Incorporation of the herpes simplex virus type 1 tegument protein VP22 into the virus particle is independent of interaction with VP16

O'Regan, Kevin J.; Murphy, Michael A.; Bucks, Michelle A.; Wills, John W.; Courtney, Richard J.

doi:10.1016/j.virol.2007.07.020

Cited by 31 publications

(55 citation statements)

References 44 publications

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“…While GFP alone showed no binding activity to any of the fusion proteins, GFP-VP22 interacted efficiently with GST-gE and GST-VP16 but not GST alone (Fig. 2C), as described previously by others (32,33). Interestingly, GFP-22 also bound, but more weakly, to the C-terminal tail of gM.…”

Section: Resultssupporting

confidence: 84%

“…HSV-1 VP22 has been reported to have a number of virus binding partners, namely, VP16, gE, and gD (4,13,19,32,33). In addition, PRV VP22 has been shown to interact with the cytoplasmic tail of gM (20).…”

Section: Resultsmentioning

confidence: 99%

“…However, the role of this interaction in virus infection has not yet been clearly defined and the fact that additional glycoprotein interactions have been described, with gM in the case of PRV and gD in the case of HSV-1, may point to potential redundancy in the mechanism of VP22 packaging (4,19,20). In addition, we and others have previously shown that HSV-1 VP22 interacts directly with a second tegument protein, namely, VP16 (13,33), an interaction that could provide an alternative route for VP22 to enter the virion. In a previous study, we concluded that the region of VP22 containing its VP16 interaction domain was required but not sufficient for optimal VP22 packaging into the assembling virion, with an additional C-terminal determinant also involved (23).…”

mentioning

confidence: 99%

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Virion Incorporation of the Herpes Simplex Virus Type 1 Tegument Protein VP22 Occurs via Glycoprotein E-Specific Recruitment to the Late Secretory Pathway

Stylianou

Maringer

Cook

et al. 2009

J Virol

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The mechanism by which herpesviruses acquire their tegument is not yet clear. One model is that outer tegument proteins are recruited by the cytoplasmic tails of viral glycoproteins. In the case of herpes simplex virus tegument protein VP22, interactions with the glycoproteins gE and gD have been shown. We have previously shown that the C-terminal half of VP22 contains the necessary signal for assembly into the virus. Here, we show that during infection VP22 interacts with gE and gM, as well as its tegument partner VP16. However, by using a range of techniques we were unable to demonstrate VP22 binding to gD. By using pulldown assays, we show that while the cytoplasmic tails of both gE and gM interact with VP22, only gE interacts efficiently with the C-terminal packaging domain of VP22. Furthermore, gE but not gM can recruit VP22 to the Golgi/trans-Golgi network region of the cell in the absence of other virus proteins. To examine the role of the gE-VP22 interaction in infection, we constructed a recombinant virus expressing a mutant VP22 protein with a 14-residue deletion that is unable to bind gE (⌬gEbind). Coimmunoprecipitation assays confirmed that this variant of VP22 was unable to complex with gE. Moreover, VP22 was no longer recruited to its characteristic cytoplasmic trafficking complexes but exhibited a diffuse localization. Importantly, packaging of this variant into virions was abrogated. The mutant virus exhibited poor growth in epithelial cells, similar to the defect we have observed for a VP22 knockout virus. These results suggest that deletion of just 14 residues from the VP22 protein is sufficient to inhibit binding to gE and hence recruitment to the viral envelope and assembly into the virus, resulting in a growth phenotype equivalent to that produced by deleting the entire reading frame.The herpesvirus tegument is the virion compartment located between the DNA-containing capsid and the virus envelope (6). Although it is well defined that the viral capsid assembles in the nucleus (37,38) and the viral envelope is acquired from cellular membranes (3, 24), the mechanism of tegument protein acquisition is still to be established. At least 20 virusencoded components are recruited into the herpes simplex virus type 1 (HSV-1) tegument (32), and there is increasing evidence to suggest that subsets of these proteins may be added as assembly progresses along the maturation pathway (28). To ensure efficient incorporation, it is likely that individual tegument proteins are specifically targeted to their cellular site of recruitment. Such targeting could involve interaction with a viral partner, a cellular partner, or both. A clearer understanding of how individual tegument proteins are acquired by newly assembling virions will help to define the herpesvirus assembly pathway.A number of protein-protein interactions between individual tegument proteins (13,40,42), and between tegument proteins and glycoproteins (19,20,22,32), have been described that may provide useful insight into the assembly process. In p...

