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David Meredith - One of the best experts on this subject based on the ideXlab platform.

  • antigenic and protein sequence homology between vp13 14 a herpes simplex virus type 1 tegument protein and gp10 a glycoprotein of Equine Herpesvirus 1 and 4
    Journal of Virology, 1991
    Co-Authors: Gary R Whittaker, George P. Allen, M P Riggio, Ian W Halliburton, R A Killington, David Meredith
    Abstract:

    Monospecific polyclonal antisera raised against VP13/14, a major tegument protein of herpes simplex virus type 1 cross-reacted with structural Equine Herpesvirus 1 and 4 proteins of Mr 120,000 and 123,000, respectively; these proteins are identical in molecular weight to the corresponding glycoprotein 10 (gp10) of each virus. Using a combination of immune precipitation and Western immunoblotting techniques, we confirmed that anti-VP13/14 and a monoclonal antibody to gp10 reacted with the same protein. Sequence analysis of a lambda gt11 insert of Equine Herpesvirus 1 gp10 identified an open reading frame in Equine Herpesvirus 4 with which it showed strong homology; this open reading frame also shared homology with gene UL47 of herpes simplex virus type 1 and gene 11 of varicella-zoster virus. This showed that, in addition to immunological cross-reactivity, VP13/14 and gp10 have protein sequence homology; it also allowed identification of VP13/14 as the gene product of UL47.

  • Antigenic and protein sequence homology between VP13/14, a herpes simplex virus type 1 tegument protein, and gp10, a glycoprotein of Equine Herpesvirus 1 and 4.
    Journal of virology, 1991
    Co-Authors: Gary R Whittaker, George P. Allen, M P Riggio, Ian W Halliburton, R A Killington, David Meredith
    Abstract:

    Monospecific polyclonal antisera raised against VP13/14, a major tegument protein of herpes simplex virus type 1 cross-reacted with structural Equine Herpesvirus 1 and 4 proteins of Mr 120,000 and 123,000, respectively; these proteins are identical in molecular weight to the corresponding glycoprotein 10 (gp10) of each virus. Using a combination of immune precipitation and Western immunoblotting techniques, we confirmed that anti-VP13/14 and a monoclonal antibody to gp10 reacted with the same protein. Sequence analysis of a lambda gt11 insert of Equine Herpesvirus 1 gp10 identified an open reading frame in Equine Herpesvirus 4 with which it showed strong homology; this open reading frame also shared homology with gene UL47 of herpes simplex virus type 1 and gene 11 of varicella-zoster virus. This showed that, in addition to immunological cross-reactivity, VP13/14 and gp10 have protein sequence homology; it also allowed identification of VP13/14 as the gene product of UL47.

Gary R Whittaker - One of the best experts on this subject based on the ideXlab platform.

  • antigenic and protein sequence homology between vp13 14 a herpes simplex virus type 1 tegument protein and gp10 a glycoprotein of Equine Herpesvirus 1 and 4
    Journal of Virology, 1991
    Co-Authors: Gary R Whittaker, George P. Allen, M P Riggio, Ian W Halliburton, R A Killington, David Meredith
    Abstract:

    Monospecific polyclonal antisera raised against VP13/14, a major tegument protein of herpes simplex virus type 1 cross-reacted with structural Equine Herpesvirus 1 and 4 proteins of Mr 120,000 and 123,000, respectively; these proteins are identical in molecular weight to the corresponding glycoprotein 10 (gp10) of each virus. Using a combination of immune precipitation and Western immunoblotting techniques, we confirmed that anti-VP13/14 and a monoclonal antibody to gp10 reacted with the same protein. Sequence analysis of a lambda gt11 insert of Equine Herpesvirus 1 gp10 identified an open reading frame in Equine Herpesvirus 4 with which it showed strong homology; this open reading frame also shared homology with gene UL47 of herpes simplex virus type 1 and gene 11 of varicella-zoster virus. This showed that, in addition to immunological cross-reactivity, VP13/14 and gp10 have protein sequence homology; it also allowed identification of VP13/14 as the gene product of UL47.

  • Antigenic and protein sequence homology between VP13/14, a herpes simplex virus type 1 tegument protein, and gp10, a glycoprotein of Equine Herpesvirus 1 and 4.
    Journal of virology, 1991
    Co-Authors: Gary R Whittaker, George P. Allen, M P Riggio, Ian W Halliburton, R A Killington, David Meredith
    Abstract:

    Monospecific polyclonal antisera raised against VP13/14, a major tegument protein of herpes simplex virus type 1 cross-reacted with structural Equine Herpesvirus 1 and 4 proteins of Mr 120,000 and 123,000, respectively; these proteins are identical in molecular weight to the corresponding glycoprotein 10 (gp10) of each virus. Using a combination of immune precipitation and Western immunoblotting techniques, we confirmed that anti-VP13/14 and a monoclonal antibody to gp10 reacted with the same protein. Sequence analysis of a lambda gt11 insert of Equine Herpesvirus 1 gp10 identified an open reading frame in Equine Herpesvirus 4 with which it showed strong homology; this open reading frame also shared homology with gene UL47 of herpes simplex virus type 1 and gene 11 of varicella-zoster virus. This showed that, in addition to immunological cross-reactivity, VP13/14 and gp10 have protein sequence homology; it also allowed identification of VP13/14 as the gene product of UL47.

