Biological evaluation of glycoproteins mapping to two distinct mRNAs within the BamHI fragment 7 of pseudorabies virus: Expression of the coding regions by vaccinia virus

Kost, Thomas A.; Jones, Elaine V.; Smith, Kitty P.; Reed, A. P.; Brown, Anna L.; Miller, Todd

doi:10.1016/0042-6822(89)90604-1

Cited by 33 publications

(22 citation statements)

References 30 publications

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“…In HSV-1 and SHV-1, the gE transcripts are polyadenylated downstream of the US9 gene, at the same site that a monocistronic transcript for the US9 gene is polyadenylated (Davison & McGeoch, 1986;Kost et al, 1989). Preliminary data indicate a similar transcription of the gE gene and US9 gene of BHV-1 (F.A.M.…”

Section: Discussionmentioning

confidence: 54%

A glycoprotein E deletion mutant of bovine herpesvirus 1 is avirulent in calves

Engelenburg¹,

Kaashoek²,

Rijsewijk³

et al. 1994

Journal of General Virology

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A marker vaccine elicits an antibody response in the host that can be distinguished from the antibody response induced by a wild-type strain. To obtain a bovine herpesvirus 1 (BHV-1) marker vaccine, we constructed a glycoprotein E (gE) deletion mutant. This was obtained by removing the complete gE coding region from the BHV-1 genome. To attenuate the gE deletion mutant further, we also introduced a small deletion in the thymidine kinase (TK) gene. We selected three mutants: the gE deletion mutant, a TK deletion mutant and a gE/TK double deletion mutant, and examined their virulence and immunogenicity in calves.After intranasal inoculation, the TK deletion mutant showed some residual virulence, whereas the gE and gE/TK deletion mutants were avirulent. The calves inoculated with the deletion mutants were protected against disease after challenge exposure and shed significantly less virus than control calves. Deleting the gE gene, therefore, has little effect on the immunogenicity of BHV-1, but is sufficient to reduce the virulence of BHV-1 in calves. These findings led us to conclude that the gE deletion mutant is a good candidate for a modified live BHV-1 marker vaccine.

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Section: Discussionmentioning

confidence: 54%

A glycoprotein E deletion mutant of bovine herpesvirus 1 is avirulent in calves

Engelenburg¹,

Kaashoek²,

Rijsewijk³

et al. 1994

Journal of General Virology

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“…2, lanes 2 and 4). This pattern has already been described for proteins from PRV-infected cells immunoprecipitated by an anti-gp50 monoclonal antibody (Kost et al, 1989). The lower band seems to be a non-glycosylated precursor of the mature glycoprotein (Petrovskis et al, 1986).…”

Section: Expression Of the Gp50 Glycoprotein By Ad-gp50 In Cell Culturementioning

confidence: 75%

Construction of a defective adenovirus vector expressing the pseudorabies virus glycoprotein gp50 and its use as a live vaccine

Éloit

Gilardi-Hebenstreit²,

Toma³

et al. 1990

Journal of General Virology

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“…The HSV-1 gD transcript includes the next downstream gene (US7) (McGeoch et al, 1985). Surprising data from the transcriptional mapping of the Us region of the PRV genome suggested that gp50 and gp63 were translated from a single coterminal transcript (Kost et al, 1989). Based on the lack of evident transcriptional regulatory signals upstream to EHV-1 ORF 3 and the short ORF 2-ORF 3 intergenic region, it is possible that the transcriptional organization for EHV-1 gD and gI genes is similar to the proposed PRV gp50 and gp63 genes' transcriptional organization, but transcriptional data from the EHV-1 Us region are needed to confirm such a model, which is quite different from the transcriptional organization of the HSV-1 gD and gI genes described by McGeoch et al (1985).…”

Section: Discussionmentioning

confidence: 99%

Equine Herpesvirus Type 1 Unique Short Fragment Encodes Glycoproteins with Homology to Herpes Simplex Virus Type 1 gD, gI and gE

Audonnet

Winslow

Allen

et al. 1990

Journal of General Virology

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The nucleotide sequence of a 6.4 kbp portion of the 10-6 kbp BamHI fragment D contained in the unique short region of the equine herpesvirus type 1 (EHV-1) genome has been determined. Analysis of this sequence revealed five open reading frames (ORFs), four complete and one incomplete, which were encoded by the same sense strand. Comparison of the EHV-1 DNA sequence with that encoding glycoproteins of other alphaherpesviruses has revealed no significant homologies. Comparison at the amino acid level, however, has demonstrated regions of significant sequence similarity between the three complete EHV-1 ORFs 2, 3 and 4, and the herpes simplex virus type 1 (HSV-1) glycoprotein gD encoded by the US6 gene, the HSV-1 glycoprotein gI encoded by the US7 gene and the HSV-1 glycoprotein gE encoded by the US8 gene, respectively. The interrupted ORF 5 was found to display partial homology with the HSV-1 US9-encoded protein, but no homology was found between the protein encoded by ORF 1 and other proteins. The three collinear EHV-10RFs encoding putative glycoproteins with homology to the HSV-1 glycoproteins were therefore designated EHV-1 gD, gI and gE, respectively. Moreover, further similarities were found between EHV-1 gD and pseudorabies virus (PRV) gp50, between EHV-1 gI and PRV gp63 and varicellazoster virus (VZV) gplV, and between EHV-1 gE and PRV gI and VZV gpI. It is concluded that EHV-1, PRV, HSV-1 and VZV encode homologous glycoprotein genes in the small unique components of their genomes and that the genetic organization of these regions is conserved.

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Biological evaluation of glycoproteins mapping to two distinct mRNAs within the BamHI fragment 7 of pseudorabies virus: Expression of the coding regions by vaccinia virus

Cited by 33 publications

References 30 publications

A glycoprotein E deletion mutant of bovine herpesvirus 1 is avirulent in calves

A glycoprotein E deletion mutant of bovine herpesvirus 1 is avirulent in calves

Construction of a defective adenovirus vector expressing the pseudorabies virus glycoprotein gp50 and its use as a live vaccine

Equine Herpesvirus Type 1 Unique Short Fragment Encodes Glycoproteins with Homology to Herpes Simplex Virus Type 1 gD, gI and gE

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