Determination of Interactions between Tegument Proteins of Herpes Simplex Virus Type 1

Vittone, Valerio; Diefenbach, Eve; Triffett, Damian; Douglas, Mark W.; Cunningham, Anthony L.; Diefenbach, Russell J.

doi:10.1128/jvi.79.15.9566-9571.2005

Cited by 186 publications

(237 citation statements)

References 43 publications

(63 reference statements)

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“…The amino-terminal half of VP1/2 includes binding sites for the VP16 and pUL37 tegument proteins, which is consistent with structural incorporation of the fragment into viral particles by coassembly with the tegument and envelope components of virions (31,88). In contrast, the carboxyl-terminal isoform lacks these sites but includes a binding site for the pUL25 capsid protein (16,56).…”

Section: Discussionsupporting

confidence: 52%

Nuclear Egress of Pseudorabies Virus Capsids Is Enhanced by a Subspecies of the Large Tegument Protein That Is Lost upon Cytoplasmic Maturation

Leelawong

Lee

Smith

2012

J Virol

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Herpesviruses morphogenesis occurs stepwise both temporally and spatially, beginning in the nucleus and concluding with the emergence of an extracellular virion. The mechanisms by which these viruses interact with and penetrate the nuclear envelope and subsequent compartments of the secretory pathway remain poorly defined. In this report, a conserved viral protein (VP1/2; pUL36) that directs cytoplasmic stages of egress is identified to have multiple isoforms. Of these, a novel truncated VP1/2 species translocates to the nucleus and assists the transfer of DNA-containing capsids to the cytoplasm. The capsids are handed off to full-length VP1/2, which replaces the nuclear isoform on the capsids and is required for the final cytoplasmic stages of viral particle maturation. These results document that distinct VP1/2 protein species serve as effectors of nuclear and cytoplasmic egress.

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Section: Discussionsupporting

confidence: 52%

Nuclear Egress of Pseudorabies Virus Capsids Is Enhanced by a Subspecies of the Large Tegument Protein That Is Lost upon Cytoplasmic Maturation

Leelawong

Lee

Smith

2012

J Virol

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“…The latter point was debated because the unique portal vertex lacks the major capsid protein, VP5, which is juxtaposed to pUL36 in reconstructions (3,51). The pUL37 tegument protein is a binding partner of pUL36 and possessed properties indistinguishable from pUL25 and pUL36 (52,53).…”

Section: Discussionmentioning

confidence: 99%

Differential protein partitioning within the herpesvirus tegument and envelope underlies a complex and variable virion architecture

Bohannon

Jun

Gross

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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The herpesvirus virion is a multilayered structure consisting of a DNA-filled capsid, tegument, and envelope. Detailed reconstructions of the capsid are possible based on its icosahedral symmetry, but the surrounding tegument and envelope layers lack regular architecture. To circumvent limitations of symmetry-based ultrastructural reconstruction methods, a fluorescence approach was developed using single-particle imaging combined with displacement measurements at nanoscale resolution. An analysis of 11 tegument and envelope proteins defined the composition and plasticity of symmetric and asymmetric elements of the virion architecture. The resulting virion protein map ascribes molecular composition to density profiles previously acquired by traditional ultrastructural methods, and provides a way forward to examine the dynamics of the virion architecture during infection.pseudorabies | virus | heterogeneity | asymmetry | point-spread function H erpesviruses are responsible for a broad range of diseases in humans and other animals. The herpesvirus virion consists of four components: (i) the linear dsDNA genome, (ii) a 125-nm diameter T = 16 icosahedral capsid, (iii) a tegument consisting of more than 20 proteins that surround the capsid, and (iv) a lipid bilayer envelope studded with viral glycoproteins. The fully assembled particle is ∼200-250 nm in diameter and is referred to as the heavy particle (H-particle) (1). The capsid has been solved to 8.5 Å resolution and a fraction of the tegument that is symmetrically bound to the capsid surface has been solved to 20 Å resolution by cryo-electron microscopy (cryo-EM) reconstruction (2-4). The detailed resolution afforded by cryo-EM results from the averaging of many particles that are aligned in silico, based on icosahedral symmetry. However, such studies provide an incomplete picture of herpesvirus virions because unlike some smaller enveloped viruses that project icosahedral symmetry into the envelope proteins, the herpesvirus envelope, and the majority of the tegument mass lack radial symmetry and are not "seen" by cryo-EM (5-7). Our understanding of these variable structural layers predominantly comes from single-particle imaging methods that do not use symmetry-based averaging. In particular, cryo-electron tomography (cryo-ET) has provided insight into the general structure of the outer virion layers, but has not yielded sufficient detail to resolve the organization of the constituent protein components (8).Extracellular herpes virions are metastable structures that are triggered by interactions between virion membrane surface proteins and corresponding receptors on the cell, culminating in membrane fusion (9). Although tegument proteins are critical for postfusion steps in nuclear delivery (10-14), their perceived role before cell entry has been as rigid structural elements that bridge the capsid shell to the tails of envelope membrane proteins (15, 16). However, recent evidence indicates that the tegument may reorganize before membrane fusion (17)(18)(19). A de...

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“…It is widely speculated that herpesvirus tegument proteins mediate the delivery of genome-containing capsids to the nuclear pore complex and perhaps the release of the viral DNA into the nucleus. In the alphaherpesviruses, there is accumulating evidence that the homologs of HCMV UL47 and UL48 (termed UL37 and UL36 [VP1/2], respectively) do indeed interact with each other and with capsids (36,93,193) and help transport those capsids along microtubules to the nucleus (112,205). Further evidence that the HCMV UL47/UL48 complex may be analogous to the alphaherpesvirus UL37/UL36 complex is the similar phenotypes of HCMV UL47 and HSV-1 UL36 mutants described above as well as the observations that HSV-1 UL36 is also a deubiquitinating protease that appears to play a role in viral egress (43,87).…”

Section: Discussionmentioning

confidence: 99%

Tegument Proteins of Human Cytomegalovirus

Kalejta

2008

Microbiol Mol Biol Rev

159

142

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SUMMARY Human cytomegalovirus (HCMV) is a common, medically relevant human herpesvirus. The tegument layer of herpesvirus virions lies between the genome-containing capsids and the viral envelope. Proteins within the tegument layer of herpesviruses are released into the cell upon entry when the viral envelope fuses with the cell membrane. These proteins are fully formed and active and control viral entry, gene expression, and immune evasion. Most tegument proteins accumulate to high levels during later stages of infection, when they direct the assembly and egress of progeny virions. Thus, viral tegument proteins play critical roles at the very earliest and very last steps of the HCMV lytic replication cycle. This review summarizes HCMV tegument composition and structure as well as the known and speculated functions of viral tegument proteins. Important directions for future investigation and the challenges that lie ahead are identified and discussed.

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Determination of Interactions between Tegument Proteins of Herpes Simplex Virus Type 1

Cited by 186 publications

References 43 publications

Nuclear Egress of Pseudorabies Virus Capsids Is Enhanced by a Subspecies of the Large Tegument Protein That Is Lost upon Cytoplasmic Maturation

Nuclear Egress of Pseudorabies Virus Capsids Is Enhanced by a Subspecies of the Large Tegument Protein That Is Lost upon Cytoplasmic Maturation

Differential protein partitioning within the herpesvirus tegument and envelope underlies a complex and variable virion architecture

Tegument Proteins of Human Cytomegalovirus

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