The cytoplasmic tail of herpes simplex virus envelope glycoprotein D binds to the tegument protein VP22 and to capsids

I., Jung Hee; Harley, Carol A.; Mukhopadhyay, Aparna; Wilson, Duncan W.

doi:10.1099/vir.0.80444-0

Cited by 65 publications

(72 citation statements)

References 20 publications

(30 reference statements)

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“…A number of studies have begun to shed light on VP22 localization and compartmentalization during virus infection (2, 9, 13-15, 22, 23, 26, 28, 29, 34, 35). VP22 has been reported to interact with membranes in infected cells (3) and, potentially in a related fashion, to bind to the cytoplasmic tail of the glycoprotein gD (4). Interactions between VP22 and glycoproteins E and M have been reported in PRV (19).…”

Section: Discussionmentioning

confidence: 99%

Characterization of VP22 in Herpes Simplex Virus-Infected Cells

Mouzakitis

McLauchlan²,

Barreca

et al. 2005

J Virol

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We examine biochemical characteristics of the herpes simplex virus (HSV) tegument protein VP22 by gel filtration, glycerol sedimentation, and chemical cross-linking experiments and use time course radiolabeling and immunoprecipitation assays to analyze its synthesis and interaction with other infected-cell proteins. VP22 was expressed as a delayed early protein with optimal synthesis requiring DNA replication. In immunoprecipitation assays, VP22 was found in association with several additional proteins including VP16 and a kinase activity likely to be that of UL13. Furthermore, in sizing chromatography experiments, VP22 was present in several higher-order complexes in infected cells. From gel filtration analysis the major form of VP22 migrated with a molecular mass of approximately 160 kDa, consistent with its presence as a tetramer, or a dimer complexed with other proteins, with a fraction of the protein migrating at larger molecular mass. In vitrosynthesized VP22 sedimented in a size range consistent with a mixture of tetramers and dimers. Short N-or C-terminal deletions resulted in migration almost exclusively as dimers, indicating that VP22, in the absence of additional virus-encoded proteins, could form higher-order assemblies, most likely tetramers, but that both N-and C-terminal determinants were required for stabilizing such assemblies. Consistent with this we found that isolated proteins encompassing either the N-terminal or C-terminal region of VP22 sedimented as dimers, and that the purified C-terminal domain could be cross-linked into dimeric structures. These results are discussed with regard to possible virus and host interactions involved in VP22 recruitment into virus particles.

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Section: Discussionmentioning

confidence: 99%

Characterization of VP22 in Herpes Simplex Virus-Infected Cells

Mouzakitis

McLauchlan²,

Barreca

et al. 2005

J Virol

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“…5, it is likely that some components of the capsid-associated inner tegument proteins are assembled inside the host nucleus at or near the nuclear lamina prior to budding through the inner nuclear membrane in the early stage of virion maturation. Our observation of the outer tegument layer conforming to the pleomorphic shape of viral envelope implies that the outer tegument proteins might be packaged into maturing virion particles through interactions with the viral glycoproteins decorated on the trans Golgi membrane (Chi et al 2005;Farnsworth et al 2007;Fuchs et al 2002). As the first to be released into the cellular environment upon infection, outer layer proteins are probably essential viral functional proteins during the early stages of infection.…”

Section: Discussionmentioning

confidence: 99%

Unique structures in a tumor herpesvirus revealed by cryo-electron tomography and microscopy

Dai

Jia

Bortz

et al. 2008

Journal of Structural Biology

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Gammaherpesviruses, including the human pathogens Epstein-Barr virus and Kaposi's sarcomaassociated herpesvirus, are causative agents of lymphomas and other malignancies. The structural characterization of these viruses has been limited due to difficulties in obtaining adequate amount of virion particles. Here we report the first three-dimensional structural characterization of a whole gammaherpesvirus virion by an emerging integrated approach of the technique of cryo-electron tomography combined with single-particle cryo-electron microscopy, using murine gammaherpesvirus-68 (MHV-68) as a model system. We found that the MHV-68 virion consists of distinctive envelope and tegument compartments, and a highly conserved nucleocapsid. Two layers of tegument are identified: an inner tegument layer tethered to the underlying capsid and an outer, flexible tegument layer conforming to the overlying, pleomorphic envelope, consistent with the sequential viral tegumentation process inside host cells. Surprisingly, comparison of the MHV-68 virion and capsid reconstructions shows that the interactions between the capsid and inner tegument proteins are completely different from those observed in alpha and betaherpesviruses. These observations support the notion that inner layer tegument across different subfamilies of herpesviruses have evolved significantly to confer specific characteristics related to viral-host interactions, in contrast to a highly conserved capsid for genome encapsidation and protection.

