1993
DOI: 10.1099/0022-1317-74-6-1185
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Identification and sequence analysis of the homologues of the herpes simplex virus type 1 glycoprotein H in Marek's disease virus and the herpesvirus of turkeys

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Cited by 23 publications
(14 citation statements)
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“…In all human and animal herpesviruses studied to date, homologs of glycoprotein H (gH) and glycoprotein L (gL) have been found (9,14,15,17,18,21,22,26,32,34,35,40,41,43,44). These two envelope glycoproteins, which associate to form a gH-gL complex, have been implicated as key participants in fusion events that are critical to herpesvirus infection.…”
mentioning
confidence: 99%
“…In all human and animal herpesviruses studied to date, homologs of glycoprotein H (gH) and glycoprotein L (gL) have been found (9,14,15,17,18,21,22,26,32,34,35,40,41,43,44). These two envelope glycoproteins, which associate to form a gH-gL complex, have been implicated as key participants in fusion events that are critical to herpesvirus infection.…”
mentioning
confidence: 99%
“…The gH homologous genes are conserved downstream of the thymidine kinase (TK) homologous genes in various herpesviruses [8,21,25] including MDV1 and HVT [35]. As shown in Fig.…”
Section: Identification and Sequencing Of The Mdv2 Gh Genementioning
confidence: 99%
“…Because HSV-1 gH required glycoprotein L (gL) for proper posttranslational processing and transport to the cell surface [13]. Similarly, gH and gL associations have also been described in VZV [5], pseudorabies virus (PRV) [22], and equine herpesvirus type 1 (EHV-1) [38].In MDV1 and HVT genomes, the potential open reading frames (ORFs) which are homologous to the HSV-1 gH gene were reported [35]. The predicted primary polypeptide products of the MDV1 gH and HVT gH ORFs were 813 and 808 amino acids, respectively.…”
mentioning
confidence: 99%
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“…In MDV genomes, eight glycoproteins, designated gB [33,45], gC [9,20], gD [7,17,48], gE [7,16,48], gH [36,38], gI [7,18,48], gK [32,43], and gL [47] have been found. Amino acid sequence analysis characterizes most of these proteins as type I membrane proteins, comprising an aminoterminal hydrophobic region as a putative signal sequence and a carboxy-terminal hydrophobic region as a transmembrane domain resulting in location of most of the amino-terminal part of the protein on the outside of the membrane.…”
mentioning
confidence: 99%