A comparison of herpes simplex and pseudorabies viruses

Kaplan, Albert S.; Vatter, A. E.

doi:10.1016/0042-6822(59)90068-6

Cited by 289 publications

(152 citation statements)

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“…Isolation of porcine blood monocytes, in vitro cultivation of SK cells and monocytes, and in vitro PRV inoculation of SK cells and monocytes were carried out as described before (8,10). PRV strains 89V87, Kaplan, Kaplan gE-gI null, Kaplan ICP18.5 null, and Kaplan UL49 null were used, and all were described before (13,21,29,30,33). At 13 h postinfection (p.i.…”

Section: Methodsmentioning

confidence: 99%

Copatching and Lipid Raft Association of Different Viral Glycoproteins Expressed on the Surfaces of Pseudorabies Virus-Infected Cells

Favoreel

Mettenleiter²,

Nauwynck³

2004

J Virol

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Pseudorabies virus (PRV) is a swine alphaherpesvirus that is closely related to human herpes simplex virus (HSV). Both PRV and HSV express a variety of viral envelope glycoproteins in the plasma membranes of infected cells. Here we show that at least four major PRV glycoproteins (gB, gC, gD, and gE) in the plasma membrane of infected swine kidney cells and monocytes seem to be linked, since monospecific antibody-induced patching of any one of these proteins results in copatching of the others. Further, for all four PRV glycoproteins, monospecific antibody-induced patches were enriched in GM1, a typical marker of lipid raft microdomains, but were excluded for transferrin receptor, a nonraft marker, suggesting that these viral proteins may associate with lipid rafts. However, only gB and, to a lesser extent, gE were found in lipid raft fractions by using detergent floatation assays, indicating that gC and gD do not show strong lipid raft association. Addition of methyl-␤-cyclodextrin (MCD), a cholesterol-depleting agent that is commonly used to disrupt lipid rafts, only slightly reduced copatching efficiency between the different viral proteins, indicating that other factors, perhaps tegument-glycoprotein interactions, may be important for the observed copatching events. On the other hand, MCD strongly reduced polarization of the antibody-induced viral glycoprotein patches to a cap structure, a gE-dependent process that has been described for specific PRV-and HSV-infected cells. Therefore, we hypothesize that efficient gE-mediated capping of antibody-antigen patches may require the lipid raft-associated signal transduction machinery.

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Section: Methodsmentioning

confidence: 99%

Copatching and Lipid Raft Association of Different Viral Glycoproteins Expressed on the Surfaces of Pseudorabies Virus-Infected Cells

Favoreel

Mettenleiter²,

Nauwynck³

2004

J Virol

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“…Virus particles from infected porcine kidney cell cultures were purified by sucrose-density-gradient centrifugation (Karger et al, 1998). Deletion mutants were propagated on cells maintained in DME/F12 cell culture medium (SigmaAldrich D-9785) supplemented with conventional leucine, whereas wild-type PrV-Ka (Kaplan & Vatter, 1959) was harvested from cells that had been cultured in medium containing exclusively deuterated leucine (L-leucine-5,5,5-d 3 ; Sigma-Aldrich, 99 atom% D), inserting a mass tag of 3 Da per leucine residue. Mutant and mass-tagged purified PrV-Ka were mixed at 1 : 1 protein ratios and proteins were separated by SDS-PAGE (Laemmli, 1970).…”

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confidence: 99%

Pseudorabies virus particles lacking tegument proteins pUL11 or pUL16 incorporate less full-length pUL36 than wild-type virus, but specifically accumulate a pUL36 N-terminal fragment

