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Besides, the P protein can work as a chaperone, preventing the interaction of the newly synthesized unassembled N protein with the viral RNA, during the encapsidation process of the new hRSV virions in infected cells. On the other hand, the L gene contains a highly conserved sequence that encodes for a 2, amino acid long protein that works as the major catalytic subunit of the RNA-dependent RNA polymerase RdRp complex Fix et al.

Also, the M and the M proteins participate and regulate the hRSV transcription and replication processes. While the M along with the P protein regulate the transcription of mRNAs, contributing to the processivity of the L-polymerase; the M protein mediates the transition from transcription to replication Bermingham and Collins, ; Collins et al. Recently, it was shown that the M is located between the ribonucleoprotein complex and the M protein in the viral particle Kiss et al.

The F protein is a transmembrane protein composed of amino acids McLellan et al. Further, the F protein promotes viral fusion to the host cell membrane and formation of epithelial cell-cell syncytium in the infected airway tissue Openshaw and Tregoning, Such function has been previously suggested through the binding of two specific inhibitors of hRSV F protein CL and RFI , herein preventing the entry and fusion of the virus to the Vero cells Razinkov et al.

Another study, in which a mutant hRSV strain, lacking the glycoprotein G and SH genes, was studied and showed that the F protein favors the post-attachment rate entry in the Hep-2 cells. Furthermore, it has also been reported that the F protein interacts with nucleolin, an ubiquitous host receptor Losfeld et al. Specifically, co-immunoprecipitation assays, using human airway epithelial cell lysates, showed that the nucleolin interacted with the F protein Tayyari et al.

The requirement of this receptor for the entry of hRSV to cells was demonstrated by applying a treatment with an anti-nucleolin antibody, which caused a poor co-localization of the virus on the cell surface and decreased hRSV infection Tayyari et al. Recently, it was found that the hRSV entry is mediated by the Rab5 macropinosomes, since Rab5-deficient HeLa cells displayed lower levels of hRSV infection, as compared to wild type cells Tayyari et al. Further, such hRSV entry mechanism was demonstrated to be pH, clathrin and dynamin independent Tayyari et al.

Moreover, it was shown that hRSV transient macropinocytosis requires two cleavages of the F protein Krzyzaniak et al.

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Nevertheless, this notion is at variance with a previous study, proposing that the hRSV entry takes place due to a clathrin-mediated endocytosis Kolokoltsov et al. Moreover, a soluble form of the G protein, lacking the cytoplasmatic and transmembrane domains, has been described to work as a decoy for neutralizing antibodies, thereby avoiding the antiviral response of the host Bukreyev et al.

Additionally, the G protein, due to its sequence diversity, has been employed as a molecular marker to discriminate between the hRSV subtypes A and B Anderson et al. Importantly, the G gene encodes for a viral transmembrane protein that is important for the hRSV attachment to the host cell Levine et al. In fact, the attachment function of the G protein was first identified in HeLa cell monolayers Levine et al. These cells were treated with anti-G and then challenged with a radiolabeled hRSV. As a result, an inhibition of viral particle attachment to the HeLa cells was observed Levine et al.

Initially, it was thought that the G protein binds to the heparan sulfate on the extracellular matrix of the host cells Feldman et al. However, a study in human airway epithelium HAE showed that CX3R1, a receptor on ciliated cells, is pivotal for the G protein-mediated attachment of viral particles Johnson et al. Indeed, a decreased of hRSV infection was observed with the neutralization of CX3R1 by using two specific monoclonal antibodies Johnson et al. The molecular explanation for this specific attachment of the virus with CX3R1, derives from the similarity of the G protein to CX3CL1, a chemokine produced by immune cells, such as macrophages and dendritic cells Papadopoulos et al.

The sequence similarity between the G glycoprotein and the CX3CL1 molecule locates at the chemokine-like motif, composed of 4 amino acids, at the positions — of the G protein conserved region Tripp et al. The SH glycoprotein is neither required for the entry to the host cells nor needed for viral RNA replication Bukreyev et al. However, several studies that evaluated mutant hRSV strains that lack the SH gene, have shown an attenuation in the virulence Karron et al.

