Book contents
- Frontmatter
- Contents
- List of contributors
- Preface
- Part I Introduction: definition and classification of the human herpesviruses
- Part II Basic virology and viral gene effects on host cell functions: alphaherpesviruses
- 5 Genetic comparison of human alphaherpesvirus genomes
- 6 Alphaherpes viral genes and their functions
- 7 Entry of alphaherpesviruses into the cell
- 8 Early events pre-initiation of alphaherpes viral gene expression
- 9 Initiation of transcription and RNA synthesis, processing and transport in HSV and VZV infected cells
- 10 Alphaherpesvirus DNA replication
- 11 Envelopment of HSV nucleocapsids at the inner nuclear membrane
- 12 The egress of alphaherpesviruses from the cell
- 13 The strategy of herpes simplex virus replication and takeover of the host cell
- Part II Basic virology and viral gene effects on host cell functions: betaherpesviruses
- Part II Basic virology and viral gene effects on host cell functions: gammaherpesviruses
- Part III Pathogenesis, clinical disease, host response, and epidemiology: HSV-1 and HSV-2
- Part III Pathogenesis, clinical disease, host response, and epidemiology: VZU
- Part III Pathogenesis, clinical disease, host response, and epidemiology: HCMV
- Part III Pathogenesis, clinical disease, host response, and epidemiology: HHV- 6A, 6B, and 7
- Part III Pathogenesis, clinical disease, host response, and epidemiology: gammaherpesviruses
- Part IV Non-human primate herpesviruses
- Part V Subversion of adaptive immunity
- Part VI Antiviral therapy
- Part VII Vaccines and immunothgerapy
- Part VIII Herpes as therapeutic agents
- Index
- Plate section
- References
13 - The strategy of herpes simplex virus replication and takeover of the host cell
from Part II - Basic virology and viral gene effects on host cell functions: alphaherpesviruses
Published online by Cambridge University Press: 24 December 2009
Book contents
- Frontmatter
- Contents
- List of contributors
- Preface
- Part I Introduction: definition and classification of the human herpesviruses
- Part II Basic virology and viral gene effects on host cell functions: alphaherpesviruses
- 5 Genetic comparison of human alphaherpesvirus genomes
- 6 Alphaherpes viral genes and their functions
- 7 Entry of alphaherpesviruses into the cell
- 8 Early events pre-initiation of alphaherpes viral gene expression
- 9 Initiation of transcription and RNA synthesis, processing and transport in HSV and VZV infected cells
- 10 Alphaherpesvirus DNA replication
- 11 Envelopment of HSV nucleocapsids at the inner nuclear membrane
- 12 The egress of alphaherpesviruses from the cell
- 13 The strategy of herpes simplex virus replication and takeover of the host cell
- Part II Basic virology and viral gene effects on host cell functions: betaherpesviruses
- Part II Basic virology and viral gene effects on host cell functions: gammaherpesviruses
- Part III Pathogenesis, clinical disease, host response, and epidemiology: HSV-1 and HSV-2
- Part III Pathogenesis, clinical disease, host response, and epidemiology: VZU
- Part III Pathogenesis, clinical disease, host response, and epidemiology: HCMV
- Part III Pathogenesis, clinical disease, host response, and epidemiology: HHV- 6A, 6B, and 7
- Part III Pathogenesis, clinical disease, host response, and epidemiology: gammaherpesviruses
- Part IV Non-human primate herpesviruses
- Part V Subversion of adaptive immunity
- Part VI Antiviral therapy
- Part VII Vaccines and immunothgerapy
- Part VIII Herpes as therapeutic agents
- Index
- Plate section
- References
Summary
Introduction
The fundamental mission of all viruses is to replicate and spread, and above all, to persist in the host environment to which they have become adapted. Viruses vary with respect to the mechanisms by which they attain their objectives. This variation is reflected not only in the basic mechanisms of viral entry into cells, synthesis of viral proteins, viral nuclei acid synthesis, virion assembly, and egress but also with respect to the basic strategies by which they preclude the enormous resources of the host cell and of the multicellular organism from totally blocking viral replication. The terminology used: “totally blocking” is appropriate; in essence the evolution of functions encoded in the viral genome reflects a fundamental accommodation between replication and spread as well as persistence in the human population. A replication and spread that kills the host will not permit the survival of the virus. The objective of this chapter is to examine the basic strategies evolved by HSV to replicate in its cellular environment.