George P. Allen - One of the best experts on this subject based on the ideXlab platform.

  • Risk factors for development of neurologic disease after experimental exposure to Equine Herpesvirus-1 in horses.
    American journal of veterinary research, 2008
    Co-Authors: George P. Allen
    Abstract:

    Objective—To identify risk factors associated with development of clinical neurologic signs in horses exposed to Equine Herpesvirus-1 (EHV-1). Animals—36 adult horses. Procedures—Blood samples collected before and after challenge inoculation with nonneuropathogenic or neuropathogenic EHV-1 were analyzed for leukocyte-associated viremia, serum neutralizing antibody, and EHV-1–specific cytotoxic T-lymphocyte precursors (CTLPs). Associations between variables and neurologic disease and correlations between age category or breed and development of neurologic disease were examined. Results—9 horses developed CNS signs (ataxia, hind limb paresis or paralysis, bladder atony, or recumbency). Neurologic deficits were correlated with infection by a neuropathogenic strain of EHV-1, age > 20 years, high postexposure viremic load, and low preexposure concentration of CTLPs. No significant correlations were observed between preinfection titers or horse breed and postinfection development of neurologic signs. Conclusion...

  • Antemortem detection of latent infection with neuropathogenic strains of Equine Herpesvirus-1 in horses.
    American journal of veterinary research, 2006
    Co-Authors: George P. Allen
    Abstract:

    Objective—To evaluate a technique for identifying horses latently infected with neuropathogenic strains of Equine Herpesvirus-1 (EHV-1). Animals—36 adult mares, 24 of which were experimentally infected as weanlings with neuropathogenic or nonneuropathogenic EHV-1. Procedures—Mandibular lymph node (MLN) tissue was obtained from each horse via biopsy during general anesthesia. Purified DNA from MLNs was tested for EHV-1 DNA by use of a magnetic bead, sequencecapture, nested PCR assay. For MLNs that contained EHV-1 DNA, the 256-bp DNA fragments amplified via sequence-capture nested PCR were sequenced to determine the nucleotide at the polymorphic site that determines pathotype (ie, neuropathotype [G2254] or non-neuropathotype [A2254]). Results—Latent viral DNA was detected in 26 of the 36 (72%) mares tested. Neuropathogenic and nonneuropathogenic EHV-1 genotypes were detected in the latently infected horses. In each mare previously infected with known EHV-1 pathotypes, the open reading frame 30 genotype of l...

  • antigenic and protein sequence homology between vp13 14 a herpes simplex virus type 1 tegument protein and gp10 a glycoprotein of Equine Herpesvirus 1 and 4
    Journal of Virology, 1991
    Co-Authors: Gary R Whittaker, George P. Allen, M P Riggio, Ian W Halliburton, R A Killington, David Meredith
    Abstract:

    Monospecific polyclonal antisera raised against VP13/14, a major tegument protein of herpes simplex virus type 1 cross-reacted with structural Equine Herpesvirus 1 and 4 proteins of Mr 120,000 and 123,000, respectively; these proteins are identical in molecular weight to the corresponding glycoprotein 10 (gp10) of each virus. Using a combination of immune precipitation and Western immunoblotting techniques, we confirmed that anti-VP13/14 and a monoclonal antibody to gp10 reacted with the same protein. Sequence analysis of a lambda gt11 insert of Equine Herpesvirus 1 gp10 identified an open reading frame in Equine Herpesvirus 4 with which it showed strong homology; this open reading frame also shared homology with gene UL47 of herpes simplex virus type 1 and gene 11 of varicella-zoster virus. This showed that, in addition to immunological cross-reactivity, VP13/14 and gp10 have protein sequence homology; it also allowed identification of VP13/14 as the gene product of UL47.