Specifically, these studies demonstrate that SH protein has an important role in hRSV infection, since SH prolongs the cellular life, allowing a continuous virion production. Those regions are suggested to be important channels for hRSV pathogenesis. Thereby, it may be a mechanism to inhibit ligand-mediated apoptosis in the hRSV-infected cells.

Virology Lectures 2017 #13: Intrinsic and Innate Defenses

Interestingly, an interaction between the F protein and the TLR-4 activate this receptor, herein initiating an antiviral immune response Rallabhandi et al. Furthermore, it has been reported that the NS1 protein co-localizes with a critical molecule of the type I IFN pathway, the mitochondrial signaling protein MAVS , thus inhibiting the phosphorylation of the interferon regulatory factor 3 IRF-3 Boyapalle et al. This notion is supported by previous studies showing that NS1 and NS2 were involved in the inhibition of cell apoptosis in the early stages of the hRSV infection Bitko et al.

Thus, through the action of NS proteins, hRSV can inhibit apoptosis to persist for longer periods in the host and avoid the innate immune response. Additionally, it has recently been shown that both the NS1 and NS2 proteins induce the proteosomal degradation of the signal transducer and activator of transcription 2 STAT2 Whelan et al.

As a result, the host antiviral response mediated by the type IFN I pathway is largely impaired, as well as viral clearance Lo et al. The capacity of hRSV to inhibit this process is likely to contribute to the frequent re-infections caused by hRSV throughout life. Another important protein that affects the ability of the innate immune response to recognize and respond to an hRSV infection is the G protein, specifically a CX3C motif present in this protein Chirkova et al. Thus, the G protein of hRSV also contributes to impairing the host immune response and promotes viral dissemination.

Also, the hRSV-infected cells express caspase 1, a pivotal element in the inflammasome activation Triantafilou et al. Taken together, these data suggest that hRSV SH protein is involved in the assembly of ion channels required for the inflammasome activation Gan et al. However, additional research is needed to elucidate the mechanisms employed by the SH protein to impair the proper function of the host immune system. Antigen-presenting cells APCs play an essential role during the infection, as these cells can present peptide-, lipid-, and vitamin B precursor-based antigens Ags in the context of the major histocompatibility complex MHC or MHC-like molecules, respectively Beckman et al.

At the interface, between pMHC complexes and the T cell receptor, there are three hyper variable loops, termed complementarity-determining regions CDRs that make contact with antigens Hughes et al. Effective interaction between TCR and pMHC molecules triggers a tyrosine phosphorylation cascade inside of the T-cell membrane, as well the activation of multiple signaling pathways Janeway et al. The adaptive immune response complex processes, such as the T cell proliferation, require of the TCR engagement and triggering of the respective signaling cascades, which occur within minutes or hours.

However, the sustained TCR engagement with its cognate antigen that takes place is constrained by many barriers. Different studies related to the interaction between pMHCs with TCRs have revealed the formation of a specialized supra molecular structure, termed the immunological synapse IS. This process triggers the rearrangement of a variety of receptor-ligand pairs. This interaction facilitates cytoskeletal movements that ultimately can position peripheral TCRs close to their cognates ligands.

As the assembly of the IS is a pivotal requirement for the establishment of proper T-cell responses and the development of the T-cell memory, many pathogens such as viruses have developed virulence mechanisms to impair the assembly of the IS and the initiation of the adaptive immunity Muller et al. However, these APCs are impaired in their ability to induce T cell activation despite the fact that these cells present either allo- cognate or superantigens to T lymphocytes Gonzalez et al. These results suggest that the NS genes modulate the maturation of DCs, reduce antigen presentation and the T cell activation, impairing key components of the host immune response against hRSV infection.

Thus, the impairment of the T cell function by hRSV infection seems to be a process that requires cell-to-cell contact. We have also recently found that the hRSV-N could be involved in inhibiting T-cell activation during infection Cespedes et al. As a general point, inhibition of the IS assembly by the action of the N protein, observed in this work, was in part attributable to diminished TCR signaling and pMHC clustering at the T-cell- bilayer interface.

