Evidence against involvement of host transcription in the replication of vaccinia and herpes simplex viruses

Virology ◽  
1982 ◽  
Vol 118 (1) ◽  
pp. 214-218 ◽  
Author(s):  
Morris Silver ◽  
Samuel Dales
Keyword(s):  
Herpes Simplex ◽  
Herpes Simplex Viruses

scholarly journals Antimicrobial, Antioxidant, and Cytotoxic Activities of Juglans regia L. Pellicle Extract

Antibiotics ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 159
Author(s):  
Floriana D’Angeli ◽  
Giuseppe Antonio Malfa ◽  
Adriana Garozzo ◽  
Giovanni Li Volti ◽  
Carlo Genovese ◽  
...  
Keyword(s):  
Herpes Simplex ◽  
Juglans Regia ◽  
Radical Scavenging ◽  
Fungal Growth ◽  
Bioactive Molecules ◽  
Total Phenolic ◽  
Cytotoxic Activities ◽  
Dependent Manner ◽  
Anion Formation ◽  
Herpes Simplex Viruses

The difficulty to treat resistant strains-related hospital-acquired infections (HAIs) promoted the study of phytoextracts, known sources of bioactive molecules. Accordingly, in the present study, the pharmacological activities of Juglans regia (L.) pellicle extract (WPE) were investigated. The antiviral effect was tested against Herpes simplex virus type 1 and 2, Poliovirus 1, Adenovirus 2, Echovirus 9, Coxsackievirus B1 through the plaque reduction assay. The antibacterial and antifungal activities were evaluated against medically important strains, by the microdilution method. DPPH and superoxide dismutase (SOD)s-like activity assays were used to determine the antioxidant effect. Besides, the extract was screened for cytotoxicity on Caco-2, MCF-7, and HFF1 cell lines by the 3-[4,5-dimethylthiazol-2-yl]-2,5 diphenyl tetrazolium bromide (MTT) assay. The total phenolic and flavonoid contents were also evaluated. Interestingly, WPE inhibited Herpes simplex viruses (HSVs) replication, bacterial and fungal growth. WPE showed free radical scavenging capacity and inhibited superoxide anion formation in a dose-dependent manner. These effects could be attributed to the high content of phenols and flavonoids, which were 0.377 ± 0.01 mg GE/g and 0.292 ± 0.08 mg CE/g, respectively. Moreover, WPE was able to reduce Caco-2 cell viability, at both 48 h and 72 h. The promising results encourage further studies aimed to better elucidate the role of WPE in the prevention of human infectious diseases.

Epidemiology of the herpes simplex viruses

1984 ◽  
Vol 2 (2) ◽  
pp. 29-45 ◽  
Author(s):  
William E. Rawls ◽  
Ole Hammerberg
Keyword(s):  
Herpes Simplex ◽  
Herpes Simplex Viruses

scholarly journals Disruption of Adherens Junctions Liberates Nectin-1 To Serve as Receptor for Herpes Simplex Virus and Pseudorabies Virus Entry

2002 ◽  
Vol 76 (14) ◽  
pp. 7203-7208 ◽  
Author(s):  
Miri Yoon ◽  
Patricia G. Spear
Keyword(s):  
Herpes Simplex ◽  
Epithelial Cells ◽  
Viral Entry ◽  
Pseudorabies Virus ◽  
Adherens Junctions ◽  
Cell Junctions ◽  
Immunoglobulin Superfamily ◽  
Calcium Depletion ◽  
Normal Medium ◽  
Herpes Simplex Viruses

ABSTRACT Nectin-1, a cell adhesion molecule belonging to the immunoglobulin superfamily, can bind to virion glycoprotein D (gD) to mediate entry of herpes simplex viruses (HSV) and pseudorabies virus (PRV). Nectin-1 colocalizes with E-cadherin at adherens junctions in epithelial cells. The disruption of cell junctions can result in the redistribution of nectin-1. To determine whether disruption of junctions by calcium depletion influenced the susceptibility of epithelial cells to viral entry, Madin-Darby canine kidney cells expressing endogenous nectin-1 or transfected human nectin-1 were tested for the ability to bind soluble forms of viral gD and to be infected by HSV and PRV, before and after calcium depletion. Confocal microscopy revealed that binding of HSV and PRV gD was localized to adherens junctions in cells maintained in normal medium but was distributed, along with nectin-1, over the entire cell surface after calcium depletion. Both the binding of gD and the fraction of cells that could be infected by HSV-1 and PRV were enhanced by calcium depletion. Taken together, these results provide evidence that nectin-1 confined to adherens junctions in epithelial cells is not very accessible to virus, whereas dissociation of cell junctions releases nectin-1 to serve more efficiently as an entry receptor.

Resistance of herpes simplex viruses to acyclovir: An update from a ten-year survey in France

2014 ◽  
Vol 111 ◽  
pp. 36-41 ◽  
Author(s):  
Emilie Frobert ◽  
Sonia Burrel ◽  
Sophie Ducastelle-Lepretre ◽  
Geneviève Billaud ◽  
Florence Ader ◽  
...  
Keyword(s):  
Herpes Simplex ◽  
Herpes Simplex Viruses

scholarly journals Multiple Receptor Interactions Trigger Release of Membrane and Intracellular Calcium Stores Critical for Herpes Simplex Virus Entry

2007 ◽  
Vol 18 (8) ◽  
pp. 3119-3130 ◽  
Author(s):  
Natalia Cheshenko ◽  
Wen Liu ◽  
Lisa M. Satlin ◽  
Betsy C. Herold
Keyword(s):  
Herpes Simplex ◽  
Intracellular Calcium ◽  
Viral Entry ◽  
Calcium Stores ◽  
Calcium Response ◽  
Herpes Simplex Viruses ◽  
Intracellular Calcium Stores ◽  
Viral Binding ◽  
Glycoprotein H ◽  
Simplex Virus

Herpes simplex viruses (HSV) harness cellular calcium signaling pathways to facilitate viral entry. Confocal microscopy and small interfering RNA (siRNA) were used to identify the source of the calcium and to dissect the requisite viral–cell interactions. Binding of HSV to human epithelial cells induced no calcium response, but shifting the cells to temperatures permissive for penetration triggered increases in plasma membrane calcium followed by a global release of intracellular calcium. Transfection with siRNA targeting the proteoglycan syndecan-2 blocked viral binding and abrogated any calcium response. Transfection with siRNA targeting nectin-1, a glycoprotein D receptor, also prevented both membrane and intracellular calcium responses. In contrast, the membrane response was preserved after transfection with siRNA targeting integrinαv, a novel glycoprotein H receptor. The membrane response, however, was not sufficient for viral entry, which required interactions with integrinαv and release of inositol-triphosphate receptor-dependent intracellular calcium stores. Thus, calcium plays a critical, complex role in HSV entry.

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