  • Antigenic and protein sequence homology between VP13/14, a herpes simplex virus type 1 tegument protein, and gp10, a glycoprotein of Equine Herpesvirus 1 and 4.
    Journal of virology, 1991
    Co-Authors: Gary R Whittaker, George P. Allen, M P Riggio, Ian W Halliburton, R A Killington, David Meredith
    Abstract:

    Monospecific polyclonal antisera raised against VP13/14, a major tegument protein of herpes simplex virus type 1 cross-reacted with structural Equine Herpesvirus 1 and 4 proteins of Mr 120,000 and 123,000, respectively; these proteins are identical in molecular weight to the corresponding glycoprotein 10 (gp10) of each virus. Using a combination of immune precipitation and Western immunoblotting techniques, we confirmed that anti-VP13/14 and a monoclonal antibody to gp10 reacted with the same protein. Sequence analysis of a lambda gt11 insert of Equine Herpesvirus 1 gp10 identified an open reading frame in Equine Herpesvirus 4 with which it showed strong homology; this open reading frame also shared homology with gene UL47 of herpes simplex virus type 1 and gene 11 of varicella-zoster virus. This showed that, in addition to immunological cross-reactivity, VP13/14 and gp10 have protein sequence homology; it also allowed identification of VP13/14 as the gene product of UL47.

J M Whalley - One of the best experts on this subject based on the ideXlab platform.

  • Inoculation with DNA encoding the glycoprotein gp2 reduces severity of Equine Herpesvirus 1 infection in a mouse respiratory model.
    Archives of virology, 2003
    Co-Authors: G. S. Learmonth, J. E. Wellington, D N Love, James R. Gilkerson, J M Whalley
    Abstract:

    The envelope glycoprotein 2 (gp2) of Equine Herpesvirus 1 (EHV-1) has no known homologue in other Herpesviruses with the exception of some equid alphaHerpesviruses. In order to investigate the potential of gp2 as a vaccine antigen, expression vectors were constructed to encode full-length gp2, a truncated version lacking the membrane anchor, and the C-terminal region. Intramuscular inoculation of mice with these DNA constructs induced neutralizing antibody against EHV-1 and, following intranasal challenge with EHV-1, mice inoculated with any of the gp2 DNA constructs cleared virus more rapidly from their lungs than control mice. The rate of clearance was comparable to that for glycoprotein D DNA, indicating gp2 as a potential antigen for inclusion in a subunit vaccine.

  • Potential of DNA-mediated vaccination for Equine Herpesvirus 1.
    Veterinary microbiology, 1999
    Co-Authors: K M Ruitenberg, J. E. Wellington, C Walker, D N Love, J M Whalley
    Abstract:

    The potential of DNA-mediated immunisation to protect against Equine Herpesvirus 1 (EHV-1) disease was assessed in a murine model of EHV-1 respiratory infection. Intramuscular injection with DNA encoding the EHV-1 envelope glycoprotein D (gD) in a mammalian expression vector induced a specific antibody response detectable by two weeks and maintained through 23 weeks post injection. Immune responses were proportional to the dose of DNA and a second injection markedly enhanced the antibody response. EHV-1 gD DNA-injected mice developed neutralising antibodies, and a predominance of IgG2a antibodies after the DNA injection was consistent with the generation of a type 1 helper T-cell (Th1) response. Following intranasal challenge with EHV-1, mice immunised with 50 microg of EHV-1 gD DNA were able to clear virus more rapidly from lung tissue and showed reduced lung pathology in comparison with control mice. The data indicate that DNA-mediated immunisation may be a useful strategy for vaccination against EHV-1.

  • Characteristics of glycoprotein B of Equine Herpesvirus 1 expressed by a recombinant baculovirus.
    Veterinary microbiology, 1999
    Co-Authors: K I Munro, J. E. Wellington, D N Love, J M Whalley
    Abstract:

    A recombinant baculovirus (Bac-EgB) containing the complete open reading frame of Equine Herpesvirus 1 glycoprotein B (EHV-1 gB) expressed recombinant products of 107-133 kDa, 58-75 kDa and 53-57 kDa, corresponding to EHV-1 gB precursor, large and small subunits respectively. High molecular mass products (>200 kDa) in the Bac-EgB infected insect cells were consistent with oligomerisation of the recombinant EHV-1 gB products, and analysis with tunicamycin and endoglycosidases indicated that the baculovirus-expressed gB contained N-linked sugars with high mannose and hybrid chains. N-terminal amino acid sequence analysis of the gB forms revealed identical signal and endoproteolytic cleavage sites to those of gB in EHV-1 infected mammalian cells, and authenticity of processing and transport was supported by the presence of EHV-1 gB antigen at the surface of infected insect cells. Immunogold labelling and electron microscopy of recombinant baculovirus particles indicated that the recombinant gB was also present in baculovirus envelopes. Bac-EgB infected insect cells were able to induce low levels of complement dependent virus neutralising antibody, and have been shown to evoke protective immune responses in murine models of respiratory disease and abortion.