Since the soluble N protein colocalizes with the TCR, it was hypothesized that hydrophobic residues within the N protein could transiently interact with the phospholipid bilayer after reaching the membrane of infected cells. In this sense, this study also demonstrated that N-protein, which is associated with viral RNA, could be expressed on the surface of viral particles as an early event 1 h post-infection pi.

Importantly, the results obtained also suggest that virus attachment and virus-cell fusion to target cells would be sufficient to deliver the N protein on the APCs surface to impair the IS Cespedes et al. However, the specific mechanisms accounting for the transport of the N protein to the cell surface are not well-understood. Nevertheless, we suggest that the N protein could interact with the Golgi apparatus or lysosomal membranes in the cytosol of infected cells Figure 2.

These notions are supported by the observations that at 24 h pi, a time point in which infected cells expressed mostly soluble N-protein Fearns et al. Further, it was shown that treatment with Brefeldin-A, an inhibitor of protein transport from the endoplasmic reticulum to the Golgi apparatus Klausner et al.

Therefore, both trans-Golgi and lysosomal exocytic pathway could be involved in the transport of the N protein to the cell surface Cespedes et al. Based on primary amino acidic sequence analysis, we propose that a hydrophobic-rich residue region of the hRSV N could serve to anchor the N protein on the APC surface membrane inset. HRSV is one of the major respiratory pathogens causing a major health burden worldwide. This virus can produce several reinfections throughout life even can leave sequelae, such as asthma and respiratory allergies.

Research on hRSV has taken more than five decades, however, up to date, there are no licensed vaccines available to combat this virus. Currently, only an expensive prophylactic treatment is available based on the administration of specific monoclonal antibodies against the F protein e. HRSV has co-evolved with humans during years and as a result, different hRSV genes are considered as virulence factors, which contribute to hRSV survival and dissemination in the host.

Host Shutoff in IAV: Table 3 Host shutoff mechanisms in influenza A virus. Conflicts of Interest The authors declare no conflict of interest. The herpes simplex virus 1 virion host shutoff protein enhances translation of viral late mRNAs by preventing mRNA overload. Innate immune sensing and signaling of cytosolic nucleic acids.

The interferons and their receptors—Distribution and regulation. The interferon response circuit: Induction and suppression by pathogenic viruses. Host shutoff during productive Epstein-Barr virus infection is mediated by BGLF5 and may contribute to immune evasion.

Herpes simplex virus mutants defective in the virion-associated shutoff of host polypeptide synthesis and exhibiting abnormal synthesis of alpha immediate early viral polypeptides. Herpes simplex virus-infected cells contain a function s that destabilizes both host and viral mRNAs.

Host shutoff is a conserved phenotype of gammaherpesvirus infection and is orchestrated exclusively from the cytoplasm. Functional analysis of virion host shutoff protein of pseudorabies virus. The herpes simplex virus vhs protein induces endoribonucleolytic cleavage of target RNAs in cell extracts. Genetic and biochemical evidence that vhs is a nuclease. Degradation of cellular mRNAs induced by a virion-associated factor during herpes simplex virus infection of Vero cells. Effects of herpes simplex virus on mRNA stability.

Early virion-associated suppression of cellular protein synthesis by herpes simplex virus is accompanied by inactivation of mRNA. A mutant of herpes simplex virus type 1 exhibits increased stability of immediate-early alpha mRNAs. Control of mRNA stability by the virion host shutoff function of herpes simplex virus. Selective ablation of virion host shutoff protein RNase activity attenuates herpes simplex virus 2 in mice. Role of the virion host shutoff vhs of herpes simplex virus type 1 in latency and pathogenesis.

Herpes simplex virus virion host shutoff vhs activity alters periocular disease in mice. Pathogenesis of herpes simplex virus type 2 virion host shutoff vhs mutants. Herpes simplex virus virion host shutoff attenuates establishment of the antiviral state. Herpes simplex virus 2 virion host shutoff protein interferes with type I interferon production and responsiveness. Insights into the molecular mechanisms underlying DNase activity and host shutoff.

