scholarly journals Survey of virally mediated permeability changes

1980 ◽  
Vol 190 (3) ◽  
pp. 639-646 ◽  
Author(s):  
K A Foster ◽  
K Gill ◽  
K J Micklem ◽  
C A Pasternak
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Viral Entry ◽  
Sendai Virus ◽  
Ependymal Cells ◽  
Cell Type ◽  
Organ Cultures ◽  
Nasal Turbinate ◽  
Permeability Changes ◽  
Mdbk Cells ◽  
Vesicular Stomatitis

1. Sendai virus causes permeability changes when added to freshly isolated brain cells (cerebellum or ependymal cells) or to a culture of forebrain cells. 2. Sendai virus causes permeability changes when added to organ cultures of ferret lung or nasal turbinate. Influenza virus causes no permeability changes under these conditions. 3. Rabies virus and vesicular-stomatitis virus, in contrast with Sendai virus, do not cause permeability changes in BHK cells or Lettrée cells. 4. Serum from patients suffering from viral hepatitis does not cause permeability changes in human leucocytes; addition to Sendai virus causes permeability changes. 5. It is concluded that permeability changes accompanying viral entry occur only with certain types of paramyxovirus, but that there is little restriction on cell type. 6. MDBK cells infected with Sendai virus show permeability changes during viral release, similar to those that occur during viral entry. Because these changes do not appear to be restricted to paramyxoviruses, they may have considerable clinical significance.

scholarly journals Cell Type Mediated Resistance of Vesicular Stomatitis Virus and Sendai Virus to Ribavirin

PLoS ONE ◽  
2010 ◽  
Vol 5 (6) ◽  
pp. e11265 ◽  
Author(s):  
Nirav R. Shah ◽  
Amanda Sunderland ◽  
Valery Z. Grdzelishvili
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Sendai Virus ◽  
Cell Type ◽  
Vesicular Stomatitis

scholarly journals Monitoring Viral Entry in Real-Time Using a Luciferase Recombinant Vesicular Stomatitis Virus Producing SARS-CoV-2, EBOV, LASV, CHIKV, and VSV Glycoproteins

Viruses ◽  
2020 ◽  
Vol 12 (12) ◽  
pp. 1457
Author(s):  
Maria Fernanda Lay Mendoza ◽  
Marissa Danielle Acciani ◽  
Courtney Nina Levit ◽  
Christopher Santa Maria ◽  
Melinda Ann Brindley
Keyword(s):  
Real Time ◽  
Vesicular Stomatitis Virus ◽  
Viral Entry ◽  
Cell Surface Receptor ◽  
Enveloped Virus ◽  
Glycoprotein G ◽  
Viral Glycoproteins ◽  
Surface Receptor ◽  
Vesicular Stomatitis ◽  
Time Required

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) GP, and Chikungunya (CHIKV) envelope (E) protein, we produced recombinant VSV (rVSV) viruses that produce the five glycoproteins. The rVSV virions encoded a nano luciferase (NLucP) reporter gene fused to a destabilization domain (PEST), which we used in combination with the live-cell substrate EndurazineTM to monitor viral entry kinetics in real time. Our data indicate that rVSV particles with glycoproteins that require more post-internalization priming typically demonstrate delayed entry in comparison to VSV G. In addition to determining the time required for each virus to complete entry, we also used our system to evaluate viral cell surface receptor preferences, monitor fusion, and elucidate endocytosis mechanisms. This system can be rapidly employed to examine diverse viral glycoproteins and their entry requirements.

Enhancement of vesicular stomatitis virus production by serum

1971 ◽  
Vol 17 (9) ◽  
pp. 1149-1155
Author(s):  
G. M. Kouroupis ◽  
L. R. Sabina
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Virus Production ◽  
Viral Rna ◽  
Radioactive Label ◽  
Serum Free ◽  
Mdbk Cells ◽  
Time Of Infection ◽  
Vesicular Stomatitis ◽  
Free Media ◽  
Replicative Cycle