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Section: Resultssupporting

confidence: 84%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Virion Incorporation of the Herpes Simplex Virus Type 1 Tegument Protein VP22 Occurs via Glycoprotein E-Specific Recruitment to the Late Secretory Pathway

Stylianou

Maringer

Cook

et al. 2009

J Virol

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“…Several studies have shown that pUL49 interacts with the cytoplasmic tails of HSV-1 gE, gD and envelope protein pUS9 (Chi et al, 2005;Farnsworth et al, 2007a;O'Regan et al, 2007). In PrV, interactions of pUL49 with the cytoplasmic tail of both gE and gM were identified (Fuchs et al, 2002b).…”

Section: Secondary Envelopmentmentioning

confidence: 99%

“…In PrV, interactions of pUL49 with the cytoplasmic tail of both gE and gM were identified (Fuchs et al, 2002b). Furthermore, for both HSV-1 and PrV, gE or gM is sufficient for recruitment of pUL49 into virions through a direct interaction (Fuchs et al, 2002b;Michael et al, 2006;O'Regan et al, 2007;Stylianou et al, 2009).…”

Section: Secondary Envelopmentmentioning

confidence: 99%

Role of tegument proteins in herpesvirus assembly and egress

et al. 2010

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Morphogenesis and maturation of viral particles is an essential step of viral replication. An infectious herpesviral particle has a multilayered architecture, and contains a large DNA genome, a capsid shell, a tegument and an envelope spiked with glycoproteins. Unique to herpesviruses, tegument is a structure that occupies the space between the nucleocapsid and the envelope and contains many virus encoded proteins called tegument proteins. Historically the tegument has been described as an amorphous structure, but increasing evidence supports the notion that there is an ordered addition of tegument during virion assembly, which is consistent with the important roles of tegument proteins in the assembly and egress of herpesviral particles. In this review we first give an overview of the herpesvirus assembly and egress process. We then discuss the roles of selected tegument proteins in each step of the process, i.e., primary envelopment, deenvelopment, secondary envelopment and transport of viral particles. We also suggest key issues that should be addressed in the near future.

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Host factors associated with either VP16 or VP16‐induced complex differentially affect HSV‐1 lytic infection

Ding

Neumann

Zhu

2022

Reviews in Medical Virology

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Herpes simplex virus type 1 (HSV‐1) is an important human pathogen with neurotropism. Following lytic infection in mucosal or skin epithelium, life‐long latency is established mainly in sensory neurons, which can periodically reactivate by stress, leading to recurrent disease and virus transmission. During the virus's productive infection, the tegument protein VP16, a component of HSV‐1 virion, is physically associated with two cellular factors, host cell factor‐1 (HCF‐1), and POU domain protein Oct‐1, to construct the VP16‐induced complex, which is essential to stimulate immediate early (IE)‐gene transcription as well as initiate the lytic programme. Apart from HCF‐1 and Oct‐1, VP16 also associates with a series of other host factors, making a VP16‐induced regulatory switch to either activate or inactivate virus gene transcription. In addition, VP16 has effects on distinct signalling pathways via binding to various host molecules that are essentially related to innate immune responses, RNA polymerases, molecular chaperones, and virus infection‐induced host shutoff. VP16 also functionally compensates for given host factors, such as PPAR‐γ and ß‐catenin. In this review, we provide an overview of the updated insights on the interplay between VP16 and the host factors that coordinate virus infection.

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Incorporation of the herpes simplex virus type 1 tegument protein VP22 into the virus particle is independent of interaction with VP16

Cited by 31 publications

References 44 publications

Virion Incorporation of the Herpes Simplex Virus Type 1 Tegument Protein VP22 Occurs via Glycoprotein E-Specific Recruitment to the Late Secretory Pathway

Virion Incorporation of the Herpes Simplex Virus Type 1 Tegument Protein VP22 Occurs via Glycoprotein E-Specific Recruitment to the Late Secretory Pathway

Role of tegument proteins in herpesvirus assembly and egress

Host factors associated with either VP16 or VP16‐induced complex differentially affect HSV‐1 lytic infection

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