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Herpes simplex virus (HSV-2, DNA virus) on and in a peripheral blood lymphocyte (Herpesviridae Family). For licensing, contact Dennis Kunkel (scientific stock photography, science images, science stock photography, electron microscopy images, biomedical microscopy photos, microscopic pictures, microscope photos). Glycoproteins that exhibit strong immunological responses in patients with herpes infection are targets for diagnostic as well as therapeutic utility. Bio-Rad has taken advantage of some minor antigenic variation in glycoprotein G (also referred as gG) between the two subtypes in order to develop type-specific polypeptide probes for detecting IgG antibodies to HSV-1 and HSV-2.
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Emerging evidence highlights a critical role for protein acetylation during herpesvirus infection. Human histone deacetylase (HDAC) interactions with viral proteins during herpesvirus infection. Biological, medical and general sciences images are available for licensed, rights-managed, non-exclusive use. Dennis Kunkel Ph.D has over 35 years of microscopy expertise in biological and medical sciences.
The Herpes Simplex Envelope contains at least 11 glycoproteins that exhibit significant protein and DNA (50%) homology between the two herpes immunological variants, type 1 (HSV-1) and type 2 (HSV-2). This was achieved by constructing the HSV-1 specific recombinant antigen and HSV-2* specific synthetic peptide conjugated to BSA. To support this effort, the company has implemented a discount policy that allows high school and college teaching laboratories to purchase kits, instruments, reagents, and other equipment at preferred prices. Ob Tag oder Nacht, ihr glamouroses, raffiniertes Funkeln macht diese Kreation immer zu einem begehrten Style-Favoriten! As prominent modulators of protein acetylation, histone deacetylases (HDACs) are essential transcriptional and epigenetic regulators. IntroductionProtein acetylation has recently emerged as a critical regulatory factor during herpesvirus infection.
Acetylation-dependent localization of IFI16 allows dual-compartment sensing of viral DNA, promoting pro-inflammatory response and innate immune signaling during herpesvirus infection. RIG-I, a sensor of viral double-stranded RNA that acts through the MAVS adapter protein to induce IFN signaling [83], is acetylated at Lys858 within its C-terminal repression domain [13]. Microscopy photographs (science images, electron microscope images, photomicrographs, microscopy photos, microscope photos, microscopic pictures) are available for use in editorial and commercial formats.
Not surprisingly, viruses have evolved a wide array of mechanisms to subvert HDAC functions. As components of the CoREST complex, HDAC1 and HDAC2 act as repressors of host gene transcription within the nucleus.
While Lys858 acetylation has yet to be tested for modulation of RIG-I activity, acetylation of PRRs and HDAC modulation of PRR activities may be a more prominent regulatory feature of the innate immune system than currently appreciated.Once PRRs bind their pathogen-derived ligands, innate immune signals are transmitted to neighboring cells via cytokine production and secretion. Image categories include Algae, Arachnids, Bacteria, Crystals, Fungi, Insects, Invertebrates, Medical, Miscellaneous, Plants, Protozoa, Vertebrates and Viruses.
These studies examined herpes simplex virus 1 (HSV-1), human cytomegalovirus (HCMV), Kaposi’s sarcoma-associated herpesvirus (KSHV) and Epstein-Barr virus (EBV) [1,2,3,4], thereby pointing to similarities among alpha-, beta- and gamma-herpesvirus infections.
No images or graphics on this site may be used without written permission of their respective owners. During latent infection, the HSV-1 genome is assembled into an ordered nucleosome-associated structure; however, during active lytic infection, the structure of viral chromatin exists in a more disordered state [5,6]. Resembling viral replication compartments, these structures suggest a function for this complex in active transcription of the viral genome [28]. Animals treated with valproic acid (VPA), a broad-acting HDAC inhibitor, exhibit increased susceptibility to infection by bacterial and fungal pathogens, while being protected from septic shock [73].
Finally, we provide a perspective on the contribution of current mass spectrometry-based “omic” technologies to infectious disease research, offering a systems biology view of infection.