Gene content, organization, and fundamental design of the viral genome
Several aspects of the structure, content and function of the viral genome are worthy of note. They are as follows.
(i) We do not know with any degree of certainty the exact number of transcriptional units or proteins encoded by the viral genome. The problem stems from several considerations. […]
- Type
- Chapter
- Information
- Human HerpesvirusesBiology, Therapy, and Immunoprophylaxis, pp. 163 - 174Publisher: Cambridge University PressPrint publication year: 2007
References
, , , and (2000). The disappearance of cyclins A and B and the increase in activity of the G2/M-phase cellular kinase cdc2 in herpes simplex virus 1-infected cells require expression of the α22/Us1.5 and UL13 viral genes. J. Virol., 74, 8–15.CrossRefGoogle Scholar
, , and (2001). cdc2 cyclin-dependent kinase binds and phosphorylates herpes simplex virus 1 UL42 DNA synthesis processivity factor. J. Virol., 75, 10326–10333.CrossRefGoogle Scholar
, , and (2003). Herpes simplex virus 1 activates cdc2 to recruit topoisomerase IIα for post-DNA synthesis expression of late genes. Proc. Natl Acad. Sci. USA, 100, 4825–4830.CrossRefGoogle Scholar
, , , and (2001). Activation of IκB kinase by herpes simplex virus type 1. A novel target for anti-herpetic therapy. J. Biol. Chem., 276, 28759–28766.CrossRefGoogle ScholarPubMed
and (1999). The Herpes simplex virus type 1 regulatory protein ICP27 is required for the prevention of apoptosis in infected human cells. J. Virol., 73, 2803–2813.Google ScholarPubMed
, , and (2003). ARED 2.0: an update of AU-rich element mRNA database. Nucl. Acids Res., 31, 421–423.CrossRefGoogle ScholarPubMed
, , and (1994). Transcriptional analysis of the region of the herpes simplex virus type 1 genome containing the UL8, UL9, and UL10 genes and identification of a novel delayed-early gene product, OBPC. J. Virol., 68, 4251–4261.Google ScholarPubMed
and (2003). Herpes simplex virus protein kinase US3 activates and functionally overlaps protein kinase A to block apoptosis. Proc. Natl Acad. Sci. USA, 101, 9411–9416.CrossRefGoogle Scholar
, , and (2003). The herpes simplex virus 1 US3 protein kinase blocks caspase-dependent double cleavage and activation of the proapoptotic protein BAD. J. Virol., 77, 6567–6573.CrossRefGoogle ScholarPubMed
(2002). Tristetraprolin and other CCCH tandem zinc-finger proteins in the regulation of mRNA turnover. Biochem. Soc. Trans., 30, 945–952.CrossRefGoogle ScholarPubMed
, , and (2002). Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro. J. Virol., 76, 841–850.CrossRefGoogle ScholarPubMed
, , and (2004). The role of mRNA turnover in the regulation of tristetraprolin expression: evidence for an extracellular signal-regulated kinase-specific, AU-rich element-dependent, autoregulatory pathway. J. Immunol., 172, 7263–7271.CrossRefGoogle ScholarPubMed
and (1996). The promoter and transcriptional unit of a novel herpes simplex virus 1α gene are contained in, and encode a protein in frame with, the open reading frame of the α22 gene. J. Virol., 70, 172–178.Google Scholar
, , and (1998). The herpes simplex virus US11 protein effectively compensates for the γ1 34.5 gene if present before activation of protein kinase R by precluding its phosphorylation and that of the alpha subunit of eukaryotic translation initiation factor 2. J. Virol., 72, 8620–8626.Google Scholar
and (2004). Herpes simplex virus 1 gene products occlude the interferon signaling pathway at multiple sites. J. Virol., 78, 4185–4196.CrossRefGoogle ScholarPubMed
, , , and (2003). Promyleocytic leukemia protein mediates interferon-based anti-herpes simplex virus 1 effects. J. Virol., 77, 7101–7105.CrossRefGoogle Scholar