The production of vesicular stomatitis virus in MDBK cells has been shown to be markedly enhanced by the addition of whole serum to maintenance media. Maximum virus production occurred in the presence of human and fetal calf sera. When different serum protein fractions were tested, cultures nourished with medium containing bovine fraction IV-1 gave the highest infectivity, but fraction IV-1 did not completely substitute for whole serum. In contrast, fetuin was strongly inhibitory for the production of infectious virus. No loss of infectivity was observed if serum was added to cultures as late as 8 h postinfection. The incorporation of 3H-uridine into viral RNA of actinomycin D treated cultures nourished with serum or serum-free media proceeded at nearly similar rates from the time of infection up to 7 h postinfection. This result indicates that viral RNA synthesis was initiated with equal amounts of template. Late in the virus replicative cycle the incorporation rates of radioactive label were higher in serum-containing cultures than in serum-free cultures. The results of this investigation suggest that serum does not have a direct specific viral function but rather acts indirectly through the host cell to promote maximum virus production.

scholarly journals Structure of the Dimerization Domain of the Rabies Virus Phosphoprotein

2010 ◽  
Vol 84 (7) ◽  
pp. 3707-3710 ◽  
Author(s):  
Ivan Ivanov ◽  
Thibaut Crépin ◽  
Marc Jamin ◽  
Rob W. H. Ruigrok
Keyword(s):  
Crystal Structure ◽  
Rabies Virus ◽  
Vesicular Stomatitis Virus ◽  
Hydrophobic Interactions ◽  
Sendai Virus ◽  
Hydrophobic Surfaces ◽  
Dimerization Domain ◽  
Tetramerization Domain ◽  
Helical Hairpin ◽  
Vesicular Stomatitis

ABSTRACT The crystal structure of the dimerization domain of rabies virus phosphoprotein was determined. The monomer consists of two α-helices that make a helical hairpin held together mainly by hydrophobic interactions. The monomer has a hydrophilic and a hydrophobic face, and in the dimer two monomers pack together through their hydrophobic surfaces. This structure is very different from the dimerization domain of the vesicular stomatitis virus phosphoprotein and also from the tetramerization domain of the Sendai virus phosphoprotein, suggesting that oligomerization is conserved but not structure.

scholarly journals Double-Layered Membrane Vesicles Released from Mammalian Cells Infected with Sendai Virus Expressing the Matrix Protein of Vesicular Stomatitis Virus

Virology ◽  
1999 ◽  
Vol 263 (1) ◽  
pp. 230-243 ◽  
Author(s):  
Takemasa Sakaguchi ◽  
Tsuneo Uchiyama ◽  
Yutaka Fujii ◽  
Katsuhiro Kiyotani ◽  
Atsushi Kato ◽  
...  
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Mammalian Cells ◽  
Matrix Protein ◽  
Sendai Virus ◽  
Membrane Vesicles ◽  
The Matrix ◽  
Vesicular Stomatitis

scholarly journals The role of environmental factors on the evolution of phenotypic diversity in vesicular stomatitis virus populations

2013 ◽  
Vol 94 (4) ◽  
pp. 860-868 ◽  
Author(s):  
Sarah D. Smith-Tsurkan ◽  
Roger A. Herr ◽  
Sadik Khuder ◽  
Claus O. Wilke ◽  
Isabel S. Novella
Keyword(s):  
Environmental Factors ◽  
Vesicular Stomatitis Virus ◽  
Phenotypic Diversity ◽  
Cell Type ◽  
Persistent Infections ◽  
Acute Infections ◽  
Vesicular Stomatitis ◽  
Virus Adaptation ◽  
Virus Strains

Virus adaptation to an ever-changing environment requires the availability of variants with phenotypes that can fulfil new requirements for replication. High mutation rates result in the generation of these variants. The factors that contribute to the maintenance or elimination of this diversity, however, are not fully understood. This study used a collection of vesicular stomatitis virus strains generated under different conditions to measure the extent of variation within each population, and tested the effects of several environmental factors on diversity. It was found that the host-cell type used for selection sometimes had an effect on the extent of variation and that there may be different levels of variation over time. Persistent infections promoted higher levels of diversity than acute infections, presumably due to complementation. In contrast, environmental heterogeneity, host breadth and the cell type used for testing (as opposed to the cell type used for selection) did not seem to have an effect on the amount of phenotypic diversity observed.

scholarly journals A GP64-Null Baculovirus Pseudotyped with Vesicular Stomatitis Virus G Protein