In lytic stages of infection, histones associate with herpesvirus promoter regions, and chromatin adopts a conformation consistent with more actively transcribed host genomic regions [6]. As LSD1 is an established histone demethylase, this association can couple demethylase and deacetylase activities for coordinated regulation of histone post-translational modifications associated with the viral genome [28,29,30].
Moreover, it is well established that the post-translational modification of herpesvirus-associated histone tails is important for the regulation of viral gene transcription [7,8,9,10,11]. It is possible that the association of separate viral factors could trigger preferential association of specific accessory demethylases with the core CoREST complex. Given the significance of acetylation during viral infection and its requirement for essential host functions, knowledge of the regulation of the enzymes controlling protein acetylation is critical for understanding viral pathogenicity and host defense.
This position is further emphasized by the recent finding that acetylation is a more prominent post-translational modification than previously thought, with several thousand host protein acetylations identified to date [12,13].

Among the enzymes involved in regulating protein acetylation are the human histone deacetylases (HDACs), which remove acetylations from their substrates [14].
However, dampened cytokine expression does not necessarily correlate with repressive chromatin modifications, as histone H4 acetylation at Tnf and IL6 promoters has been shown to increase following TSA treatment [73]. Along with the numerous histone acetyltransferases (HATs) responsible for lysine acetylation, HDACs control the activity of substrates by acting as components of diverse multi-protein complexes with co-repressor functions (reviewed in [15,16]). Both HDAC1 and HDAC2 hyperphosphorylation during herpesvirus infection depends on the activity of US3, yet HDAC phosphorylation appears to be an indirect effect of US3 activity, suggesting the involvement of additional viral or host kinases (Figure 1A) [36,37]. Thus, it is likely that a significant subset of the immunosuppressive, anti-inflammatory effects of HDAC inhibitors occur at a non-histone level. HDACs themselves are a conserved family of proteins that evolutionarily predate histones, indicating that their interactions with non-histone proteins are integral to their cellular functions [17].
In the absence of infection, phosphorylation is an established regulator of HDAC1 and HDAC2 activity and protein associations. Given the array of human deacetylases, which encompasses eleven Zn2+-dependent HDACs and seven NAD+-dependent sirtuins (SIRTs), as well as their ability to participate in multiple protein complexes, viral interactions with members of this enzymatic family are likely to be protein-specific and individually regulated. HDACs have been linked to viral replication and pathogenesis during infection with a variety of human pathogens, including herpesviruses, hepatitis B and C, HIV-1 and HPV (reviewed in [18]). Similarly, mSin3 and Mi2 (member of the NuRD complex) preferentially associate with phosphorylated HDAC2 [50]. It is therefore not surprising that, during co-evolution with their hosts, viruses have gathered finely tuned mechanisms for targeting HDACs to either appropriate or inhibit their enzymatic activities. The activity of viral kinases and perturbations in kinase signaling pathways could alter the phosphorylation landscape of these proteins, ultimately contributing to aberrant regulation of HDACs and rearrangement of HDAC complexes. During HCMV infection, HDACs are recruited to the viral MIEP promoters by Daxx, a component of PML bodies, to repress viral gene expression at early stages of infection [47].
These observations highlight the importance of understanding the mechanisms of HDAC regulation during viral infection.In this review, we summarize the mechanisms employed by herpesviruses to perturb the functions of this important family of host transcriptional regulators, the histone deacetylases. Phosphorylations can directly mediate HDAC protein interactions; however, a second level of regulation results from phosphorylation-dependent changes in HDAC localization. However, this intrinsic immune defense mechanism is counteracted by the activity of viral proteins.
Next, we discuss the roles of acetylation in regulating host defense mechanisms against herpesvirus infection. Class IIa HDACs (HDAC4, -5, -7 and -9) shuttle between the nucleus and the cytoplasm through a mechanism that relies on site-specific phosphorylation of 14-3-3 binding sites [51,52,53,54]. Specifically, the HCMV protein pp71 promotes degradation of Daxx, and the interaction of the immediate early viral proteins, IE1 and IE2, with HDAC3 relieves repression of viral transcription [46,47].