and (1995). AU-rich elements: characterization and importance in mRNA degradation. Trends Biochem. Sci., 20, 465–470.CrossRefGoogle ScholarPubMed
, , et al., (2001). AU binding proteins recruit the exosome to degrade ARE-containing mRNAs. Cell, 107, 451–464.CrossRefGoogle ScholarPubMed
, , , and (2004). Herpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H. J. Virol., 78, 4684–4699.CrossRefGoogle ScholarPubMed
, , and (2005). 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. J. Virol., 79, 6757–6762.CrossRefGoogle ScholarPubMed
, , , and (2004a). The herpes simplex virus 1 UL41 gene-dependent destabilization of cellular RNAs is selective and may be sequence-specific. Proc. Natl Acad. Sci. USA, 101, 3603–3608.CrossRefGoogle Scholar
, , and (2004b). Herpes simplex virus 1 induces cytoplasmic accumulation of TIA-1/TIAR and both synthesis and cytoplasmic accumulation of tristetraprolin, two cellular proteins that bind and destabilize AU-rich RNAs. J. Virol., 78, 8582–8592.CrossRefGoogle Scholar
, , and (2004c). The UL41 protein of herpes simplex virus mediates selective stabilization or degradation of cellular mRNAs. Proc. Natl Acad. Sci. USA, 101, 18165–18170.CrossRefGoogle Scholar
(2001). DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene, 20, 7266–7273.CrossRefGoogle ScholarPubMed
, , , and (2002). mRNA degradation by the virion host shutoff (Vhs) protein of herpes simplex virus: genetic and biochemical evidence that Vhs is a nuclease. J. Virol., 76, 8560–8571.CrossRefGoogle Scholar
and (1998). Herpes simplex virus 1 induces and blocks apoptosis at multiple steps during infection and protects cells from exogenous inducers in a cell-type-dependent manner. Proc. Natl Acad. Sci. USA, 95, 3931–3936.CrossRefGoogle Scholar
, , and (1999). Herpes simplex virus 1 blocks caspase-3-independent and caspase-dependent pathways to cell death. J. Virol., 73, 3219–3226.Google ScholarPubMed
, , and (2003). NF-κB is required for apoptosis prevention during herpes simplex virus type 1 infection. J. Virol., 77, 7261–7280.CrossRefGoogle ScholarPubMed
, , , , and (2004). Efficient replication by herpes simplex virus type 1 involves activation of the IκB kinase-IκB-p65 pathway. J. Virol., 78, 13582–13590.CrossRefGoogle ScholarPubMed
and (2003). The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a. Proc. Natl Acad. Sci. USA, 100, 8963–8968.CrossRefGoogle ScholarPubMed
, , , and (2005). Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells. Proc. Natl Acad. Sci. USA, 102, 7571–7576.CrossRefGoogle ScholarPubMed
and (2002). Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0. Proc. Natl Acad. Sci. USA, 99, 7889–7894.CrossRefGoogle ScholarPubMed
and (2003). Herpes simplex virus 1 mutant in which the ICP0 HUL-1 E3 ubiquitin ligase site is disrupted stabilizes cdc34 but degrades D-type cyclins and exhibits diminished neurotoxicity. J. Virol., 77, 13194–13202.CrossRefGoogle ScholarPubMed
and (2004). Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1. J. Virol., 78, 2169–2178.CrossRefGoogle ScholarPubMed
, , , and (2002). Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes. Proc. Natl Acad. Sci. USA, 99, 631–636.CrossRefGoogle Scholar
and (1994). The herpes simplex virus regulatory protein ICP27 contributes to the decrease in cellular mRNA levels during infection. J. Virol., 68, 4797–4810.Google ScholarPubMed
, , , , , and (1997a). Suppression of the phenotype of γ1 34.5- herpes simplex virus 1: failure of activated RNA-dependent protein kinase to shut off protein synthesis is associated with a deletion in the domain of the α47 gene. J. Virol., 71, 6049–6054.Google Scholar