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“…Attachments of the innermost layer of mature tegument to capsid pentons have been observed, suggesting that they serve to anchor the tegument layer to the nucleocapsid (51). The means of attachment of the tegument to the virion envelope is uncertain, although interactions between some tegument proteins and some glycoproteins have been detected (8,12,17,21). …”

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confidence: 99%

Electron Tomography of Nascent Herpes Simplex Virus Virions

Baines

Hsieh

Wills

et al. 2007

J Virol

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Electron microscopic studies have shown that cells infected with herpesviruses contain four types of capsids. Procapsids, believed to represent the progenitor of other capsid types, contain a porous outer shell that is roughly spherical, surrounding an inner protein shell or scaffold (23, 33). Type A capsids consist mostly of a 125-nm-diameter protein shell that comprises 12 vertices of fivefold symmetry (termed pentons) and 20 identical planar facets (53). Collectively, the planar facets are composed of 150 sixfold symmetrical subunits or hexons. Type B capsids have an outer protein shell that is indistinguishable from that of A capsids but also contain an inner, roughly spherical protein shell (19,52). Type C capsids, or nucleocapsids, also contain an identical outer shell but lack the inner shell, which is replaced with the densely packed linear double-stranded DNA genome (5, 49).In a process unique to herpesviruses, nucleocapsids bud through the inner nuclear membrane (INM) of infected cells into the perinuclear space, a compartment that is continuous with the lumen of the endoplasmic reticulum (ER), to become virions. The envelope of these nascent virions is therefore derived from the INM. In alphaherpesviruses, nucleocapsids are enveloped preferentially over A or B capsids (40). In one model of virion egress, the virion envelope derived from the INM fuses with the outer nuclear membrane (ONM), dumping the nucleocapsid into the cytoplasm, where it subsequently undergoes a second envelopment step(s) in the Golgi apparatus, in the trans-Golgi apparatus network, or in vesicles derived from these compartments (6,31,45). Others have proposed that some nucleocapsids pass through expanded nuclear pores, receiving tegument prior to or at the time of budding into other organelles such as the ER or Golgi apparatus (28, 48). (For purposes of discussion this will be termed the expanded nuclear pore model.) In both of these cases, the final virion envelope is (in the deenvelopment model) or can be (in the expanded nuclear pore model) derived from organelles other than the INM. Alternatively, it has been proposed that one or more enveloped virions bud from the ONM, forming transport vesicles. Fusion of the outer membrane of the transport vesicle with the Golgi apparatus or other membranes would deliver enveloped virions into the Golgi apparatus lumen for glycoprotein processing or, upon fusion with the plasma membrane, would deliver virions within the vesicle to the extracellular space (26). Thus, in this model, the original virion envelope derived from the INM is retained throughout virion egress.The space between the nucleocapsid surface and the inner surface of the virion envelope is termed the tegument. The tegument of mature extracellular virions contains approximately 20 different proteins of varying stoichiometry, and electron tomography has shown that the tegument is arranged asymmetrically around the nucleocapsid as a series of concentric rings (22). Attachments of the innermost layer of mature tegument to capsi...

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The cytoplasmic tail of herpes simplex virus envelope glycoprotein D binds to the tegument protein VP22 and to capsids

Cited by 65 publications

References 20 publications

Characterization of VP22 in Herpes Simplex Virus-Infected Cells

Characterization of VP22 in Herpes Simplex Virus-Infected Cells

Unique structures in a tumor herpesvirus revealed by cryo-electron tomography and microscopy

Electron Tomography of Nascent Herpes Simplex Virus Virions

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