scholarly journals Role of cell membrane composition in receptor-mediated internalization of vesicular stomatitis virus in human HEp-2 cells.

1985 ◽  
Vol 260 (9) ◽  
pp. 5265-5270
Author(s):  
R Pottathil ◽  
P L Gutierrez ◽  
L H Davis ◽  
K A Chandrabose
1990 ◽  
Vol 64 (4) ◽  
pp. 1716-1725 ◽  
Author(s):  
D Blondel ◽  
G G Harmison ◽  
M Schubert

Proceedings ◽  
2020 ◽  
Vol 50 (1) ◽  
pp. 108
Author(s):  
Victor Latorre ◽  
Ron Geller

The viral order Mononegavirales consist of eight virus families. Members of these families include some of the most infectious (Measles, lethal (Ebola and Rabies), and most common viruses (Respiratory syncytial virus, RSV). Despite their medical importance, few vaccines and no antiviral treatments are available for treating infections with these viruses. Being obligate cellular parasites, viruses must rely on the cellular machinery for their replication. One example of this is the widespread use of molecular chaperones, which assist the correct folding of newly synthesized proteins, refold misfolded or aggregated proteins, and play key roles in maintaining proteostasis in cells. Targeting chaperones required for viral replication may, therefore, provide an antiviral approach. In this work, we set out to identify all the members of the cytoplasmic chaperone network that are involved in the replication of RSV using an RNA interference screen. Among our hits is valosin-containing protein (VCP; also known as p97), a chaperone involved in ubiquitin-mediated protein degradation, which has been shown to play a role in the life cycle of several viruses. We investigated the role of VCP during RSV and vesicular stomatitis virus (VSV) infections using specific VCP inhibitors. Our results suggest that VCP activity is necessary for RSV and VSV replication and may constitute a promising antiviral approach for the Mononegavirales.


2019 ◽  
Vol 40 (6Supl3) ◽  
pp. 3769
Author(s):  
Camila de Sousa Bezerra ◽  
Jéssica Tatiane Sauthier ◽  
Juliana Felipetto Cargnelutti ◽  
Gisele Cândida Ramalho ◽  
Denise Batista Nogueira ◽  
...  

This study aimed to determine the prevalence of vesicular stomatitis virus (VSV) in buffaloes in the state of Paraíba, Northeastern Brazil. The study was carried out in 14 herds in the municipalities of Alagoa Nova, Areia, Campina Grande, Guarabira, Juripiranga, Santa Helena, Sapê, Rio Tinto, Santana dos Garrotes, Itatuba, Solânea, and Cacimbas. The studied population was formed by buffalo females reared for meat and milk, comprising of mixed and Murrah breeds, at least 24 months of age. For the serological diagnosis of VSIV-3, the virus-neutralization test (VN) was performed, using the VSIV-3 isolate 2013 São Bento/Paraíba. Real prevalence was 2.6% for VSIV-3, with antibody titers ranging from 160 to 1280. This is the first study to characterize VSV circulation in the buffalo population in Northeastern Brazil, where infection is considered endemic; some aspects of virus maintenance are not fully understood, such as the role of reservoirs in endemic areas. The identification of seroreactive animals in this study demonstrates the circulation of VSIV-3 in the buffalo species. Reports of virus isolation in this species have not yet been described, which suggests the need for investigating the role of buffaloes in vesicular stomatitis epidemiology.


1996 ◽  
Vol 135 (1) ◽  
pp. 153-167 ◽  
Author(s):  
J Peränen ◽  
P Auvinen ◽  
H Virta ◽  
R Wepf ◽  
K Simons

Rab8 is a small Ras-like GTPase that regulates polarized membrane transport to the basolateral membrane in epithelial cells and to the dendrites in neurons. It has recently been demonstrated that fibroblasts sort newly synthesized proteins into two different pathways for delivery to the cell surface that are equivalent to the apical and the basolateral post-Golgi routes in epithelial cells (Yoshimori, T., P. Keller, M.G. Roth, and K. Simons. 1996. J. Cell Biol. 133:247-256). To determine the role of Rab8 in fibroblasts, we used both transient expression systems and stable cell lines expressing mutant or wild-type (wt) Rab8. A dramatic change in cell morphology occurred in BHK cells expressing both the wt Rab8 and the activated form of the GTPase, the Rab8Q67L mutant. These cells formed processes as a result of a reorganization of both their actin filaments and microtubules. Newly synthesized vesicular stomatitis virus G glycoprotein, a basolateral marker protein in MDCK cells, was preferentially delivered into these cell outgrowths. Based on these findings, we propose that Rab8 provides a link between the machinery responsible for the formation of cell protrusions and polarized biosynthetic membrane traffic.


2006 ◽  
Vol 87 (3) ◽  
pp. 673-678 ◽  
Author(s):  
Waris A. Shah ◽  
Huashan Peng ◽  
Salvatore Carbonetto

Dystroglycan (DG) is an extracellular matrix receptor necessary for the development of metazoans from flies to humans and is also an entry route for various pathogens. Lymphocytic choriomeningitis virus (LCMV), a member of the family Arenaviridae, infects by binding to α-DG. Here, the role of cholesterol lipid rafts in infection by LCMV via α-DG was investigated. The cholesterol-sequestering drugs methyl-β-cyclodextrin (MβCD), filipin and nystatin inhibited the infectivity of LCMV selectively, but did not affect infection by vesicular stomatitis virus. Cholesterol loading after depletion with MβCD restored infectivity to control levels. DG was not found in lipid rafts identified with the raft marker ganglioside GM1. Treatment with MβCD, however, enhanced the solubility of DG. This may reflect the association of DG with cholesterol outside lipid rafts and suggests that association of DG with non-raft cholesterol is critical for infection by LCMV through α-DG.


1985 ◽  
Vol 5 (10) ◽  
pp. 2502-2513 ◽  
Author(s):  
B W Grinnell ◽  
R R Wagner

The leader RNA transcript of vesicular stomatitis virus inhibits transcription of the adenovirus major late promoter and virus-associated genes in a soluble HeLa cell transcription system. We examined the specific nucleotide sequence involved and the potential role of leader-protein interactions in this inhibition of RNA polymerase II- and III-directed transcription. Using synthetic oligodeoxynucleotides homologous to regions of the leader RNA molecule, we extend our previous results (B.W. Grinnell and R.R. Wagner, Cell 36:533-543, 1984) that suggest a role for the AU-rich region of the leader RNA or the homologous AT region of a cloned cDNA leader in the inhibition of DNA-dependent transcription. Our results indicate that a short nucleotide sequence (AUUAUUA) or its deoxynucleotide homolog (ATTATTA) appears to be the minimal requirement for the leader RNA to inhibit transcription by both RNA polymerases, but sequences flanking both sides of this region increase the inhibitory activity. Nucleotide changes in the homologous AT-rich region drastically decrease the transcriptional inhibitory activity. Leader RNAs from wild-type virus, but not from a 5'-defective interfering particle, form a ribonuclease-resistant, protease-sensitive ribonucleoprotein complex in the soluble HeLa cell extract. Several lines of evidence suggest that the leader RNA specifically interacts with a 65,000-dalton (65K) cellular protein. In a fractionated cell extract, only those fractions containing this 65K protein could reverse the inhibition of DNA-dependent RNA synthesis by the plus-strand vesicular stomatitis virus leader RNA or by homologous DNA. In studies with synthetic oligodeoxynucleotides homologous to leader RNA sequences, only those oligonucleotides containing the inhibitory sequence were able to bind to a gradient fraction containing the 65K protein.


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