Role of glycoproteins of pseudorabies virus in eliciting neutralizing antibodies

Ben-Porat, Tamar; Demarchi, J; Lomniczi, B.; Kaplan, Albert S.

doi:10.1016/0042-6822(86)90458-7

Cited by 116 publications

(96 citation statements)

References 20 publications

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“…The envelope glycoproteins are the principal immunogens of herpesviruses involved in eliciting both humoral and cellular host immune responses (Ben Porat et al, 1986;Cantin et al, 1987;Glorioso et al, 1984; IP: 34.215.51.103…”

Section: Introductionmentioning

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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Section: Introductionmentioning

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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“…Most of gE-tests use the principle of blocking ELISA based on one or two MAbs against gE (Eloit et al, 1988;Van Oirschot et al, 1988;Tonelli, 1991;Grom et al, 1992;Morenkov et al, 1997b). The high antigenic drift of gE (Ben-Porat et al, 1986;Mettenleiter et al, 1987;Katz and Pederson, 1992) and the variability of epitopespecific immune response to gE present a serious problem in the diagnostics of AD by such tests. Therefore, at present there is a need for a confirmation gE-test which should preferably be based on another principle and should be able to detect antibodies directed against many potential epitopes of gE.…”

Section: Discussionmentioning

confidence: 99%

“…The affinity-purified gE or recombinant proteins expressed in eukaryotic systems appear to be a better choice for such kind of assays. Binding gE-ELISAs are able to detect antibodies against many epitopes, which offers some advantages over blocking gE-ELISAs, especially if the antigenic drift of gE and the variability of epitope-specific immune responses to gE are taken into account (Ben-Porat et al, 1986;Mettenleiter et al, 1987;Katz and Pederson, 1992;). …”

Section: Discussionmentioning

confidence: 99%

“…The majority of gE-assays used in AD eradication programs detect antibodies against one or two epitopes of gE (Eloit et al, 1988;Van Oirschot et al, 1988;Tonelli, 1991;Grom et al, 1992;Morenkov et al, 1997b). However, it is well known that gE displays an antigenic drift, which may be due to the expression of the altered form of gE or mutations in antigenic determinants of gE (Ben-Porat et al, 1986;Mettenleiter et al, 1987;Katz and Pederson, 1992). Therefore, field ADV strains lacking several epitopes on gE may arise.…”

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confidence: 99%

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Indirect Elisas Based on Recombinant and Affinity-Purified Glycoprotein E of Aujeszky's Disease Virus to Differentiate Between Vaccinated and Infected Animals

Morenkov

Fodor

1999

Acta Veterinaria Hungarica

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Two indirect ELISAs for the detection of antibodies against glycoprotein E (gE) of Aujeszkys disease virus (ADV) in sera have been developed. The rec-gE-ELISA is based on the E. coli-expressed recombinant protein containing the Nterminal sequences of gE (aa 1-125) fused with the glutathione S-transferase from Schistosoma japonicum. The affi-gE-ELISA is based on native gE, which was purified from virions by affinity chromatography. The tests were optimised and compared with each other, as well as with the recently developed blocking gE-ELISA (Morenkov et al., 1997>), with respect to specificity and sensitivity. The recgE-ELISA was less sensitive in detecting ADV-infected animals than the affi-gE-ELISA (sensitivity 80% and 97%, respectively), which is probably due to the lack of conformation-dependent immunodominant epitopes on the recombinant protein expressed in E. coli. The specificity of the rec-gE-ELISA and affi-gE-ELISA was rather moderate (90% and 94%, respectively) because it was necessary to set such cut-off values in the tests that provided a maximum level of sensitivity, which obviously increased the incidence of false positive reactions. Though the indirect ELISAs detect antibodies against many epitopes of gE, the blocking gE-ELISA, which detects antibodies against only one immunodominant epitope of gE, showed a better test performance (specificity 99% and sensitivity 98%). This is most probably due to rather high dilutions of the sera used in the indirect gE-ELISAs (1:30) as compared to the serum dilution in the blocking gE-ELISA (1:2). We conclude that the indirect gE-ELISAs are sufficiently specific and sensitive to distinguish ADVinfected swine from those vaccinated with gE-negative vaccine and can be useful, in particularly affi-gE-ELISA, as additional tests for the detection of antibodies to gE.

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“…Being situated on the envelope surface of mature virus particles, glycoprotein C contains many antigen determinants, and can adequately induce the immune response (Ben-Porat et al, 1986;Guo et al, 1989;Tewari et al, 1995). In the DPV genome, the UL44 gene, which is conserved with the UL44 gene of other alphaherpesviruses (Allen and Coogle, 1988;Fitzpatrick et al, 1989;Nicolson and Onions, 1990), was identified and sequenced in our laboratory.…”

Section: Introductionmentioning

confidence: 99%

Bioinformatic analysis and characteristics of glycoprotein C encoded by the newly identified UL44 gene of duck plague virus

Sun¹,

Cheng²,

Wang³

2014

Genet. Mol. Res.

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ABSTRACT. Glycoprotein C is one of the duck plague virus (DPV) glycoproteins and is encoded by the DPV UL44 gene. DPV glycoprotein C (DPV-gC) comprises 431 amino acids with a putative molecular mass of 47.35 kDa. Sequence analysis indicated that the protein possesses typical characteristics of type-I membrane glycoproteins, containing an N-terminal signal sequence, an external domain, a C-terminal membrane anchor region, and a short cytoplasmic domain. Comparisons of 22 alphaherpesvirus-gC protein sequences revealed eight conservative Cys-residue sites, which may play a crucial role in the biological functions and structural stabilization of the DPV-gC protein. Estimates of potential antigenic epitopes and secondary structure identified four B cell dominant epitopes, which are located at amino acids 68-71, 87-91, 369-352, and 372-374. A model for the structure of DPV-gC was derived by associating its predicted secondary and three-dimensional structures. In conclusion, these results will provide a basis for further functional studies of DPV-gC, establishing novel clinical diagnoses of DPV, and in the development of a new DPV vaccine.

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Role of glycoproteins of pseudorabies virus in eliciting neutralizing antibodies

Cited by 116 publications

References 20 publications

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

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

Indirect Elisas Based on Recombinant and Affinity-Purified Glycoprotein E of Aujeszky's Disease Virus to Differentiate Between Vaccinated and Infected Animals

Bioinformatic analysis and characteristics of glycoprotein C encoded by the newly identified UL44 gene of duck plague virus

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