Insight from molecular modeling and phylogenetic analysis. Coordinated destruction of cellular messages in translation complexes by the gammaherpesvirus host shutoff factor and the mammalian exonuclease Xrn1. Global mRNA degradation during lytic gammaherpesvirus infection contributes to establishment of viral latency. Gammaherpesviral gene expression and virion composition are broadly controlled by accelerated mRNA degradation. Silencing the shutoff protein of Epstein-Barr virus in productively infected B cells points to innate targets for immune evasion.

A common strategy for host RNA degradation by divergent viruses. Mutations that affect translation of an mRNA influence the sites at which it is cleaved by the HSV virion host shutoff vhs protein. The UL41 protein of herpes simplex virus mediates selective stabilization or degradation of cellular mRNAs. Tristetraprolin recruits the herpes simplex virion host shutoff RNase to AU-rich elements in stress response mRNAs to enable their cleavage.

Interaction between a putative viral nuclease and a cellular translation factor. The virion host shutoff endonuclease UL41 of herpes simplex virus interacts with the cellular cap-binding complex eIF4F. The vhs1 mutant form of herpes simplex virus virion host shutoff protein retains significant internal ribosome entry site-directed RNA cleavage activity. A matter of survival. Networks controlling mRNA decay in the immune system. The nuclear-cytoplasmic shuttling of virion host shutoff RNase is enabled by pUL47 and an Embedded nuclear export signal and defines the sites of degradation of AU-rich and stable cellular mRNAs.

Transcriptome-wide cleavage site mapping on cellular mRNAs reveals features underlying sequence-specific cleavage by the viral ribonuclease SOX. Deep sequencing reveals direct targets of gammaherpesvirus-induced mRNA decay and suggests that multiple mechanisms govern cellular transcript escape. Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs. A single amino acid substitution in herpes simplex virus type 1 VP16 inhibits binding to the virion host shutoff protein and is incompatible with virus growth. Replication-competent herpes simplex virus 1 isolates selected from cells transfected with a bacterial artificial chromosome DNA lacking only the UL49 gene vary with respect to the defect in the UL41 gene encoding host shutoff RNase.

KSHV and the pathogenesis of Kaposi sarcoma: Listening to human biology and medicine. Human herpesvirus 8-associated neoplasms: The roles of viral replication and antiviral treatment. A ribonucleoprotein complex protects the interleukin-6 mRNA from degradation by distinct herpesviral endonucleases. Herpes simplex virus eliminates host mitochondrial DNA. Elimination of mitochondrial DNA is not required for herpes simplex virus 1 replication.

The product of a 1. Herpes simplex virus UL The product of the UL Mitochondrial DNA stress primes the antiviral innate immune response. Aberrant herpesvirus-induced polyadenylation correlates with cellular messenger RNA destruction. Nuclear import of cytoplasmic poly A binding protein restricts gene expression via hyperadenylation and nuclear retention of mRNA. The human poly A -binding protein 1 shuttles between the nucleus and the cytoplasm.

Expression of poly A -binding protein is upregulated during recovery from heat shock in HeLa cells. Poly A -binding protein 1 partially relocalizes to the nucleus during herpes simplex virus type 1 infection in an ICPindependent manner and does not inhibit virus replication. Classical nuclear localization signals: Influenza A virus host shutoff disables antiviral stress-induced translation arrest. Viral nucleases induce an mRNA degradation-transcription feedback loop in mammalian cells. The herpes simplex virus 1 vhs protein enhances translation of viral true late mRNAs and virus production in a cell type-dependent manner.

The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formation. The Tao of RNA triage. P bodies, stress granules, and viral life cycles. Herpes simplex virus 2 infection impacts stress granule accumulation. Host transcript accumulation during lytic KSHV infection reveals several classes of host responses.

The many roles of the regulatory protein ICP27 during herpes simplex virus infection. The herpes simplex virus regulatory protein ICP27 contributes to the decrease in cellular mRNA levels during infection. Herpes simplex virus inhibits host cell splicing, and regulatory protein ICP27 is required for this effect. Splicing is required for rapid and efficient mRNA export in metazoans. Splicing inhibition at the level of spliceosome assembly in the presence of herpes simplex virus protein ICP Herpes simplex virus IE63 ICP27 protein interacts with spliceosome-associated protein and inhibits splicing prior to the first catalytic step.

