Identification and DNA Sequence Analysis of the Marek's Disease Virus Serotype 2 Gene Homologous to the Herpes Simplex Virus Type 1 Glycoprotein H.

Abstract

ABSTRACT. Marek's disease virus (MDV) serotype 2 (MDV2) gene homologous to the glycoprotein H (gH) gene of herpes simplex virus type 1 was identified and sequenced. The predicted region encoding for the MDV2 gH gene was 2436 nucleotide and the primary translation product was 812 amino acids with a molecular weight of 89.4 kDa. The protein encoded by MDV2 gH gene has a number of features characteristic of a membrane-associated glycoprotein. First, there are 9 potential N-linked glycosylation sites and 11 cysteine residues, and 6 of the sites and 8 of the residues were conserved among all of the three MDV serotypes. Second, this protein had Nterminal and C-terminal hydrophobic regions, which were a signal sequence and a transmembrane-anchor domain, respectively. From the northern blot analysis, it was suggested that a transcript encoding MDV2 gH and a poly-cistronic transcript encoding MDV2 thymidine kinase, gH, and possibly other genes of downstream on this strand existed. Alignment of the amino acid sequences of the gH homologues among the three MDV serotypes showed 57.5% (MDV1 and MDV2), 56.2% (MDV1 and HVT), and 50.1% (MDV2 and HVT) identities. [8,19,29]. Further, antibodies raised against gH homologues neutralize the infectivity of HSV-1, VZV and so on [7,18]. However, HSV-1 gH alone synthesized in a mammalian cell expression system or recombinant vaccinia virus-infected cells was slightly smaller than authentic HSV-1 gH and antigenically distinct from it, and not transported to the cell surface [6,10]. 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. Using polyclonal antiserum against MDV1 gL, gL coprecipitated with a molecular weight of 115 kDa which was predicted to be MDV1 gH from the size of the primary translational product. Further, MDV1 gL expressed alone was not properly processed to a mature form [41]. However, there is no evidence of the complex formation of gH and gL in MDV. Further it is unknown that the gH-gL complex is required

Identification and DNA Sequence Analysis of the Marek's Disease Virus Serotype 2 Genes Homologous to the Herpes Simplex Virus Type 1 UL20 and UL21

“…The 120 bp of 3' terminus of the MDV2 UL21 gene was previously reported [24]. To obtain the entire MDV2 UL21 gene and further upstream sequence of the MDV2 UL21 gene, a 3.1 kb ClaI-PstI subfragment from the EcoRI-E fragment ( Fig.…”

“…However, the restriction endonuclease digestion patterns vary among MDV1, MDV2, and HVT [10,21,26]. In MDV2 genome, genes encoding for glycoproteins gB [30], gC [15], gD [13], gE [12], gH [24], and gI [13], thymidine kinase and UL24 [25], and phosphoprotein pp38 [19] homologues have been identified and analyzed.…”

Mechanism of herpesvirus UL24 protein regulating viral immune escape and virulence

“…The proteins encoded by the HCMV UL76, VZV ORF35, KSHV ORF20 and EHV-1 ORF37 genes also belong to the herpesvirus UL24 protein family ( Bateman et al, 2004 ; Ito et al, 2005 ; Kasem et al, 2010 ; Hoffman et al, 2021 ). Except for the HCMV UL76 gene, the UL24 genes and TK genes of other herpesviruses are arranged in a head-to-head manner at the 5′ end ( Figure 1B ; Jacobson et al, 1989 ; Dezélée et al, 1996 ; Shimojima et al, 1997 ; Pearson and Coen, 2002 ; Ito et al, 2005 ; Li et al, 2006 ).…”

Identification and Structure of the Marek's Disease Virus Serotype 2 Glycoprotein M Gene: Comparison with Glycoprotein M Genes of Herpesviridae Family

“…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.…”