, , and (1997b). The γ1 34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1 α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc. Natl Acad. Sci. USA, 94, 843–848.CrossRefGoogle Scholar
, , and (1998). The γ1 34.5 protein of herpes simplex virus 1 has the structural and functional attributes of a protein phosphatase 1 regulatory subunit and is present in a high molecular weight complex with the enzyme in infected cells. J. Biol. Chem., 273, 20737–20743.CrossRefGoogle Scholar
, , , and (1998). Herpes simplex virus type 1 renders infected cells resistant to cytotoxic T-lymphocyte-induced apoptosis. J. Virol., 72, 436–441.Google ScholarPubMed
, , , , , and (1999). Herpes simplex virus inhibits apoptosis through the action of two genes, US5 and US3. J. Virol., 73, 8950–8957.Google ScholarPubMed
, , et al., (2001). HSV and glycoprotein J inhibit caspase activation and apoptosis induced by granzyme B or Fas. J. Immunol., 167, 3928–3935.CrossRefGoogle ScholarPubMed
and (1999). The virion host shutoff function of herpes simplex virus degrades the 5 end of a target mRNA before the 3 end. Virology, 264, 195–204.CrossRefGoogle ScholarPubMed
, , and (1998). Eukaryotic elongation factor 1δ is hyperphosphorylated by the protein kinase encoded by the UL13 gene of herpes simplex virus 1. J. Virol., 72, 1731–1736.Google ScholarPubMed
, , , and (1999). Cellular elongation factor 1 δ is modified in cells infected with representative alpha-, beta-, or gamma-herpesviruses. J. Virol., 73, 4456–4460.Google Scholar
and (1997). Suppression of apoptotic DNA fragmentation in herpes simplex virus type 1-infected cells. J. Virol., 71, 2567–2571.Google ScholarPubMed
, , and (1988). Herpes simplex virus virion host shutoff function. J. Virol., 62, 912–921.Google ScholarPubMed
, , , , , and (1999). Interferons regulate the phenotype of wild-type and mutant herpes simplex viruses in vivo. J. Exp. Med., 189, 663–672.CrossRefGoogle ScholarPubMed
, , , , and (2000). Specific phenotypic restoration of an attenuated virus by knockout of a host resistance gene. Proc. Natl Acad. Sci. USA, 97, 6097–6101.CrossRefGoogle ScholarPubMed
and (1996). The herpes simplex virus major regulatory protein ICP4 blocks apoptosis induced by the virus or by hyperthermia. Proc. Natl Acad. Sci. USA, 93, 9583–9587.CrossRefGoogle ScholarPubMed
, , and (1997a). The herpes simplex virus 1 protein kinase US3 is required for protection from apoptosis induced by the virus. Proc. Natl Acad. Sci. USA, 94, 7891–7896.CrossRefGoogle Scholar
, , , and (1997b). Association of herpes simplex virus regulatory protein ICP22 with transcriptional complexes containing EAP, ICP4, RNA polymerase II, and viral DNA requires posttranslational modification by the UL13 protein kinase. J. Virol., 71, 1133–1139.Google Scholar
, , , , and (1999). ICP22 and the UL13 protein kinase are both required for herpes simplex virus-induced modification of the large subunit of RNA polymerase II. J. Virol., 73, 5593–5604.Google ScholarPubMed
, , and (2001). Requirements for the nuclear-cytoplasmic translocation of infected-cell protein 0 of herpes simplex virus 1. J. Virol., 75, 3832–3840.CrossRefGoogle Scholar
, , and (2002). Overexpression of promyelocytic leukemia protein precludes the dispersal of ND10 structures and has no effect on accumulation of infectious herpes simplex virus 1 or its proteins. J. Virol., 76, 9355–9367.CrossRefGoogle ScholarPubMed
and (1996). A herpesvirus genetic element which affects translation in the absence of the viral GADD34 function. EMBO J., 15, 4759–4766.Google ScholarPubMed