Finally, we provide a perspective on the promise of emerging “omic” technologies for gaining a systems biology view of infection and an in-depth understanding of virus-induced changes within cellular pathways.
Interestingly, the subcellular distribution of class IIa HDACs has also been observed to be dynamic during infection. This mechanism of evading HDAC-mediated anti-viral response appears to be conserved across species, as the mouse CMV protein mIE1 is also reported to bind mHDAC2, which is recruited to ND10 structures via PML and Daxx [86]. HDAC4, -5 and -7 co-localize with ICP0 within the nucleus during HSV-1 infection (Figure 1A) [48]. Consistent with a model in which HDAC activity represses viral gene transcription through association with the HCMV MIEP, HDAC inhibition has been demonstrated to rescue IE gene expression [87]. ICP0 was shown to physically interact with these enzymes via the conserved N-terminal extensions shared by class IIa HDACs and absent in their class I counterparts [48]. During HSV-1 infection, disruption of ND10 structures is necessary for productive viral replication and is accomplished by ICP0 [88]. ICP0 serves to relieve repression of MEF2 induced by the binding of HDAC N-terminal domains to MEF2. Moreover, ICP0 promotes the disruption of HDAC1-CoREST to enhance viral gene expression and replication [31,34]. However, transcription mediated by the HDAC C-terminal deacetylation domain was not relieved by ICP0, consistent with continued co-localization of HDACs with SMRT, another member of the nuclear co-repressor complex [48].
An N-terminal domain of ICP0 shares homology with and binds to a C-terminal domain of CoREST immediately adjacent to the HDAC1 binding site [34].
Increased viral gene expression allows the growing population of ICP0 to outcompete HDAC1 in the binding of CoREST. Therefore, the phosphorylation status of HDACs significantly contributes to the regulation of both protein interactions and localizations in the context of infection. Through this mechanism, ICP0 promotes inhibition of CoREST-associated gene repression by abolishing its interaction with HDAC1.
Recent results have demonstrated that Aurora B-dependent phosphorylation of class IIa HDACs modulates cell cycle-dependent functions of these enzymes, indicating that HDAC phosphorylations are both spatially and temporally regulated [55]. The importance of temporally regulated phosphorylations during viral infection remains to be established.Altogether, multiple viral factors, including ICP0, ICP8 and US3, promote changes in the localization and functional roles of HDACs and co-repressor complexes during HSV-1 infection to promote viral reproduction.

Further investigation of viral protein interactions with HDACs will contribute to development of a comprehensive understanding of the roles of individual HDAC family members during HSV-1 infection. Careful regulation of viral gene expression is necessary for efficient replication, but also for maintenance of latency. As SMRT also associates with HDAC3 and class IIa HDACs, it is possible that multiple co-repressor complexes are recruited by EBNA3C to modulate complex-specific functions during infection [23,59]. Specifically, the de-phosphorylation of MEF2D has been shown to be important for regulating HDAC-mediated repression of Zp [61]. A consequence of this interaction is limited production of the immediate early viral protein BLZF1, which is a transcriptional activator important for exit from latency [60,61]. The temporal regulation of EBV gene expression is not only connected to HDAC transcriptional repressive functions (as in the case of MEF2), but also to deacetylation activity. HDAC1 and HDAC2 stably associate with the telomere repeat factor 2 (TRF2), which binds the EBV origin of plasmid replication (OriP) (Figure 1C) [43]. Thus, the temporal regulation of genome acetylation status and gene expression by HDACs is important for the preservation of latent stores of EBV within the host cell.In addition to protein interactions, signaling pathways activated by viral infection affect HDAC activities, possibly through signal-dependent post-translational modification. The KSHV protein vGPCR has been reported to induce signaling pathways that converge on HDACs, among other targets [62].
