence data, whereas all other henipaviruses have been isolated from bats (Hendra virus, Nipah virus, Cedar virus) or discovered by sequence data from material of bat origin (Ghana virus). Ephrin-B2 and -B3 are entry receptors for Hendra and Nipah viruses, but Cedar virus can utilize human ephrin-B1, -B2, -A2 and -A5 and mouse ephrin-A1. However, the entry receptor for MojV remains unknown, and its species tropism is not well characterized. Here, we utilized recombinant full-length and soluble forms of the

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Gerg, Anthony, and Hana M. Dobrovolny. "Quantifying Impact of HIV Receptor Surface Density Reveals Differences in Fusion Dynamics of HIV Strains." Viruses 17, no. 4 (2025): 583. https://doi.org/10.3390/v17040583.

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Human Immunodeficiency Virus (HIV) Type-1 has been studied heavily for decades, yet one area that is still poorly understood is the virus’ ability to cause cell–cell fusion. In HIV, the fusion process is mediated by viral surface glycoproteins that bind to CD4 cell receptors. This virus-mediated cell fusion creates multi-nucleated cells called syncytia that can affect infection dynamics. Syncytia formation is often studied using a cell–cell fusion assay, in which donor cells expressing the viral surface protein fuse with acceptor cells expressing the cell receptor. A mathematical model capable

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Markosyan, Ruben M., Margaret Kielian, and Fredric S. Cohen. "Fusion Induced by a Class II Viral Fusion Protein, Semliki Forest Virus E1, Is Dependent on the Voltage of the Target Cell." Journal of Virology 81, no. 20 (2007): 11218–25. http://dx.doi.org/10.1128/jvi.01256-07.

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ABSTRACT Cells expressing the low pH-triggered class II viral fusion protein E1 of Semliki Forest virus (SFV) were fused to target cells. Fusion was monitored by electrical capacitance and aqueous dye measurements. Electrical voltage-clamp measurements showed that SFV E1-induced cell-cell fusion occurred quickly after acidification for a trans-negative potential across the target membrane (i.e., negative potential inside the target cell) but that a trans-positive potential eliminated all fusion. Use of an ionophore to control potentials for a large population of cells confirmed the dependence

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Chu, Victor C., Lisa J. McElroy, Vicky Chu, Beverley E. Bauman, and Gary R. Whittaker. "The Avian Coronavirus Infectious Bronchitis Virus Undergoes Direct Low-pH-Dependent Fusion Activation during Entry into Host Cells." Journal of Virology 80, no. 7 (2006): 3180–88. http://dx.doi.org/10.1128/jvi.80.7.3180-3188.2006.

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ABSTRACT Coronaviruses are the causative agents of respiratory disease in humans and animals, including severe acute respiratory syndrome. Fusion of coronaviruses is generally thought to occur at neutral pH, although there is also evidence for a role of acidic endosomes during entry of a variety of coronaviruses. Therefore, the molecular basis of coronavirus fusion during entry into host cells remains incompletely defined. Here, we examined coronavirus-cell fusion and entry employing the avian coronavirus infectious bronchitis virus (IBV). Virus entry into cells was inhibited by acidotropic ba

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