  • The detection of latency-associated transcripts of Equine Herpesvirus 1 in ganglionic neurons.
    Journal of General Virology, 1995
    Co-Authors: M. K. Baxi, Glenda Lawrence, J M Whalley, Stacey Efstathiou, J. D. Slater, Hugh J. Field
    Abstract:

    Neural tissues from specific pathogen-free ponies that had been experimentally infected with Equine Herpesvirus 1 (EHV-1) were analysed by in situ hybridization. Digoxigenin-labelled EHV-1 BamHI fragments spanning almost the entire EHV-1 genome were hybridized to RNA in tissue sections from latently infected trigeminal ganglia. The BamHI E fragment detected EHV-1 RNA antisense to gene 63 (HSV-1 homologue ICP0) in a small number of neurons. Sixteen other BamHI fragments gave negative results in 20 sections tested with each fragment. Latency associated transcripts (LATs) were localized to the neuronal nuclei. EHV-1 nucleotide sequence data in the region reveals the presence of a putative EHV-1 LAT promoter that shares similar motifs with the HSV-1 LAT promoter, including the LAT promoter-binding factor, and may have a role in EHV-1 LAT expression.

  • Immunization with glycoprotein C of Equine Herpesvirus-1 is associated with accelerated virus clearance in a murine model
    Archives of Virology, 1995
    Co-Authors: Deepanker Tewari, H J Field, D N Love, S. V. Nair, M. C. Ungria, G. L. Lawrence, M. Hayden, J M Whalley
    Abstract:

    The glycoprotein C (gC) gene of Equine Herpesvirus-1 (EHV-1) was expressed in insect cells by a recombinant baculovirus as several products with apparent molecular weights of 66 kDa–80 kDa. The baculovirus EHV-1 gC products were recognised by monoclonal antibody and by EHV-1 convalescent Equine sera, indicating conservation of antigenic determinants and confirming this glycoprotein as a target for the Equine immune system. Mice immunized with recombinant EHV-1 gC showed accelerated clearance of EHV-1 from respiratory tissues following intranasal challenge. Virus clearance was accompanied by virus specific antibodies and by cell mediated immune responses measured by a delayed type hypersensitivity reaction and lymphocyte stimulation by killed EHV-1 as antigen.

M P Riggio - One of the best experts on this subject based on the ideXlab platform.

  • antigenic and protein sequence homology between vp13 14 a herpes simplex virus type 1 tegument protein and gp10 a glycoprotein of Equine Herpesvirus 1 and 4
    Journal of Virology, 1991
    Co-Authors: Gary R Whittaker, George P. Allen, M P Riggio, Ian W Halliburton, R A Killington, David Meredith
    Abstract:

    Monospecific polyclonal antisera raised against VP13/14, a major tegument protein of herpes simplex virus type 1 cross-reacted with structural Equine Herpesvirus 1 and 4 proteins of Mr 120,000 and 123,000, respectively; these proteins are identical in molecular weight to the corresponding glycoprotein 10 (gp10) of each virus. Using a combination of immune precipitation and Western immunoblotting techniques, we confirmed that anti-VP13/14 and a monoclonal antibody to gp10 reacted with the same protein. Sequence analysis of a lambda gt11 insert of Equine Herpesvirus 1 gp10 identified an open reading frame in Equine Herpesvirus 4 with which it showed strong homology; this open reading frame also shared homology with gene UL47 of herpes simplex virus type 1 and gene 11 of varicella-zoster virus. This showed that, in addition to immunological cross-reactivity, VP13/14 and gp10 have protein sequence homology; it also allowed identification of VP13/14 as the gene product of UL47.

  • Antigenic and protein sequence homology between VP13/14, a herpes simplex virus type 1 tegument protein, and gp10, a glycoprotein of Equine Herpesvirus 1 and 4.
    Journal of virology, 1991
    Co-Authors: Gary R Whittaker, George P. Allen, M P Riggio, Ian W Halliburton, R A Killington, David Meredith
    Abstract:

    Monospecific polyclonal antisera raised against VP13/14, a major tegument protein of herpes simplex virus type 1 cross-reacted with structural Equine Herpesvirus 1 and 4 proteins of Mr 120,000 and 123,000, respectively; these proteins are identical in molecular weight to the corresponding glycoprotein 10 (gp10) of each virus. Using a combination of immune precipitation and Western immunoblotting techniques, we confirmed that anti-VP13/14 and a monoclonal antibody to gp10 reacted with the same protein. Sequence analysis of a lambda gt11 insert of Equine Herpesvirus 1 gp10 identified an open reading frame in Equine Herpesvirus 4 with which it showed strong homology; this open reading frame also shared homology with gene UL47 of herpes simplex virus type 1 and gene 11 of varicella-zoster virus. This showed that, in addition to immunological cross-reactivity, VP13/14 and gp10 have protein sequence homology; it also allowed identification of VP13/14 as the gene product of UL47.