Michael

Böttcher

Klupp

et al. 2006

Journal of General Virology

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Proteins of the virion tegument of alphaherpesviruses are involved in protein-protein interactions, which play important roles in virus morphogenesis. Seven single-gene deletion mutants of Pseudorabies virus were analysed for alterations in the overall composition of the virion beyond the loss of the targeted protein. The UL36 protein (pUL36) was present in equal amounts in wild-type virions and mutants lacking pUL21, pUL49, pUL51, pUS3 or pUS8. Virions lacking pUL11 or pUL16 incorporated less full-length pUL36 than wild-type particles, but contained increased amounts of an N-terminal fragment of pUL36 that is present only in traces in wild-type virus and the other mutants.Homologues of the large tegument protein encoded by the UL36 open reading frame of herpes simplex virus (HSV) are present in all members of the Herpesviridae analysed so far. They constitute the largest herpesviral gene products and are proposed to be part of the capsid-proximal inner tegument, a structure that resides between nucleocapsid and envelope. Pseudorabies virus (PrV) pUL36 is a 3084 aa protein that is strictly essential for virus replication . PrV pUL36 function is important for virion morphogenesis in the cytoplasm after nuclear egress. pUL36 interacts with pUL37, another conserved tegument protein (Klupp et al., 2002). However, removal of the N-terminally located pUL37-binding domain does not result in a complete loss of function of pUL36, indicating that the essential requirement for this protein is due to additional, still unknown, functions . Recently, a deubiquitinating proteolytic activity was demonstrated to reside in the very N terminus of herpesvirus pUL36 homologues (Kattenhorn et al., 2005). Thus, both hitherto assigned functional regions of pUL36 reside in the Nterminal part of the protein. It has been shown in a previous study that PrV particles devoid of the tegument proteins pUS3, pUL47 and pUL49 or pUS8 (the envelope glycoprotein E) incorporated the same amounts of several tegument proteins like pUL36, pUL37 and pUL47 as wild-type virions (Michael et al., 2006). This stoichiometric incorporation suggests that, like assembly of the capsid, the architecture of the tegument might, in part, be strictly controlled. On the other hand, amounts of other tegument proteins like pUL46, pUL48 and pUL49 varied to some extent among the different mutants, indicating also some degree of flexibility in tegument composition. The suggested interaction of pUL36 with pentonal sites on the capsid (Zhou et al., 1999), which are devoid of the small capsid protein pUL35 that decorates hexons, may partly explain this strict stoichiometry.In a study to analyse single-protein-deleted PrV mutants for alterations in the composition of the virion beyond the loss of the deleted protein, structural proteins in virus particles were quantified by a procedure designated 'stable isotope labelling by amino acids in cell culture' (SILAC) developed by Ong et al. (2002), which was adapted for virions by our group (Michael et al., 2006). Virus particles fro...

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“…Based on immunological studies, virus morphology, intranuclear inclusions and ether sensitivity, Sabin (1934) [55] and Kaplan and Vatter (1959) [21] classified Aujeszky's disease virus (ADV)/pseudorabies virus (PrV) in the herpesvirus group. PrV was linked with sporadic problems in pigs world-wide and pigs were identified as a reservoir between 1920 and 1940 [30].…”

Section: Historical Backgroundmentioning

confidence: 99%

Cell biological and molecular characteristics of pseudorabies virus infections in cell cultures and in pigs with emphasis on the respiratory tract

et al. 2007

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-In the present review, several cell biological and molecular aspects of virus-cell and virus-host (pig) interactions are reviewed for pseudorabies (Aujeszky's disease) virus. Concerning the virus-cell interactions, the complex cascade of events in the virus replication cycle is given together with the different mechanisms of cell-to-cell spread. The pathogenesis of pseudorabies virus infections in pigs is concentrated on the sequence of events in the respiratory tract. Finally, a short overview is given on the control of the disease and eradication of the virus by the combination of marker vaccines and discriminating ELISA. pseudorabies virus / virus replication / cell-associated spread / pathogenesis / control

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A comparison of herpes simplex and pseudorabies viruses

Cited by 289 publications

References 7 publications

Copatching and Lipid Raft Association of Different Viral Glycoproteins Expressed on the Surfaces of Pseudorabies Virus-Infected Cells

Copatching and Lipid Raft Association of Different Viral Glycoproteins Expressed on the Surfaces of Pseudorabies Virus-Infected Cells

Pseudorabies virus particles lacking tegument proteins pUL11 or pUL16 incorporate less full-length pUL36 than wild-type virus, but specifically accumulate a pUL36 N-terminal fragment

Cell biological and molecular characteristics of pseudorabies virus infections in cell cultures and in pigs with emphasis on the respiratory tract

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