Lipoproteins of varicella-zoster virus

Harper, David R.; Kangro, H. O.

doi:10.1099/0022-1317-71-2-459

Cited by 19 publications

(12 citation statements)

References 41 publications

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“…Different species have also been described for the HSV-1 UL11 protein (4,26) which most probably are a result of different protein modifications. For the HSV-1 (25), VZV (17), and HCMV UL11 homologs (36), myristoylation and phosphorylation have been demonstrated. In addition, the HSV-1 UL11 protein have recently been shown to be palmitoylated (24).…”

Section: Discussionmentioning

confidence: 99%

“…The conservation of these features indicates that fatty acid modification may play an important role for UL11 function. The presence of N-myristic acid has indeed been shown for the HSV-1 UL11 protein (26), the homologous VZV gene 49 product (17), and the HCMV homolog pp28 (36). When expressed in the absence of other viral proteins, pp28 was detected in a cytoplasmic compartment which overlaps the endoplasmic reticulum-Golgi-intermediate compartment (36).…”

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confidence: 92%

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The Pseudorabies Virus UL11 Protein Is a Virion Component Involved in Secondary Envelopment in the Cytoplasm

Kopp

Granzow

Fuchs

et al. 2003

J Virol

160

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Homologs of the small tegument protein encoded by the UL11 gene of herpes simplex virus type 1 are conserved throughout all herpesvirus subfamilies. However, their function during viral replication has not yet been conclusively shown. Using a monospecific antiserum and an appropriate viral deletion and rescue mutant, we identified and functionally characterized the UL11 protein of the alphaherpesvirus pseudorabies virus (PrV). PrV UL11 encodes a protein with an apparent molecular mass of 10 to 13 kDa that is primarily detected at cytoplasmic membranes during viral replication. In the absence of the UL11 protein, viral titers were decreased approximately 10-fold and plaque sizes were reduced by 60% compared to wild-type virus. Intranuclear capsid maturation and nuclear egress resulting in translocation of DNA-containing capsids into the cytoplasm were not detectably affected. However, in the absence of the UL11 protein, intracytoplasmic membranes were distorted. Moreover, in PrV-⌬UL11-infected cells, capsids accumulated in the cytoplasm and were often found associated with tegument in aggregated structures such as had previously been demonstrated in cells infected with a PrV triple-mutant virus lacking glycoproteins E, I, and M (A. R. Brack, J. M. Dijkstra, H. Granzow, B. G. Klupp, and T. C. Mettenleiter, J. Virol. 73:5364-5372, 1999). Thus, the PrV UL11 protein, like glycoproteins E, I, and M, appears to be involved in secondary envelopment.The herpesvirus virion is a complex structure that contains at least 30 different virally encoded proteins. More than 15 viral proteins constitute the tegument that surrounds the herpesvirus capsid. The tegument itself is bounded by a cell-derived lipid bilayer envelope which contains more than 10 viral (glyco)proteins (28,35). Although the formation of capsids and the involved viral components has been delineated in some detail (41), the molecular mechanisms that drive assembly of the viral tegument and envelope during herpesvirus morphogenesis are still largely unknown. Initially, it had been postulated that herpesvirus virions are fully assembled in the nucleus, acquiring their final envelope by budding at the inner nuclear membrane. They should then be transported through the secretory pathway as complete virus particles (34). In this model, all envelope glycoproteins have to be present in the inner nuclear membrane and all tegument proteins have to be assembled onto the nascent virus particle in the nucleus. During the last few years, data have accumulated showing that capsids which bud at the inner nuclear membrane lose their primary envelope by fusion with the outer nuclear or the contiguous endoplasmic reticulum membrane and acquire a final envelope and tegument in the cytoplasm by budding into vesicles derived from the trans-Golgi network that contain mature viral glycoproteins (reviewed in reference 29). This envelopment-deenvelopment-reenvelopment mechanism revived investigations on the localization and site of addition of tegument proteins to the nascent virus par...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 92%

The Pseudorabies Virus UL11 Protein Is a Virion Component Involved in Secondary Envelopment in the Cytoplasm

Kopp

Granzow

Fuchs

et al. 2003

J Virol

160

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“…The HSV-1 (5, 43), varicella-zoster virus (31), and human cytomegalovirus (59) UL11 homologues have been demonstrated to be myristoylated, and the HSV-1 UL11 protein is also palmitoylated (42). These proteins thus have a high membrane affinity and might possess membrane-targeting functions (8,44,58).…”

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confidence: 99%

Influence of Tegument Proteins of Pseudorabies Virus on Neuroinvasion and Transneuronal Spread in the Nervous System of Adult Mice after Intranasal Inoculation

