Pseudorabies Virus and Herpes Simplex Virus Type 1 Utilize Different Tegument-Glycoprotein Interactions to Mediate the Process of Envelopment

Omar, Omar S.; Simmons, Alicia J.; André, Nicole M.; Wilson, Duncan W.; Gross, Sarah T.

doi:10.1159/000339467

Cited by 7 publications

(7 citation statements)

References 24 publications

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“…Triple deletions of gE, gI, and either gM or gD blocks secondary envelopment (Brack et al, 1999;Farnsworth et al, 2003), whereas individual deletions of these glycoproteins or VP22 (UL49) have minimal effects on secondary envelopment, indicating that these protein interactions function in a redundant manner. VP16 (UL48), another central hub of tegument protein interactions, is reported to bind gH (Gross et al, 2003;Kamen et al, 2005), although this interaction may not be conserved with PRV (Omar et al, 2013).…”

Section: Tegument/membrane Interactions In Secondary Envelopmentmentioning

confidence: 99%

Tegument Assembly, Secondary Envelopment and Exocytosis

Hogue

2022

Current Issues in Molecular Biology

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Alphaherpesvirus tegument assembly, secondary envelopment, and exocytosis processes are understood in broad strokes, but many of the individual steps in this pathway, and their molecular and cell biological details, remain unclear. Viral tegument and membrane proteins form an extensive and robust protein interaction network, such that essentially any structural protein can be deleted, yet particles are still assembled, enveloped, and released from infected cells.We conceptually divide the tegument proteins into three groups: conserved inner and outer teguments that participate in nucleocapsid and membrane contacts, respectively; and "middle" tegument proteins, consisting of some of the most abundant tegument proteins that serve as central hubs in the protein interaction network, yet which are unique to the alphaherpesviruses. We then discuss secondary envelopment, reviewing the tegument-membrane contacts and cellular factors that drive this process. We place this viral process in the context of cell biological processes, including the endocytic pathway, ESCRT machinery, autophagy, secretory pathway, intracellular transport, and exocytosis mechanisms. Finally, we speculate about potential relationships between caister.com/cimb 551 Curr. Issues Mol. Biol. Vol. 42 Curr. Issues Mol.

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Section: Tegument/membrane Interactions In Secondary Envelopmentmentioning

confidence: 99%

Tegument Assembly, Secondary Envelopment and Exocytosis

Hogue

2022

Current Issues in Molecular Biology

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“…Second, the tegument is involved in many facets of the viral life cycle, including the migration of capsids on microtubules (9)(10)(11)(12)(13)(14), the anchorage of the capsids to nuclear pores (15)(16)(17)(18)(19)(20), the transactivation of viral genes (21), the modulation of host protein expression (22,23), viral latency (24), and the regulation of the immune response (13,(25)(26)(27). Finally, many tegument proteins also interact with each other and/or with viral glycoproteins and accumulate at the trans-Golgi network (TGN), where they altogether delineate the likely final envelopment site (4,5,28).…”

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confidence: 99%

Analysis of the Early Steps of Herpes Simplex Virus 1 Capsid Tegumentation

Henaff

Rémillard-Labrosse

Loret

et al. 2013

J Virol

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Herpes simplex virus type 1 particles are multilayered structures with a DNA genome surrounded by a capsid, tegument, and envelope. While the protein content of mature virions is known, the sequence of addition of the tegument and the intracellular compartments where this occurs are intensely debated. To probe this process during the initial stages of egress, we used two approaches: an in vitro nuclear egress assay, which reconstitutes the exit of nuclear capsids to the cytoplasm, and a classical nuclear capsid sedimentation assay. As anticipated, in vitro cytoplasmic capsids did not harbor U L 34, U L 31, or viral glycoproteins but contained U S 3. In agreement with previous findings, both nuclear and in vitro capsids were positive for ICP0 and ICP4. Unexpectedly, nuclear C capsids and cytoplasmic capsids produced in vitro without any cytosolic viral proteins also scored positive for U L 36 and U L 37. Immunoelectron microscopy confirmed that these tegument proteins were closely associated with nuclear capsids. When cytosolic viral proteins were present in the in vitro assay, no additional tegument proteins were detected on the capsids. As previously reported, the tegument was sensitive to high-salt extraction but, surprisingly, was stabilized by exogenous proteins. Finally, some tegument proteins seemed partially lost during egress, while others possibly were added at multiple steps or modified along the way. Overall, an emerging picture hints at the early coating of capsids with up to 5 tegument proteins at the nuclear stage, the shedding of some viral proteins during nuclear egress, and the acquisition of others tegument proteins during reenvelopment.

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“…The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. Several studies 50,51 have indicated that viral PrV envelopment and tegumentation occurs at late Golgi or post-Golgi compartments, suggesting that this gene may have a role in PrV virulence and dissemination. As previously reported (Figure 4a), this gene is linked to other two gene of interest, the JMJD6 (JmjC domain-containing protein) and the METTL23 (methyltransferase like 23) genes.…”

Section: Discussionmentioning

confidence: 99%

Identification of Candidate Genes Associated with Bacterial and Viral Infections in Wild Boars Hunted in Tuscany (Italy)

Fabbri

Crovetti

Tinacci

et al. 2021

Preprint

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Wild boar (Sus scrofa L.) is one of the large mammals most spread worldwide, highly adaptable, and its population has rapidly increased in many areas in Europe. Central Italy, as well as Tuscany, is an area particularly suitable for wild boar. Wild boars are potential hosts for different etiological agents, such as Brucella spp., Leptospira spp. and Pseudorabies virus and can contribute to maintain and/or to disseminate some bacterial or viral pathogens to humans and domestic animals, above all-in free-range farms. In order to identify hypothetical genomic regions associated with these infection diseases, 96 samples of wild boars hunted in Tuscany during the 2018–2019 and 2019-2020 hunting seasons were considered. Diagnosis was achieved by serological tests and 42 Pseudorabies, 31 Leptospira and 15 Brucella positive animals were identified. All animals were genotyped with Geneseek Genomic Profiler Porcine HD (70k) and a genome-wide scan was then performed. Significant markers were highlighted for Pseudorabies (two SNPs), Brucella (seven SNPs), and Leptospira (four SNPs) and they were located within, or nearby, 29 annotated genes on chromosome 6, 9, 12, 13, 14 and 18. Eight genes are implicated in viral (SEC14L1, JMJD6, SRSF2, TMPRSS2, MX1, MX2) or bacterial (COL8A1, SPIRE1) infections, seven genes (MFSD11, METTL23, CTTNBP2, BACE2, IMPA2, MPPE1 and GNAL) are involved in mental disorders and one gene (MGAT5B) is related to the Golgi complex. Results presented here provide interesting starting points for future research, validation studies and fine mapping of candidate genes involved in bacterial and viral infections in wild boar.

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Pseudorabies Virus and Herpes Simplex Virus Type 1 Utilize Different Tegument-Glycoprotein Interactions to Mediate the Process of Envelopment

Cited by 7 publications

References 24 publications

Tegument Assembly, Secondary Envelopment and Exocytosis

Tegument Assembly, Secondary Envelopment and Exocytosis

Analysis of the Early Steps of Herpes Simplex Virus 1 Capsid Tegumentation

Identification of Candidate Genes Associated with Bacterial and Viral Infections in Wild Boars Hunted in Tuscany (Italy)

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