Sorting out the complexity of SR protein functions. U5 tri-snRNP to the spliceosome. Both hyper- and hypophosphorylation inhibit splicing. Widespread disruption of host transcription termination in HSV-1 infection. Ribonucleic acid synthesis in cells infected with herpes simplex virus I. Patterns of ribonucleic acid synthesis in productively infected cells. Infection by herpes simplex virus 1 causes near-complete loss of RNA polymerase II occupancy on the host cell genome.

RNA polymerase II is aberrantly phosphorylated and localized to viral replication compartments following herpes simplex virus infection. Herpes simplex virus type 1 infection leads to loss of serine-2 phosphorylation on the carboxyl-terminal domain of RNA polymerase II. ICP27 interacts with the C -terminal domain of RNA polymerase II and facilitates its recruitment to herpes simplex virus 1 transcription sites, where it undergoes proteasomal degradation during infection.

The carboxyl-terminal domain of RNA polymerase II is phosphorylated by a complex containing CDK9 and infected-cell protein 22 of herpes simplex virus 1. Control of inducible gene expression by signal-dependent transcriptional elongation. Molecular mechanisms enhancing the proteome of influenza A viruses: An overview of recently discovered proteins. Inhibition of host protein synthesis and degradation of cellular mRNAs during infection by influenza and herpes simplex virus. Functions of the influenza A virus NS1 protein in antiviral defense.

The multifunctional NS1 protein of influenza A viruses. Transfectant influenza A viruses with long deletions in the NS1 protein grow efficiently in Vero cells. Influenza A virus lacking the NS1 gene replicates in interferon-deficient systems. Viral strategies to arrest host mRNA nuclear export. Influenza virus targets the mRNA export machinery and the nuclear pore complex. Inhibition of pyrimidine synthesis reverses viral virulence factor-mediated block of mRNA nuclear export.

Biogenesis, assembly, and export of viral messenger ribonucleoproteins in the influenza A virus infected cell. The H5N1 influenza virus NS genes selected after enhance virus replication in mammalian cells. Multiple anti-interferon actions of the influenza A virus NS1 protein. Structural basis for suppression of a host antiviral response by influenza A virus. The virulence of H5N1 influenza viruses in the mouse model is increased by correcting a defect in their NS1 proteins. Influenza virus infection causes specific degradation of the largest subunit of cellular RNA polymerase II. Mechanisms and functional implications of the degradation of host RNA polymerase II in influenza virus infected cells.

The role of the influenza virus RNA polymerase in host shut-off. Degradation of cellular mRNA during influenza virus infection: HCMV -induced alterations to the cellular splicing machinery apparently ensures the continued production of the unspliced transcript encoding pUL37x1 throughout infection Su et al. Presence of functional antiapoptotic genes in HCMV strains. The fact that UL 37x1-containing gene products provide antiapoptotic activity emerged from transient expression of viral DNA fragments and functional analyses of pUL37x1, gpUL37 and gpUL37M clones in a cell death suppression assay Goldmacher et al.

Rather this, protein is composed of an amino terminal region, aa 5—34, that is important for localization to mitochondria and a carboxyl terminal region, aa —, that is critical for anti-apoptotic activity Hayajneh et al. The regions of highest sequence conservation are coincident with regions defined by mutational studies to be required for vMIA activity McCormick et al.

Thus, vMIA is dispensable unless other mutations are present which render the virus dependent on the gene to prevent apoptosis. Consistent with this conclusion and in contrast to the caspase-dependent cell death noted for strains that require vMIA, premature death in Towne var ATCC mutant virus is caspase-independent McCormick et al. This betaherpesvirus-conserved anti-apoptotic gene product is dispensable for HCMV replication in cultured fibroblasts and is mutated in many common laboratory strains Patterson and Shenk, ; Skaletskaya et al.

