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http://purl.uniprot.org/citations/2455821http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2455821http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2455821http://www.w3.org/2000/01/rdf-schema#comment"The molecular structure of the equine herpesvirus type 1 (EHV-1) gene encoding glycoprotein 13 (gp13) was analyzed. The gene is contained within a 1.8-kilobase AccI-EcoRI restriction fragment mapping at map coordinates 0.136 to 0.148 in the UL region of the EHV-1 genome and is transcribed from right to left. Determination of the nucleotide sequence of the DNA fragment revealed a complete transcriptional unit composed of typical regulatory promoter elements upstream to a long open reading frame (1,404 base pairs) that encoded a 468-amino-acid primary translation product of 51 kilodaltons. The predicted protein has the characteristic features of a membrane-spanning protein: an N-terminal signal sequence, a hydrophobic membrane anchor region, a charged C-terminal cytoplasmic tail, and an exterior domain with nine potential N-glycosylation sites. The EHV-1 DNA sequences expressed in lambda gt11 as gp13 epitopes were present in the open reading frame. Amino acid sequences composing a major antigenic site, recognized by 35% of a panel of 42 anti-gp13 monoclonal antibodies, were identified in the N-terminal surface domain of the deduced gp13 molecule. Comparison of the EHV-1 gp13 DNA sequence with that encoding glycoproteins of other alphaherpesviruses revealed no detectable homology. However, a search for homology at the amino acid level showed regions of significant sequence similarity between the amino acids of the carboxy half of EHV-1 gp13 and those of the same region of gC-like glycoproteins of herpes simplex virus (gC-1 and gC-2), pseudorabies herpesvirus (gIII), and varicella-zoster virus (gp66). The sequences of the N-terminal portion of gp13, by contrast, were much less conserved. The results of these studies indicate that EHV-1 gp13 is the structural homolog of herpes simplex virus glycoprotein C and further suggest that the epitope-containing N-terminal amino acid sequences of the herpesvirus gC-like glycoproteins have undergone more extensive evolutionary divergence than the C-terminal sequences."xsd:string
http://purl.uniprot.org/citations/2455821http://purl.org/dc/terms/identifier"doi:10.1128/jvi.62.8.2850-2858.1988"xsd:string
http://purl.uniprot.org/citations/2455821http://purl.org/dc/terms/identifier"doi:10.1128/jvi.62.8.2850-2858.1988"xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/author"Allen G.P."xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/author"Allen G.P."xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/author"Coogle L.D."xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/author"Coogle L.D."xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/pages"2850-2858"xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/pages"2850-2858"xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/title"Characterization of an equine herpesvirus type 1 gene encoding a glycoprotein (gp13) with homology to herpes simplex virus glycoprotein C."xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/title"Characterization of an equine herpesvirus type 1 gene encoding a glycoprotein (gp13) with homology to herpes simplex virus glycoprotein C."xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/volume"62"xsd:string
http://purl.uniprot.org/citations/2455821http://purl.uniprot.org/core/volume"62"xsd:string
http://purl.uniprot.org/citations/2455821http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2455821
http://purl.uniprot.org/citations/2455821http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2455821
http://purl.uniprot.org/citations/2455821http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2455821
http://purl.uniprot.org/citations/2455821http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2455821
http://purl.uniprot.org/uniprot/P68325http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/2455821
http://purl.uniprot.org/uniprot/#_P68325-citation-2455821http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/2455821