Ultratrace determination of penciclovir-triphosphate (PCV-TP) in a herpes simplex virus type 1 (HSV-1)-infected cell line using flow-injection electrospray ionization tandem mass spectrometry (MS-MS)

1995 ◽  
Vol 26 (3) ◽  
pp. A232
Keyword(s):  
Mass Spectrometry ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Infected Cell ◽  
Infected Cell Line ◽  
Tandem Mass ◽  
Simplex Virus ◽  
Ionization Tandem Mass Spectrometry

The glycoproteins C and G are equivalent target antigens for the determination of herpes simplex virus type 1-specific antibodies

2010 ◽  
Vol 166 (1-2) ◽  
pp. 42-47 ◽  
Author(s):  
Thomas Scheper ◽  
Sandra Saschenbrecker ◽  
Katja Steinhagen ◽  
Andreas Sauerbrei ◽  
Waltraud Suer ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Specific Antibodies ◽  
Simplex Virus

scholarly journals Flow cytometric analysis of herpes simplex virus type 1 susceptibility to acyclovir, ganciclovir, and foscarnet.

1997 ◽  
Vol 41 (12) ◽  
pp. 2686-2692 ◽  
Author(s):  
I Pavić ◽  
A Hartmann ◽  
A Zimmermann ◽  
D Michel ◽  
W Hampl ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cytopathic Effect ◽  
Flow Cytometric Analysis ◽  
Flow Cytometric ◽  
Resistant Strains ◽  
Simplex Virus

We established a quantitative flow cytometric method for determination of herpes simplex virus type 1 (HSV-1) susceptibility to acyclovir (ACV), ganciclovir, and foscarnet in vitro. Susceptibility was defined in terms of the drug concentration which reduced the number of cells expressing HSV-1 glycoprotein C (gpC) with a fluorescence intensity of > or =10(2) by 50% (IC50). Flow cytometry allowed us to use a high (1.0) as well as a low (0.005) multiplicity of infection, and determination of the IC50 was possible after one or more viral replicative cycles. IC50s were dependent on virus input and on time postinfection. In mixture experiments, 1 to 2% resistant viruses added to a sensitive strain could be detected. The results obtained by flow cytometry showed a good qualitative correlation with those achieved by cytopathic effect inhibitory assay. However, flow cytometry might detect more quantitative differences in drug susceptibility, especially among resistant strains, as confirmed also by determination of intracellular drug phosphorylation. The mean IC50s for ACV-sensitive strains were 0.45 to 1.47 microM, and those for ACV-resistant strains were between 140 and 3,134 microM. Flow cytometric analysis was fast and accurate, automatizable, and highly reproducible. Flow cytometry may be a more powerful tool than standard cytopathic effect-based assays and could have advantages for the detection of low levels of drug resistance or mixtures of sensitive and resistant virus strains.

scholarly journals The herpes simplex virus type 1 infected cell protein 22

2010 ◽  
Vol 25 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Fu-sen Lin ◽  
Qiong Ding ◽  
Hong Guo ◽  
Alan C. Zheng
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Infected Cell ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Cell Protein ◽  
Infected Cell Protein ◽  
Simplex Virus

scholarly journals Biochemical analysis of infected cell polypeptide (ICP)0, ICP4, UL7 and UL23 incorporated into extracellular herpes simplex virus type 1 virions

2012 ◽  
Vol 93 (3) ◽  
pp. 624-634 ◽  
Author(s):  
Sandra Loret ◽  
Roger Lippé
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Infected Cell ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Proteomics Data ◽  
Virus Particles ◽  
Simplex Virus ◽  
Hsv 1

Herpes simplex virus type 1 (HSV-1) capsids assemble in the nucleus but acquire their teguments from various cellular compartments. Unfortunately, little is known about their exact arrangement and when they coat the newly produced capsids. The complexity of the virions is further highlighted by our recent proteomics analysis that detected the presence of several novel or controversial components in extracellular HSV-1 virions. The present study probes the localization and linkage to the virus particles of some of these incorporated proteins. We confirm the recently reported tight association of infected cell polypeptide (ICP)0 with the capsid and show that this property extends to ICP4. We also confirm our proteomics data and show biochemically that UL7 and UL23 are indeed mature virion tegument components that, unlike ICP0 and ICP4, are salt-extractable. Interestingly, treatment with N-ethylmaleimide, which covalently modifies reduced cysteines, strongly prevented the release of UL7 and UL23 by salts, but did not perturb the interactions of ICP0 and ICP4 with the virus particles. This hitheir at distinct biochemical properties of the virion constituents and the selective implication of reduced cysteines in their organization and dynamics. Finally, the data revealed, by two independent means, the presence of ICP0 and ICP4 on intranuclear capsids, consistent with the possibility that they may at least partially be recruited to the virus particles early on. These findings add significantly to our understanding of HSV-1 virion assembly and to the debate about the incorporation of ICP0 and ICP4 in virus particles.

scholarly journals RNA Binding by the Herpes Simplex Virus Type 1 Nucleocytoplasmic Shuttling Protein UL47 Is Mediated by an N-Terminal Arginine-Rich Domain That Also Functions as Its Nuclear Localization Signal

2006 ◽  
Vol 81 (5) ◽  
pp. 2283-2296 ◽  
Author(s):  
Michelle Donnelly ◽  
Janneke Verhagen ◽  
Gillian Elliott
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Infected Cell ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Rna Binding ◽  
Localization Signal ◽  
Simplex Virus

ABSTRACT The function of the alphaherpesvirus UL47 tegument protein has not yet been defined. Nonetheless, previous studies with transfected cells have shown that both the herpes simplex virus type 1 homologue (hUL47, or VP13/14) and the bovine herpesvirus type 1 (BHV-1) homologue (bUL47, or VP8) have the capacity to shuttle between the nucleus and the cytoplasm. Furthermore, hUL47 packaged into the virion has also been shown to bind several individual virus-specific RNA transcripts. Here, we extend these observations and show that hUL47 binds a wide range of RNA species in vitro. It has a high affinity for polyadenylated transcripts but has no apparent selectivity for virus-encoded RNA over cellular RNA. We also show that the virion population of bUL47 binds RNA in vitro. However, while purified recombinant hUL47 retains its RNA binding activity, recombinant bUL47 does not, suggesting that the BHV-1 homologue may require virus-induced modification for its activity. We identify the minimal RNA binding domain in hUL47 as a 26-residue N-terminal peptide containing an arginine-rich motif that is essential but not sufficient for optimal RNA binding, and we demonstrate that this RNA binding domain incorporates the hUL47 minimal nuclear localization signal. In addition, we show that soon after hUL47 is expressed during infection, it colocalizes in the infected cell nucleus with ICP4, the major virus transcriptional activator. Using RNA immunoprecipitations, we demonstrate that hUL47 is also bound in vivo to at least one viral transcript, the ICP0 mRNA. Taken together, these results suggest that hUL47 may play a role in RNA biogenesis in the infected cell.

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