2001 ◽  
Vol 75 (6) ◽  
pp. 2544-2556 ◽  
Author(s):  
J. T. Mangor ◽  
S. A. Monsma ◽  
M. C. Johnson ◽  
G. W. Blissard
Keyword(s):  
G Protein ◽  
Vesicular Stomatitis Virus ◽  
Viral Entry ◽  
Viral Envelope ◽  
Productive Infection ◽  
Pseudotyped Virus ◽  
Sf9 Cells ◽  
Viral Envelope Protein ◽  
Virion Protein ◽  
Vesicular Stomatitis

ABSTRACT The Autographa californica multiple nucleopolyhedrovirus (AcMNPV) GP64 protein is an essential virion protein that is involved in both receptor binding and membrane fusion during viral entry. Genetic studies have shown that GP64-null viruses are unable to move from cell to cell and this results from a defect in the assembly and production of budded virions (BV). To further examine requirements for virion budding, we asked whether a GP64-null baculovirus, vAc64−, could be pseudotyped by introducing a heterologous viral envelope protein (vesicular stomatitis virus G protein [VSV-G]) into its membrane and whether the resulting virus was infectious. To address this question, we generated a stably transfected insect Sf9 cell line (Sf9VSV-G) that inducibly expresses the VSV-G protein upon infection with AcMNPV Sf9VSV-G and Sf9 cells were infected with vAc64−, and cells were monitored for infection and for movement of infection from cell to cell. vAc64− formed plaques on Sf9VSV-G cells but not on Sf9 cells, and plaques formed on Sf9VSV-G cells were observed only after prolonged intervals. Passage and amplification of vAc64− on Sf9VSV-G cells resulted in pseudotyped virus particles that contained the VSV-G protein. Cell-to-cell propagation of vAc64− in the G-expressing cells was delayed in comparison to wild-type (wt) AcMNPV, and growth curves showed that pseudotyped vAc64− was generated at titers of approximately 106 to 107 infectious units (IU)/ml, compared with titers of approximately 108 IU/ml for wt AcMNPV. Propagation and amplification of pseudotyped vAc64− virions in Sf9VSV-G cells suggests that the VSV-G protein may either possess the signals necessary for baculovirus BV assembly and budding at the cell surface or may otherwise facilitate production of infectious baculovirus virions. The functional complementation of GP64-null viruses by VSV-G protein was further demonstrated by identification of a vAc64−-derived virus that had acquired the G gene through recombination with Sf9VSV-G cellular DNA. GP64-null viruses expressing the VSV-G gene were capable of productive infection, replication, and propagation in Sf9 cells.

scholarly journals A replication-competent vesicular stomatitis virus for studies of SARS-CoV-2 spike-mediated cell entry and its inhibition

2020 ◽  
Author(s):  
M. Eugenia Dieterle ◽  
Denise Haslwanter ◽  
Robert H. Bortz ◽  
Ariel S. Wirchnianski ◽  
Gorka Lasso ◽  
...  
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Viral Entry ◽  
Cell Entry ◽  
Immune Protection ◽  
Mechanistic Studies ◽  
Fluorescent Reporter ◽  
Large Panel ◽  
Vesicular Stomatitis ◽  
Highly Correlated ◽  
Humoral Responses

SummaryThere is an urgent need for vaccines and therapeutics to prevent and treat COVID-19. Rapid SARS-CoV-2 countermeasure development is contingent on the availability of robust, scalable, and readily deployable surrogate viral assays to screen antiviral humoral responses, and define correlates of immune protection, and to down-select candidate antivirals. Here, we describe a highly infectious recombinant vesicular stomatitis virus bearing the SARS-CoV-2 spike glycoprotein S as its sole entry glycoprotein that closely resembles the authentic agent in its entry-related properties. We show that the neutralizing activities of a large panel of COVID-19 convalescent sera can be assessed in high-throughput fluorescent reporter assay with rVSV-SARS-CoV-2 S and that neutralization of the rVSV and authentic SARS-CoV-2 by spike-specific antibodies in these antisera is highly correlated. Our findings underscore the utility of rVSV-SARS-CoV-2 S for the development of spike-specific vaccines and therapeutics and for mechanistic studies of viral entry and its inhibition.

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