Last update 01 Nov 2024

HSV RNR

Last update 01 Nov 2024

Basic Info

Synonyms-

Introduction-

Drugs associated with HSV RNR

BILD-1357

Target

HSV RNR

Mechanism

HSV RNR inhibitors

Active Org.-

Originator Org.

Bio-Méga Research Division

Active Indication-

Inactive Indication

Herpes Simplex

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

BILD-1263

Target

HSV RNR

Mechanism

HSV RNR inhibitors

Active Org.-

Originator Org.

Bio-Méga Research Division

Active Indication-

Inactive Indication

Herpes Simplex [+1]

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with HSV RNR

100 Translational Medicine associated with HSV RNR

0 Patents (Medical) associated with HSV RNR

Literatures (Medical) associated with HSV RNR

19 Jun 2003·FEBS LettersQ3 · BIOLOGY

The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone‐like activity similar to Hsp27

Q3 · BIOLOGY

Article

Author: Jacques Landry ; Yves Langelier ; Bernard Massie ; A.Marie-Josée Sasseville ; Herman Lambert ; Hugo Lavoie ; Stéphane Chabaud ; Claire Guilbault

HSV‐2 R1, the R1 subunit of herpes simplex virus (HSV) ribonucleotide reductase, protects cells against apoptosis. Here, we report the presence in HSV‐2 R1 of a stretch exhibiting similarity to the α‐crystallin domain of the small heat shock proteins, a domain known to be important for oligomerization and cytoprotective activities of these proteins. Also, the HSV‐2 R1 protein, which forms multimeric structures in the absence of nucleotide, displayed chaperone ability as good as Hsp27 in a thermal denaturation assay using citrate synthase. In contrast, mammalian R1, which does not contain an α‐crystallin domain, has neither chaperone nor anti‐apoptotic activity. Thus, we propose that the chaperone activity of HSV‐2 R1 could play an important role in viral pathogenesis.

15 Feb 2003·Journal of VirologyQ2 · MEDICINE

The Early Expression of Glycoprotein B from Herpes Simplex Virus Can Be Detected by Antigen-Specific CD8⁺T Cells

Q2 · MEDICINE

Article

Author: Heath, William R. ; Castrucci, Maria R. ; Jones, Claerwen M. ; Chen, Weisan ; Carbone, Francis R. ; Kawaoka, Yoshihiro ; Mueller, Scott N.

ABSTRACTThe immune response to cutaneous herpes simplex virus type 1 (HSV-1) infection begins with remarkable rapidity. Activation of specific cytotoxic T lymphocytes (CTL) begins within hours of infection, even though the response within the draining lymph nodes peaks nearly 5 days later. HSV gene products are classified into three main groups, α, β, and γ, based on their kinetics and requirements for expression. In C57BL/6 mice, the immunodominant epitope from HSV is derived from glycoprotein B (gB498-505). While gB is considered a γ or “late” gene product, previous reports have indicated that some level of gene expression may occur soon after infection. Using brefeldin A as a specific inhibitor of viral antigen presentation to major histocompatibility complex class I-restricted CTL, we have formally addressed the timing of gB peptide expression in an immunologically relevant manner following infection. Presentation of gB peptide detected by T-cell activation was first observed within 2 h of infection. Comparison with another viral epitope expressed early during infection, HSV-1 ribonucleotide reductase, demonstrated that gB is presented with the same kinetics as this classical early-gene product. Moreover, this rapidity of gB expression was further illustrated via rapid priming of naïve transgenic CD8+T cells in vivo after HSV-1 infection of mice. These results establish that gB is expressed rapidly following HSV-1 infection, at levels capable of effectively stimulating CD8+T cells.

01 Nov 2002·Journal of General VirologyQ3 · MEDICINE

The R1 subunit of herpes simplex virus ribonucleotide reductase protects cells against apoptosis at, or upstream of, caspase-8 activation

Q3 · MEDICINE

Article

Author: Mosser, Dick D. ; Bergeron, Stéphane ; Denis, Stéphan ; Chabaud, Stéphane ; Sasseville, A. Marie-Josée ; Massie, Bernard ; Guilbault, Claire ; Langelier, Yves ; Lippens, Julie

The R1 subunit of herpes simplex virus (HSV) ribonucleotide reductase, which in addition to its C-terminal reductase domain possesses a unique N-terminal domain of about 400 amino acids, is thought to have an additional, as yet unknown, function. Here, we report that the full-length HSV-2 R1 has an anti-apoptotic function able to protect cells against death triggered by expression of R1(Δ2–357), an HSV-2 R1 subunit with its first 357 amino acids deleted. We further substantiate the R1 anti-apoptotic activity by showing that its accumulation at low level could completely block apoptosis induced by TNF-receptor family triggering. Activation of caspase-8 induced either by TNF or by Fas ligand expression was prevented by the R1 protein. As HSV R1 did not inhibit cell death mediated by several agents acting via the mitochondrial pathway (Bax overexpression, etoposide, staurosporine and menadione), it is proposed that it functions to interrupt specifically death receptor-mediated signalling at, or upstream of, caspase-8 activation. The N-terminal domain on its own did not exhibit anti-apoptotic activity, suggesting that both domains of R1 or part(s) of them are necessary for this new function. Evidence for the importance of HSV R1 in protecting HSV-infected cells against cytokine-induced apoptosis was obtained with the HSV-1 R1 deletion mutants ICP6Δ andhrR3. These results show that, in addition to its ribonucleotide reductase function, which is essential for virus reactivation, HSV R1 could contribute to virus propagation by preventing apoptosis induced by the immune system.

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HSV RNR

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