and (2001). The US3 protein kinase of herpes simplex virus 1 mediates the posttranslational modification of BAD and prevents BAD-induced programmed cell death in the absence of other viral proteins. Proc. Natl Acad. Sci. USA, 98, 10410–10415.CrossRefGoogle ScholarPubMed
, , and (2001). The US3 protein kinase blocks apoptosis induced by the d120 mutant of herpes simplex virus 1 at a premitochondrial stage. J. Virol., 75, 5491–5497.CrossRefGoogle Scholar
, , , , , and (2002). Herpes simplex virus type 2 US3 blocks apoptosis induced by sorbitol treatment. Microbes Infect., 4, 707–712.CrossRefGoogle ScholarPubMed
, , , , and (2004). The HSV-1 US3 protein kinase is sufficient to block apoptosis induced by overexpression of a variety of Bcl-2 family members. Virology, 319, 212–224.CrossRefGoogle ScholarPubMed
and (1999). Functional anatomy of herpes simplex virus 1 overlapping genes encoding infected-cell protein 22 and US1.5 protein. J. Virol., 73, 4305–4315.Google ScholarPubMed
, , et al., (1998). Herpes simplex type 1 induction of persistent NF-κB nuclear translocation increases the efficiency of virus replication. Virology, 247, 212–222.CrossRefGoogle Scholar
, , and (2004). RNA degradation induced by the herpes simplex virus vhs protein proceeds 5′ to 3′ in vitro. J. Virol., 78, 13391–13394.CrossRefGoogle ScholarPubMed
, , , , and (2002). The Herpes Simplex virus type 2 R1 protein kinase (ICP10 PK) blocks apoptosis in hippocampal neurons, involving activation of the MEK/MAPK survival pathway. J. Virol., 76, 1435–1449.CrossRefGoogle ScholarPubMed
, , and (2003) Herpes simplex virus 1 gene expression is accelerated by inhibitors of histone deacetylases in rabbit skin cells infected with a mutant carrying a cDNA copy of the infected-cell protein no. 0. J. Virol., 77, 12671–12678.CrossRefGoogle ScholarPubMed
and (1992). The UL13 gene of herpes simplex virus 1 encodes the functions for posttranslational processing associated with phosphorylation of the regulatory protein 22. Proc. Natl Acad. Sci. USA, 89, 7310–7314.CrossRefGoogle Scholar
, , and (1993) Processing of the herpes simplex virus regulatory protein 22 mediated by the UL13 protein kinase determines the accumulation of a subset of α and γ mRNAs and proteins in infected cells. Proc. Natl Acad. Sci. USA, 90, 6701–6705.CrossRefGoogle ScholarPubMed
and (2001). Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene, 20, 7274–7286.CrossRefGoogle ScholarPubMed
, , , and (1994). RNA polymerase II is aberrantly phosphorylated and localized to viral replication compartments following herpes simplex virus infection. J. Virol., 68, 988–1001.Google ScholarPubMed
, , , , and (1995). Herpes simplex virus immediate-early protein ICP22 is required for viral modification of host RNA polymerase II and establishment of the normal viral transcription program. J. Virol., 69, 5550–5559.Google ScholarPubMed
, , and (1965). Macromolecular synthesis in cells infected with herpes simplex virus. Nature, 206, 374–1375.CrossRefGoogle ScholarPubMed
and (1990). The herpes simplex virus US11 open reading frame encodes a sequence specific RNA-binding protein. J. Virol., 64, 3463–3470.Google ScholarPubMed
(1998). ICP27 mediates HSV RNA export by shuttling through a leucine-rich nuclear export signal and binding viral intronless RNAs through an RGG motif. Genes Dev., 12, 868–879.CrossRefGoogle ScholarPubMed
, , and (2003). NF-κB and virus infection: who controls whom. EMBO J., 22, 2552–2260.CrossRefGoogle ScholarPubMed
, , , , and (2002). Of the three tegument proteins that package mRNA in herpes simplex virions, one (VP22) transports the mRNA to uninfected cells for expression prior to viral infection. Proc. Natl Acad. Sci. USA, 99, 8318–8323.CrossRefGoogle ScholarPubMed
