Herpes Research Today is a free monthly online journal that collates and summarizes the latest research about Herpes, including details on herpes simplex virus (hsv), genital, oral, symptoms, treatment.

Herpes simplex virus 1 microRNAs expressed abundantly during latent infection are not essential for latency in mouse trigeminal ganglia.

Kramer MF, Jurak I, Pesola JM, Boissel S, Knipe DM, Coen DM

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.

Several herpes simplex virus 1 microRNAs are encoded within or near the latency associated transcript (LAT) locus, and are expressed abundantly during latency. Some of these microRNAs can repress the expression of important viral proteins and are hypothesized to play important roles in establishing and/or maintaining latent infections. We found that in lytically infected cells and in acutely infected mouse ganglia, expression of LAT-encoded microRNAs was weak and unaffected by a deletion that includes the LAT promoter. In mouse ganglia latently infected with wild type virus, the microRNAs accumulated to high levels, but deletions of the LAT promoter markedly reduced expression of LAT-encoded microRNAs and also miR-H6, which is encoded upstream of LAT and can repress expression of ICP4. Because these LAT deletion mutants establish and maintain latent infections, these microRNAs are not essential for latency, at least in mouse trigeminal ganglia, but may help promote it.

Published 29 August 2011 in Virology, 417(2): 239-47.
Full-text of this article is available online (may require subscription).

Articles on Herpes published 25 August 2011:

Roles played by toll-like receptor-9 in corneal endothelial cells after herpes simplex virus type 1 infection.   Invest Ophthalmol Vis Sci, 52(9): 6729-36.

[Abstract] [Full-text]

Articles on Herpes published 23 August 2011:

Impact of herpes simplex virus type 2 on HIV-1 acquisition and progression in an HIV vaccine trial (the Step study).   J Acquir Immune Defic Syndr, 57(3): 238-44.

[Abstract] [Full-text]

Articles on Herpes published 18 August 2011:

Herpes simplex virus 1 protein kinase Us3 and major tegument protein UL47 reciprocally regulate their subcellular localization in infected cells.   J Virol, 85(18): 9599-613.

Us3 is a serine-threonine protein kinase encoded by herpes simplex virus 1 (HSV-1). We have identified UL47, a major virion protein, as a novel physiological substrate of Us3. In vitro kinase assays and systematic analysis of mutations at putative Us3 phosphorylation sites near the nuclear localization signal of UL47 showed that serine at residue 77 (Ser-77) was required for Us3 phosphorylation of UL47. Replacement of UL47 Ser-77 by alanine produced aberrant accumulation of UL47 at the nuclear ... [Abstract] [Full-text]

Direct and specific binding of the UL16 tegument protein of herpes simplex virus to the cytoplasmic tail of glycoprotein E.   J Virol, 85(18): 9425-36.

The UL16 tegument protein of herpes simplex virus (HSV) is conserved throughout all of the herpesvirus families. Previous studies have shown that the binding of HSV to heparan sulfate molecules on the host cell triggers the release of UL16 from the capsid, but the mechanism by which the signal is sent from the virion surface into the tegument is unknown. Here, we report that a glutathione S-transferase chimera bearing the cytoplasmic tail of viral glycoprotein E (gE) is capable of binding to ... [Abstract] [Full-text]

The histone acetyltransferase CLOCK is an essential component of the herpes simplex virus 1 transcriptome that includes TFIID, ICP4, ICP27, and ICP22.   J Virol, 85(18): 9472-7.

Studies published elsewhere have shown that the herpes simplex virus regulatory protein ICP0 interacts with BMAL1, a partner and regulator of circadian histone acetyltransferase CLOCK, that both proteins localize at ND10 bodies and are stabilized by viral proteins, that enzymatically active CLOCK partially complements ΔICP0 mutants, and that silencing of CLOCK suppresses the expression of viral genes. Here we report that CLOCK is a component of the transcriptional complex that includes TFIID, ... [Abstract] [Full-text]

Interaction and interdependent packaging of tegument protein UL11 and glycoprotein e of herpes simplex virus.   J Virol, 85(18): 9437-46.

The UL11 tegument protein of herpes simplex virus plays a critical role in the secondary envelopment; however, the mechanistic details remain elusive. Here, we report a new function of UL11 in the budding process in which it directs efficient acquisition of glycoprotein E (gE) via a direct interaction. In vitro binding assays showed that the interaction required only the first 28, membrane-proximal residues of the cytoplasmic tail of gE, and the C-terminal 26 residues of UL11. A second, weaker ... [Abstract] [Full-text]

Herpes simplex virus type 2 virion host shutoff protein suppresses innate dsRNA antiviral pathways in human vaginal epithelial cells.   J Gen Virol, 92: 1981-93.

Viruses that establish persistent infections have evolved numerous strategies to evade host innate antiviral responses. We functionally assessed the role of herpes simplex virus type 2 (HSV-2) virion host shutoff (vhs) protein on innate immune sensing pathways in human vaginal epithelial cells (VK2 ECs). Infection of cells with wild-type (WT) HSV-2 significantly decreased expression of innate immune sensors of viral infection, Toll-like receptor (TLR)2, TLR3, retinoic acid inducible gene I ... [Abstract] [Full-text]

Articles on Herpes published 9 August 2011:

Autocatalytic activity of the ubiquitin-specific protease domain of herpes simplex virus 1 VP1-2.   J Virol, 85(17): 8738-51.

The herpes simplex virus (HSV) tegument protein VP1-2 is essential for virus entry and assembly. VP1-2 also contains a highly conserved ubiquitin-specific protease (USP) domain within its N-terminal region. Despite conservation of the USP and the demonstration that it can act on artificial substrates such as polyubiquitin chains, identification of the relevance of the USP in vivo to levels or function of any substrate remains limited. Here we show that HSV VP1-2 USP can act on itself and is ... [Abstract] [Full-text]

© 2004-2011 Herpes Research Today. All Rights Reserved.