Klopfleisch

Teifke

Fuchs

et al. 2004

J Virol

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Pseudorabies virus (PrV) is a neurotropic alphaherpesvirus that, after intranasal infection of adult mice, enters peripheral neurons and propagates to the central nervous system. In recent years we have analyzed the contribution of virus-encoded glycoproteins to neuroinvasion and transneuronal spread (reviewed in T. C. Mettenleiter, Virus Res. 92:197-206, 2003). We now extend our studies to analyze the role of tegument proteins in these processes. To this end, PrV mutants unable to express the UL11, UL37, UL46, UL47, and UL48 tegument proteins, as well as the corresponding rescued viruses, were intranasally instilled into 6-to 8-weekold CD1 strain mice. First, mean survival times were determined which showed that mice infected with the UL46 deletion mutant succumbed to the disease as early as wild-type PrV-infected animals. Survival times increased in the order: PrV-⌬UL47-, PrV-⌬UL11-, and PrV-⌬UL48-infected animals, a finding which parallels the growth phenotype of these viruses in cell culture. In contrast, none of the PrV-⌬UL37-infected animals died. Upon closer histological examination, all viruses except PrV-⌬UL37 were able to infect the nasal cavity and propagate to first-and second-order neurons as shown by two-color immunofluorescence. However, neuroinvasion was delayed in PrV-⌬UL47, PrV-⌬UL11, and PrV-⌬UL48, a finding that correlated with the extended survival times. Surprisingly, whereas PrV-⌬UL48 and PrV-⌬UL37 replicated to similar titers in cell culture which were ϳ500-fold lower than those of wild-type virus, after intranasal infection of mice PrV-⌬UL48 was able to infect areas of the brain like wild-type PrV, although only after a considerably longer time period. In contrast, PrV-⌬UL37 was not able to enter neurons and was restricted to the infection of single cells in the nasal respiratory epithelium. Thus, our data demonstrate the importance of herpesviral tegument proteins in neuronal infection and show a different contribution of tegument proteins to the neuroinvasion phenotype of a neurotropic alphaherpesvirus.Pseudorabies virus (PrV) is an alphaherpesvirus that causes Aujeszky's disease, a severe neurological disorder, in a broad range of mammalian species. The pig is the natural host of PrV since it is the only animal able to survive a productive infection, and latently infected pigs serve as a virus reservoir. After oronasal infection, which is the natural route of PrV entry into the organism, adult pigs usually show only mild clinical signs of respiratory distress or reproductive failure. In contrast, young piglets are very sensitive to virus invasion of the central nervous system (CNS) (36). Pruritus, the hallmark of the syndrome in nonporcine species, is usually not observed in pigs. In contrast to pigs, the course of infection in susceptible nonporcine species is peracute with a high mortality. These species are endstage hosts, i.e., they generally do not shed the virus and are therefore less important in transmission to other species (25,29,30,45,56,60).Since PrV infects a wide range o...

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“…In addition, many viruses including hepatitis B [6], vaccinia virus [7], the herpes viruses [8], polio virus [9], rotaviruses [lo], spleen necrosis virus and human immunodeficiency virus (HIV) [ l l , 121 have been shown to have myristoylated coat and regulatory proteins. For many of these viruses the myristoylation of these proteins has been demonstrated to be important for their replication [ 11 -181.…”

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confidence: 99%

Characterization of a polyhistidine‐tagged form of human myristoyl‐CoA:protein N‐myristoyltransferase produced in Escherichia coli

McIlhinney

Patel

McGLONE

1994

European Journal of Biochemistry

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The enzyme myristoyl-CoA : protein N-myristoyltransferase is responsible for the attachment of a myristoyl group to the N-terminal glycine of a number of cell, viral and fungal proteins. In order to overcome the difficulties of purification of this enzyme from tissue sources, we have produced an N-terminally polyhistidine-tagged version of the enzyme and expressed this in Escherichia coli. The resulting enzyme has a molecular mass of 53 kDa and is fully active showing the expected specificity for myristic acid and causing the N-terminal myristoylation of both synthetic peptide and protein substrates in vitro. The enzyme exhibits a broad pH optimum peaking at a pH of 8.0 and has a K,,, for myristoyl-CoA of 7.6 pM. The two synthetic peptide substrates based on the N-terminal sequence of the catalytic subunit of protein kinase A (GNAAAARR) and of p6Osrc (GSS-KSKF'KDPSQRRRY) have different kinetic parameters with K, values of 115.2 pM and 44.2 pM and V,,, values of 95 and 120 nmol . min-' . mg-l, respectively. The expressed enzyme is partially inhibited (50%) by iodoacetamide at 5 mM and fully inhibited by diethylpyrocarbonate at 10 mM.

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Lipoproteins of varicella-zoster virus

Cited by 19 publications

References 41 publications

The Pseudorabies Virus UL11 Protein Is a Virion Component Involved in Secondary Envelopment in the Cytoplasm

The Pseudorabies Virus UL11 Protein Is a Virion Component Involved in Secondary Envelopment in the Cytoplasm

Influence of Tegument Proteins of Pseudorabies Virus on Neuroinvasion and Transneuronal Spread in the Nervous System of Adult Mice after Intranasal Inoculation

Characterization of a polyhistidine‐tagged form of human myristoyl‐CoA:protein N‐myristoyltransferase produced in Escherichia coli

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