Evidence that UL 36 encodes the antiapoptotic protein vICA first emerged from transient expression of viral DNA fragments in a cell death suppression assay Skaletskaya et al. Mutants of the MCMV homologue M36 show a reduced growth phenotype in macrophages IC, JA1, and peritoneal exudate cells but not in fibroblasts or endothelial cells, but this behavior does not appear to extend to the HCMV gene product Dunn et al.

M36 mutant infected cells are, however, more susceptible to induction of apoptosis by the Fas pathway similar to HCMV viruses defective in UL 36 Skaletskaya et al. UL36 homologs and vICA function are widely conserved among betaherpesviruses and sequence conservation includes regions outside the boundaries of the US family domains McCormick et al. Ribonucleotide reductases convert ribonucleoside diphosphates to deoxyribonucleoside diphosphates and are generally important for DNA synthesis and repair. Insertional mutants of M45 grow similar to wild-type viruses in cultured fibroblasts, bone marrow stromal cells, and hepatocytes but fail to grow in either endothelial cells or macrophages Brune et al.

Cell to cell spread is thus severely restricted. The alphaherpesvirus HSV -2 RR 1 subunit prevents cell death upstream of caspase 8 activation due to an amino-terminal extention relative to other RR 1 homologs Langelier et al. It is possible that M45 has preserved such an antiapoptotic function, although there is little sequence similarity to guide how the two may be related.

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Cell-type restricted growth and induced apoptosis are not observed in HCMV UL 45 mutants, which grow poorly and are less efficient at cell-to-cell spread Patrone et al. MCMV mutant defective in m41 prematurely kills cells and replicates to reduced levels compared to parental virus Brune et al. Caspase inhibition reduces but does not eliminate cell death, suggesting that apoptosis may underlie the process.

Expression of epitope-tagged m41 during viral infection shows localization to Golgi. The mechanism of protection remains to be elucidated. Importantly, fibroblasts constitutively expressing IE 1 p72 that have been used to complement growth of IE 1 p72 mutant viruses do not exhibit any obvious altered cell cycle progression or susceptibility to apoptosis. In transient assays, a genomic clone including IE 1 p72 and IE 2 p86 rescues a temperature sensitive derivative of TAF II mutant cells ts 13 from transcriptional repression and apoptosis but not cell cycle arrest Lukac et al.

IE 2 p86 but not IE 1 p72 protects from overexpression of p53 in smooth muscle cells Tanaka et al. These data may suggest that any potential protective role includes both an induction-specific and a cell-type specific component. Although the viral factors required for the down-regulation have not been identified, either virus seems to employ a post-transcriptional mechanism. Infections by other betaherpesviruses maintain the Fas receptor available for activation. UL encodes a glycoprotein consisting of a leader peptide, cysteine-rich domains CRD , membrane extension region, transmembrane domain, and a short cytoplasmic tail.

UL exhibits dramatic strain-to-strain sequence variability Bale, ; Lurain, , although the protein has highly conserved transmembrane and cytoplasmic domains. The betaherpesviruses all appear to alter cell cycle and to block rather than promote apoptosis during infection. Cytomegaloviruses prevent cellular DNA synthesis whereas roseolaviruses allow continued cellular DNA synthesis during productive infection, although cell division is blocked in all of these viruses.

While none of the betaherpesviruses has been implicated in malignancy, such an impact on the host cell has raised interest of persistent betaherpesvirus infection in certain chronic diseases. These viruses encode a wide variety of functions that modulate the cellular environment, including functions that modulate cell cycle progression and that derail apoptosis induced by either intrinsic or extrinsic mediators. Turn recording back on. National Center for Biotechnology Information , U. Cambridge University Press ; Chapter 21 Viral modulation of the host response to infection A.

Modulation of histone deacetylase activity HCMV replication is stimulated when permissive cells are treated with inhibitors of histone deacetylases Murphy et al. Impact on the host cell cycle Betaherpesvirus genomes are transcribed and replicated within the nucleus, the same cellular compartment that regulates the cell cycle and controls apoptosis following DNA damage or aberrant protooncogene expression.

