Glycoprotein gIII of pseudorabies virus is multifunctional

Schreurs, C; Mettenleiter, Thomas C.; Zuckermann, Federico A.; Sugg, Nancy; Ben-Porat, Tamar

doi:10.1128/jvi.62.7.2251-2257.1988

Cited by 93 publications

(75 citation statements)

References 31 publications

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“…Evidence that heparan sulfate also serves as receptor for these animal viruses comes from findings that heparin inhibits infection and that treatment of cells with heparitinase or heparinase reduces the binding of virus to the cells and renders the cells at least partially resistant to virus infection (41,46,53) . In addition, both of these animal viruses encode glycoproteins that are related to HSV gC and, for both viruses, the gC homolog has heparin-binding activity and is principally responsible for the binding of virus to cells (40,41,46,53,54,64,70) . These similarities among HSV, pseudorabies virus, and bovine herpesvirus type 1 are consistent with the similarities in biological properties and pathogenesis of the viruses (despite their propensity to infect different animal species) .…”

Section: Plating Efficiencies Of Vesicular Stomatitis Virus On Wildmentioning

confidence: 99%

Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans.

Shieh

WuDunn

Montgomery

et al. 1992

The Journal of Cell Biology

504

397

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. The role of cell surface heparan sulfate in herpes simplex virus (HSV) infection was investigated using CHO cell mutants defective in various aspects of glycosaminoglycan synthesis . Binding of radiolabeled virus to the cells and infection were assessed in mutant and wild-type cells . Virus bound efficiently to wild-type cells and initiated an abortive infection in which immediate-early or a viral genes were expressed, despite limited production of late viral pro-DENTIFICATION of a particular cell surface molecule as a receptor for a virus, or identification of multiple cell surface molecules as alternative receptors, must be based on evidence satisfying at least two criteria . First, presence of the receptor (or one of multiple receptors) should be prerequisite for binding of virus to a cell and for subsequent infection . Conversely, absence of the putative receptor(s) should prevent specific binding of the virus to the cell and should render the cell resistant to infection . Second, it should be possible to show that the virus actually interacts physically with the cell surface molecule(s) in question . The purpose of this paper is to report genetic evidence that the cell surface glycosaminoglycan (GAG)', heparan sulfate, fulfills these criteria for identification as a receptor for herpes simplex virus (HSV) .HSV is isolated principally from humans under natural conditions although the virus has a broad host range under experimental conditions . A variety of laboratory animals can be infected with the virus and most adherent vertebrate cells grown in culture are susceptible to HSV infection . This implies that the cell surface receptors for HSV are ubiquitous and highly conserved or that different receptors may be used for the infection of different cell types.Two kinds of cell surface molecules have been implicated as receptors for HSV: heparan sulfate moieties of cell surface Darrell wuDunn's present address is

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Section: Plating Efficiencies Of Vesicular Stomatitis Virus On Wildmentioning

confidence: 99%

Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans.

Shieh

WuDunn

Montgomery

et al. 1992

The Journal of Cell Biology

504

397

View full text Add to dashboard Cite

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“…Despite the similarities among the various herpesviruses, though, differences have emerged. For example, virions of pseudorabies virus (PRV) lacking or containing mutant forms of gC (formerly gIII) are readily removed from cell surfaces by washing infected monolayers with phosphate-buffered saline (PBS) (6,29). The virions that do manage to infect cells do so independently of heparan sulfate (6,17).…”

mentioning

confidence: 99%

A heterologous heparin-binding domain can promote functional attachment of a pseudorabies virus gC mutant to cell surfaces

Flynn

Ryan

1995

J Virol

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The efficient attachment of pseudorabies virus to cultured cells is dependent on an electrostatic interaction between negatively charged cell surface heparan sulfate and the viral envelope glycoprotein gC. Deletion of the first one-third of gC severely impairs virus attachment, but the mutant virions are still capable of entering cells and establishing an infection via a gC-independent pathway. This region of gC contains three clusters of positively charged amino acids that exactly or nearly conform to proposed consensus motifs for heparinbinding domains (HBDs), and the loss of one or more of these potential HBDs may be responsible for the observed attachment defect. To more directly show the involvement of HBDs in pseudorabies virus attachment to cells, we replaced the first one-third of gC with a single, biochemically defined HBD from apolipoprotein B-100. On the basis of the results of attachment, penetration, and heparin competition assays, the heterologous HBD mediated heparan sulfate-dependent virus attachment, but not to fully wild-type levels. Although the intermediate phenotype is not understood, the apolipoprotein B-100 HBD may represent the smallest defined amino acid sequence that promotes functional herpesvirus attachment to cultured cells.

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“…At that time, a large number of viral antigen-positive plaques were found in the nasal mucosa. The reason for the detection of a low number of free viruses in the nasal mucus can be sought in the defect of the virus to produce gE and gC, two glycoproteins which both play an important role in virus release (Schreurs et al, 1988;Zsak et al, 1989). From a safety point of view, Kaplan gE − gC − is preferred to Kaplan gE − gI − .…”

Section: Discussionmentioning

confidence: 99%

Efficacy of an Intranasal Immunization with gEgC and gEgI Double‐deletion Mutants of Aujeszky’s Disease Virus in Maternally Immune Pigs and the Effects of a Successive Intramuscular Booster with Commercial Vaccines

Nauwynck

Labarque

Pensaert

1999

Journal of Veterinary Medicine, Series B

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In this study, an intranasal immunization strategy was set up in maternally immune pigs in order to protect them not only clinically but also virologically. Two genetically engineered Aujeszky's disease virus (ADV) strains, Kaplan gE − gI − and Kaplan gE − gC − , were used for intranasal immunization. Both strains were safe for 4-week-old pigs. A single intranasal inoculation of 10 6.0 TCID 50 of Kaplan gE − gI − and Kaplan gE − gC − at 4 weeks of age in the presence of moderate titres of maternally derived antibodies (SN titres: 12-16) reduced the amount of weight loss, fever and virus excretion upon challenge 6 weeks later. In a second experiment, the effect of an additional intramuscular booster with three different commercial vaccines (containing attenuated Bartha or NIA 3 -783 or inactivated Phylaxia; all suspended in an oil-inwater emulsion) at 10 weeks of age was evaluated. One month after the last intramuscular booster, between five and seven pigs from each group were selected for challenge. All intranasally/intramuscularly immunized pigs showed a significantly better clinical and virological protection after challenge than the single intranasally immunized pigs. In the double immunized group, the protection was better when Kaplan gE − gC − was used for the intranasal priming (only two of 14 pigs excreted virus with a duration of 4 days) than when Kaplan gE − gI − was used (13 of 18 pigs excreted virus with a duration ranging from 1 to 4 days). The virological protection was not influenced by the type of vaccine used for booster vaccination. Because the intranasal/intramuscular immunization approach is very compatible with current pig movements on farms and pigs with moderate levels of maternally derived antibodies can effectively be immunized, it can be considered as a good alternative to intramuscular/intramuscular vaccinations especially in regions with a high ADV prevalence.

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Glycoprotein gIII of pseudorabies virus is multifunctional

Cited by 93 publications

References 31 publications

Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans.

Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans.

A heterologous heparin-binding domain can promote functional attachment of a pseudorabies virus gC mutant to cell surfaces

Efficacy of an Intranasal Immunization with gEgC and gEgI Double‐deletion Mutants of Aujeszky’s Disease Virus in Maternally Immune Pigs and the Effects of a Successive Intramuscular Booster with Commercial Vaccines

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