These kinases are well-established regulators of nuclear export of class IIa HDACs [51,64], indicating that HDAC phosphorylation during infection may be an important strategy for virus-mediated control of HDAC activity and complex formation. HDACs 1, 5 and 7 were shown to associate with the ORF50 promoter during KSHV latency, and the acetylation status of the latency-associated nuclear antigen (LANA) was dependent on HDAC activity [2,44]. The KSHV LANA protein can also interact with the HDAC co-repressor complex mSin3 during EBV infection [65].
Given the importance of temporal coordination of viral gene programs, cell cycle-dependent kinase cascades could provide an additional level of regulation of gene expression during infection. Interestingly, ORF50 is also capable of repressing p53 transcriptional activity through an interaction with the CREB binding protein, CBP [66,67]. As p53 activity is regulated by acetylation, it is tempting to speculate that p53-associated responses to viral infection are, in part, due to misregulation of deacetylase complexes [68,69].Altogether, these studies have demonstrated that gamma-herpesviruses EBV and KSHV co-opt HDAC complexes to repress viral gene expression. These mechanisms likely allow for maintenance of the viral genome in a latent state until conditions are advantageous for viral replication.
Viral infection further alters HDAC activity through activation of phosphorylation signaling cascades, thereby modulating the phosphorylation states and activities of individual HDAC enzymes.
IFI16 Acetylation and Host Detection of Viral DNAIn mammals, induction of host innate immunity in response to viral infection begins with the detection of pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) by intracellular pattern recognition receptors (PRRs). Several classes of PRRs have been characterized, including AIM2-like receptors (ALRs), retinoic acid-inducible gene I-like receptors (RLRs), nucleotide oligomerization domain-like receptors (NLRs), Toll-like receptors (TLRs) and an assorted array of cytoplasmic DNA receptors [75]. These PRRs are predominantly localized to the cytosol, plasma membrane and endosome to sense and respond to a wide range of invading pathogens.
Surprisingly, recent studies have extended the range of host immuno-surveillance to the nucleus, where the DNA sensor IFI16 selectively detects the double-stranded DNA genome of herpesviruses during infection [70] (Figure 2). As an ALR family member, IFI16 senses nuclear and cytoplasmic herpesvirus DNA, inducing pro-inflammatory and interferon responses via distinct pathways to limit viral replication and spread (Figure 2) [70,75,76,77,78,79,80].
In the cytoplasm, IFI16 associates with the signaling adapter protein STING (stimulator of interferon genes) upon binding of viral DNA, subsequently activating IRF3 and NF-?B transcription factors, which then translocate to the nucleus and induce robust interferon-? (IFN-?) expression [75,80]. However, DNA sensing is not restricted to the cytoplasm, as IFI16 has also been demonstrated to bind herpesvirus DNA in the nucleus during early stages of infection to induce IFN-? expression [70].
Intriguingly, following detection of viral DNA, IFI16 and the additional ALR AIM2 form oligomeric, multi-protein complexes known as inflammasomes [76,78,79,81,82]. In the cytoplasm, these inflammasomes recruit and activate caspase-1, which, in turn, processes the pro-inflammatory cytokines pro-IL-1? and pro-IL-18 to their secreted, biologically active forms. Until recently, the underlying mechanisms regulating these localization-dependent innate immune functions of IFI16 were not well-understood.
Partly mediated by the HAT p300, acetylation of Lys99 and Lys128 within the nuclear localization signal (NLS) promotes cytoplasmic retention of IFI16, whereas HDAC activity promotes its nuclear import.
Nuclear localization of IFI16 was shown to be essential for recognition of nuclear herpesviral DNA during infection [70,76,77], indicating that HDACs may play a critical role in IFI16-mediated DNA sensing. Thus, modification by acetylation provides a means for expanding the range of IFI16-mediated immuno-surveillance of double-stranded DNA viruses and may function as a toggle for additional localization-dependent functions (Figure 2). Observations of the multiple patterns of IFI16 behavior during viral infection suggest that this protein may have varied functions in immune response.
While acetylation of IFI16 is critical for positioning this DNA sensor in the appropriate cellular compartment prior to infection, the roles of IFI16 acetylation and associated HDAC functions during infection require further investigation.

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