Protection of cattle from bovine herpesvirus type I (BHV-1) infection by immunization with individual viral glycoproteins

Babiuk, Lorne A.; L’Italien, James; Hurk, Sylvia van Drunen Littel‐van den; Zamb, Timothy J.; Lawman, M. J. P.; Hughes, Graham J.; Gifford, G. A.

doi:10.1016/0042-6822(87)90347-3

Cited by 144 publications

(79 citation statements)

References 30 publications

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“…In a previous study, four specific antigenic zones were identified among them (Stepanek et al 1990). This finding corresponds to those of Misra et al (1981) and Babiuk et al (1987), who identified four immunologically active glycoproteins, gp-l-gp-4 of BHV-l.…”

Section: Resultssupporting

confidence: 92%

Incorporation of Bovine Herpesvirus 1 Protein Subunits into Large Unilamellar and Multilamellar Liposomes

Hampl¹,

Štěpánek²,

Fränz³

et al. 1992

Acta Vet. Brno

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Hampl J., J. StC!panek, J. FranZ Acta vet. Bmo, 61, 1992: 29-36. Virus proteins, obtained by the treatment of purified bovine herpesvirus 1 with detergents, were incorporated into large unilamellar (LUV) and multilamellar (MLV) liposomes. Their antigenicity was compared with that of virus proteins adsorbed onto LUV surface in mice. Both antibody levels and dynamics of antibody responses, examined by ELISA and RIA, confirmed a marked immunostimulatory effect of the liposomes. The most pronounced antibody responses were observed in animals injected with virus proteins incorporated into LUV, prepared from egg phospholipid, or adsorbed onto their surface. BOfJine herpesT.Jirus 1, fJirus proteins, antibody response, large unilamellar liposomes, multilamellar liposomesOne of the current innovation trends in the production of vaccines against virus diseases of farm animals is the development of subunit vaccines. The principle consists in the selection from the whole complex of virus structural proteins of those, which elicit an immune response providing the protection of vaccinates (protective antigens). The question whether the proteins are obtained by degradation of complete virus particles, propagated by conventional methods, or are prepared in vitro by techniques of molecular biology, is irrelevaIit.A common drawback, limiting the immediate use of such proteins, is their rather weak immunogenicity, which is much lower than that of the same proteins as a part of complete virion structures. All attempts to compensate for this drawback by the use of current non-specific immunostimulants or adiuvants have failed (Dougan 1985;Rowland 1986;Zanetti et al. 1987; Liu and Cepica 1990).A certain effect was evident, however, when the protein subunits were incorporated back into multimolecular, corpuscular structures, such as ISCOMs (immunity stimulating complex), or various types of liposomes. In both cases, the size and shape of the particles resemble those of virions.Enhancement of antigenicity of proteins, incorporated into ISCOMs or liposomes, was reported by

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Section: Resultssupporting

confidence: 92%

Incorporation of Bovine Herpesvirus 1 Protein Subunits into Large Unilamellar and Multilamellar Liposomes

Hampl¹,

Štěpánek²,

Fränz³

et al. 1992

Acta Vet. Brno

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“…against death from bovine respiratory disease on challenge with a combined infection of BHV-1 and Pasteurella haemolytica (Babiuk et al, 1987).…”

Section: Short Communicationmentioning

confidence: 99%

The Effect of Bovine Herpesvirus Type 1 Glycoproteins gI and gIII on Herpesvirus Infections

Chase

Carter-Allen²,

Letchworth³

1989

Journal of General Virology

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SUMMARYWe expressed the bovine herpesvirus type 1 (BHV-1) glycoproteins, gI and gIII, in bovine cells using a bovine papillomavirus vector. The proteins expressed by these cells had the same Mr as the native BHV-1 proteins and monoclonal antibodies detected no differences in their antigenic structure. Cells expressing gI were infected with either BHV-1 or herpes simplex virus type 1 (HSV-1). The number of plaques in gI-expressing cells was similar to that seen with normal fibroblasts infected with BHV-1 or HSV-1. However, BHV-1 or HSV-1 plaques produced in gI-expressing cells were smaller and darker than those seen in normal fibroblasts indicating an interference with cell-to-cell transmission or cellular lysis. Virus growth curves and [3SS]methionine labelling of BHV-l-infected gI-expressing cells showed no difference in virus production, virus protein synthesis or cellular protein shutdown when compared to BHV-l-infected normal cells. This led us to conclude that the gI protein may interfere with a cellular protein(s) responsible for the cytopathic effects of BHV-1 infection. Cells expressing gIII were fully susceptible to BHV-1 infection.

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“…The role of individual herpesviral glycoproteins in the induction of neutralizing and protective antibodies in vivo is well known (Balachandran et al, 1982;Babiuk et al, 1987 ;Dix et al, 1981 ;Edson et al, 1985 ;Fuller et al, 1989;Guo et al, 1989;Pereira et al, 1980;Powell et al, 1974;Roberts et al, 1985;Spear, 1975;van Drunen Littel-van den Hurk et al, 1989). Recently PRV glycoproteins gp50 (Eloit et al, 1988 ;Ishii et al, 1988 ;Kost et al, 1989;Marchioli et al, 1987Marchioli et al, , 1988Petrovskis et al, 1986a), and gill (Eloit et al, 1988;Marchioli, 1988) were identified as important immunogens in mice and in swine.…”

Section: Discussionmentioning

confidence: 99%

Pseudorabies Virus Glycoprotein gI: in Vitro and in Vivo Analysis of Immunorelevant Epitopes

Fuchs¹,

Rziha²,

Lukàcs³

et al. 1990

Journal of General Virology

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Protection of cattle from bovine herpesvirus type I (BHV-1) infection by immunization with individual viral glycoproteins

Cited by 144 publications

References 30 publications

Incorporation of Bovine Herpesvirus 1 Protein Subunits into Large Unilamellar and Multilamellar Liposomes

Incorporation of Bovine Herpesvirus 1 Protein Subunits into Large Unilamellar and Multilamellar Liposomes

The Effect of Bovine Herpesvirus Type 1 Glycoproteins gI and gIII on Herpesvirus Infections

Pseudorabies Virus Glycoprotein gI: in Vitro and in Vivo Analysis of Immunorelevant Epitopes

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