(2002). Might a vanguard of mRNAs prepare cells for the arrival of herpes simplex virus?Proc. Natl Acad. Sci. USA, 99, 8465–8466.CrossRefGoogle ScholarPubMed
, , et al., (1996). Herpes simplex virus type 2 inhibition of Fas ligand expression. J. Virol., 70, 8747–8751.Google ScholarPubMed
, , , , and (1994). Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs. J. Virol., 68, 2339–2346.Google ScholarPubMed
(2004). Herpes simplex virus virion host shutoff protein: immune evasion mediated by a viral RNase?J. Virol., 78, 1063–1068.CrossRefGoogle ScholarPubMed
and (1987). Effects of herpes simplex virus on mRNA stability. J. Virol., 61, 2198–2207.Google ScholarPubMed
and (1966). Polysomes and protein synthesis in cells infected with a DNA virus. Science, 153, 76–78.CrossRefGoogle ScholarPubMed
and (1968). The disaggregation of host polyribosomes in productive and abortive infection with herpes simplex virus. Virology, 32, 678–686.CrossRefGoogle Scholar
, , and (2002). The patterns of accumulation of cellular RNAs in cells infected with a wild-type and a mutant herpes simplex virus 1 lacking the virion host shutoff gene. Proc. Natl Acad. Sci. USA, 99, 17031–17036.CrossRefGoogle Scholar
, , , and (2003a). The stress-inducible immediate-early responsive gene IEX-1 is activated in cells infected with herpes simplex virus 1, but several viral mechanisms, including 3′ degradation of its RNA, preclude expression of the gene. J. Virol., 77, 6178–6187.CrossRefGoogle Scholar
, , , and (2003b). Activation of NF-κB in cells productively infected with HSV-1 depends on activated protein kinase R and plays no apparent role in blocking apoptosis. Proc. Natl Acad. Sci. USA, 100, 12408–12413.CrossRefGoogle Scholar
, , , and (2004a). Cells lacking NF-κB or in which NF-κB is not activated vary with respect to ability to sustain herpes simplex virus 1 replication and are not susceptible to apoptosis induced by a replication-incompetent mutant virus. J. Virol., 78, 11615–11621.CrossRefGoogle Scholar
, , and (2004b). Post-transcriptional processing of cellular RNAs in herpes simplex virus-infected cells. Biochem. Soc. Trans., 32, 697–701.CrossRefGoogle Scholar
, , , and (2003). Pseudorabies virus US3 protein kinase mediates actin stress fiber breakdown. J. Virol., 77, 9074–9080.CrossRefGoogle ScholarPubMed
, , and (2001). The cap-to-tail guide to mRNA turnover. Nat. Rev. Mol. Cell Biol., 2, 237–246.CrossRefGoogle ScholarPubMed
and (2001). The domains of glycoprotein D required to block apoptosis depend on whether glycoprotein D is present in the virions carrying herpes simplex virus 1 genome lacking the gene encoding the glycoprotein. J. Virol., 75, 6166–6172.CrossRefGoogle Scholar
and (2002a). Cation-independent mannose 6-phosphate receptor blocks apoptosis induced by herpes simplex virus 1 mutants lacking glycoprotein D and is likely the target of antiapoptotic activity of the glycoprotein. J. Virol., 76, 6197–6204.CrossRefGoogle Scholar
and (2002b). Truncated forms of glycoprotein D of herpes simplex virus 1 capable of blocking apoptosis and of low-efficiency entry into cells form a heterodimer dependent on the presence of a cysteine located in the shared transmembrane domains. J. Virol., 76, 11469–11475.CrossRefGoogle Scholar
, , , and (2000). Glycoprotein D or J delivered in trans blocks apoptosis in SK-N-SH cells induced by a herpes simplex virus 1 mutant lacking intact genes expressing both glycoproteins. J. Virol., 74, 11782–11791.CrossRefGoogle ScholarPubMed
, , and (1995). Human cytomegalovirus IE1 and IE2 proteins block apoptosis. J. Virol., 69, 7960–7970.Google ScholarPubMed
- 16
- Cited by