Suppression of apoptosis Apoptosis is an evolutionarily conserved cellular process that removes cells during infection, development, or homeostasis. Other cell death suppressors Ribonucleotide reductases convert ribonucleoside diphosphates to deoxyribonucleoside diphosphates and are generally important for DNA synthesis and repair. Alteration of extrinsic cell death pathways during infection TNF-R1 surface expression levels decrease following HCMV infection of macrophage or astrocytoma cell lines Baillie et al.

Summary The betaherpesviruses all appear to alter cell cycle and to block rather than promote apoptosis during infection. Major human cytomegalovirus structural protein pp65 ppUL83 prevents interferon response factor 3 activation in the interferon response.

PMC ] [ PubMed: Induction of chromosome aberrations and mitotic arrest by cytomegalovirus in human cells. Human cytomegalovirus induces drug resistance and alteration of programmed cell death by accumulation of deltaN-p73alpha. A novel checkpoint in the Bclregulated apoptotic pathway revealed by murine cytomegalovirus infection of dendritic cells.

Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria. Human cytomegalovirus infection inhibits tumor necrosis factor alpha TNF-alpha signaling by targeting the kilodalton TNF -alpha receptor.


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Adenine nucleotide translocator mediates the mitochondrial membrane permeabilization induced by lonidamine, arsenite and CD Neutrality of the canonical NF -kappaB-dependent pathway for human and murine cytomegalovirus transcription and replication in vitro. Human cytomegalovirus infection leads to accumulation of geminin and inhibition of the licensing of cellular DNA replication.

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Mutant human cytomegalovirus lacking the immediate-early TRS 1 coding region exhibits a late defect. Human cytomegalovirus elicits a coordinated cellular antiviral response via envelope glycoprotein B. Cellular oncogene activation by human cytomegalovirus. Lack of correlation with virus infectivity and immediate early gene expression. Novel activation of gamma-interferon in nonimmune cells during human cytomegalovirus replication. Human cytomegalovirus IE 2 kilodalton protein binds p53 but does not abrogate G1 checkpoint function.

Engagement of the cellular receptor for glycoprotein B of human cytomegalovirus activates the interferon-responsive pathway. UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells. Human cytomegalovirus inhibits cellular DNA synthesis and arrests productively infected cells in late G1.

Human cytomegalovirus infection results in altered Cdk2 subcellular localization. Human cytomegalovirus UL coded pp65 virion protein inhibits antiviral gene expression in infected cells. Altered cellular mRNA levels in human cytomegalovirus-infected fibroblasts: A ribonucleotide reductase homologue of cytomegalovirus and endothelial cell tropism.

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Murine cytomegalovirus m41 open reading frame encodes a Golgi-localized antiapoptotic protein. Interaction between the human cytomegalovirus UL 82 gene product pp71 and hDaxx regulates immediate-early gene expression and viral replication. Human cytomegalovirus stimulates cellular IKK 2 activity and requires the enzyme for productive replication. Human cytomegalovirus TRS 1 and IRS 1 gene products block the double-stranded-RNA-activated host protein shutoff response induced by herpes simplex virus type 1 infection. Role of human cytomegalovirus immediate—early proteins in cell growth control.

Use of interferon in cytomegalovirus infections in man. Complementation of vaccinia virus lacking the double-stranded RNA -binding protein gene E3L by human cytomegalovirus. Up-regulation of Fas ligand expression by human cytomegalovirus immediate-early gene product 2: Receptors and immune sensors: Viral homologs of BCL Activation of the NF -kappaB pathway in human cytomegalovirus-infected cells is necessary for efficient transactivation of the major immediate—early promoter.

Rhesus cytomegalovirus particles prevent activation of interferon regulatory factor 3. Interferon regulatory factor 3 is necessary for induction of antiviral genes during human cytomegalovirus infection. Cytomegalovirus-enhanced induction of chromosome aberrations in human peripheral blood lymphocytes treated with potent genotoxic agents.

Functional profiling of a human cytomegalovirus genome. NF-kappaB activation can mediate inhibition of human cytomegalovirus replication. Viral proteins and the mitochondrial apoptotic checkpoint. Cytokine Growth Factor Rev.